La maladie de Parkinson en France (serveur d'exploration)

Attention, ce site est en cours de développement !
Attention, site généré par des moyens informatiques à partir de corpus bruts.
Les informations ne sont donc pas validées.

Structural and functional domains of E coli initiation factor IF2

Identifieur interne : 000F57 ( Istex/Corpus ); précédent : 000F56; suivant : 000F58

Structural and functional domains of E coli initiation factor IF2

Auteurs : S. Laalami ; C. Sacerdot ; G. Vachon ; K. Mortensen ; H. U. Sperling-Petersen ; Y. Cenatiempo ; M. Grunberg-Manago

Source :

RBID : ISTEX:6EB34AF27D0525F2BA115036672D32A805678944

Abstract

Initiation of translation in prokaryotes requires the participation of at least three soluble proteins: the initiation factors IF1, IF2 and IF3. Initiation factor 2, which is one of the largest proteins involved in translation (97.3 kDa) has been shown to stimulate in vitro the binding of fMet-tRNAfMet to the 30S ribosomal subunit. After formation of 70S translation intiation complex, IF2 is believed to participate in GTP hydrolysis, thereby promoting its own release. Here we review evidence which indicates the functional importance of the different structural domains of IF2, emphasizing new information obtained by in vivo experiments.

Url:
DOI: 10.1016/0300-9084(91)90191-3

Links to Exploration step

ISTEX:6EB34AF27D0525F2BA115036672D32A805678944

Le document en format XML

<record>
<TEI wicri:istexFullTextTei="biblStruct">
<teiHeader>
<fileDesc>
<titleStmt>
<title>Structural and functional domains of E coli initiation factor IF2</title>
<author>
<name sortKey="Laalami, S" sort="Laalami, S" uniqKey="Laalami S" first="S." last="Laalami">S. Laalami</name>
<affiliation>
<mods:affiliation>Institut de Biologie Physico-Chimique, 13 rue Pierre et Marie Curie, 75005 Paris, France</mods:affiliation>
</affiliation>
</author>
<author>
<name sortKey="Sacerdot, C" sort="Sacerdot, C" uniqKey="Sacerdot C" first="C." last="Sacerdot">C. Sacerdot</name>
<affiliation>
<mods:affiliation>Institut de Biologie Physico-Chimique, 13 rue Pierre et Marie Curie, 75005 Paris, France</mods:affiliation>
</affiliation>
</author>
<author>
<name sortKey="Vachon, G" sort="Vachon, G" uniqKey="Vachon G" first="G." last="Vachon">G. Vachon</name>
<affiliation>
<mods:affiliation>Laboratoire de Biologie Moléculaire, URA CNRS 1172, Université de Poitiers, 40, avenue du Recteur Pineau, 86022 PoitiersCedex, France</mods:affiliation>
</affiliation>
</author>
<author>
<name sortKey="Mortensen, K" sort="Mortensen, K" uniqKey="Mortensen K" first="K." last="Mortensen">K. Mortensen</name>
<affiliation>
<mods:affiliation>Laboratory of Biodesign, Department of Chemistry, Aarhus University, DK-8000 Aarhus, Denmark</mods:affiliation>
</affiliation>
</author>
<author>
<name sortKey="Sperling Petersen, H U" sort="Sperling Petersen, H U" uniqKey="Sperling Petersen H" first="H. U." last="Sperling-Petersen">H. U. Sperling-Petersen</name>
<affiliation>
<mods:affiliation>Laboratory of Biodesign, Department of Chemistry, Aarhus University, DK-8000 Aarhus, Denmark</mods:affiliation>
</affiliation>
</author>
<author>
<name sortKey="Cenatiempo, Y" sort="Cenatiempo, Y" uniqKey="Cenatiempo Y" first="Y." last="Cenatiempo">Y. Cenatiempo</name>
<affiliation>
<mods:affiliation>Laboratoire de Biologie Moléculaire, URA CNRS 1172, Université de Poitiers, 40, avenue du Recteur Pineau, 86022 PoitiersCedex, France</mods:affiliation>
</affiliation>
</author>
<author>
<name sortKey="Grunberg Manago, M" sort="Grunberg Manago, M" uniqKey="Grunberg Manago M" first="M." last="Grunberg-Manago">M. Grunberg-Manago</name>
<affiliation>
<mods:affiliation>Correspondence and reprints</mods:affiliation>
</affiliation>
<affiliation>
<mods:affiliation>Institut de Biologie Physico-Chimique, 13 rue Pierre et Marie Curie, 75005 Paris, France</mods:affiliation>
</affiliation>
</author>
</titleStmt>
<publicationStmt>
<idno type="wicri:source">ISTEX</idno>
<idno type="RBID">ISTEX:6EB34AF27D0525F2BA115036672D32A805678944</idno>
<date when="1991" year="1991">1991</date>
<idno type="doi">10.1016/0300-9084(91)90191-3</idno>
<idno type="url">https://api.istex.fr/document/6EB34AF27D0525F2BA115036672D32A805678944/fulltext/pdf</idno>
<idno type="wicri:Area/Istex/Corpus">000F57</idno>
<idno type="wicri:explorRef" wicri:stream="Istex" wicri:step="Corpus" wicri:corpus="ISTEX">000F57</idno>
</publicationStmt>
<sourceDesc>
<biblStruct>
<analytic>
<title level="a">Structural and functional domains of E coli initiation factor IF2</title>
<author>
<name sortKey="Laalami, S" sort="Laalami, S" uniqKey="Laalami S" first="S." last="Laalami">S. Laalami</name>
<affiliation>
<mods:affiliation>Institut de Biologie Physico-Chimique, 13 rue Pierre et Marie Curie, 75005 Paris, France</mods:affiliation>
</affiliation>
</author>
<author>
<name sortKey="Sacerdot, C" sort="Sacerdot, C" uniqKey="Sacerdot C" first="C." last="Sacerdot">C. Sacerdot</name>
<affiliation>
<mods:affiliation>Institut de Biologie Physico-Chimique, 13 rue Pierre et Marie Curie, 75005 Paris, France</mods:affiliation>
</affiliation>
</author>
<author>
<name sortKey="Vachon, G" sort="Vachon, G" uniqKey="Vachon G" first="G." last="Vachon">G. Vachon</name>
<affiliation>
<mods:affiliation>Laboratoire de Biologie Moléculaire, URA CNRS 1172, Université de Poitiers, 40, avenue du Recteur Pineau, 86022 PoitiersCedex, France</mods:affiliation>
</affiliation>
</author>
<author>
<name sortKey="Mortensen, K" sort="Mortensen, K" uniqKey="Mortensen K" first="K." last="Mortensen">K. Mortensen</name>
<affiliation>
<mods:affiliation>Laboratory of Biodesign, Department of Chemistry, Aarhus University, DK-8000 Aarhus, Denmark</mods:affiliation>
</affiliation>
</author>
<author>
<name sortKey="Sperling Petersen, H U" sort="Sperling Petersen, H U" uniqKey="Sperling Petersen H" first="H. U." last="Sperling-Petersen">H. U. Sperling-Petersen</name>
<affiliation>
<mods:affiliation>Laboratory of Biodesign, Department of Chemistry, Aarhus University, DK-8000 Aarhus, Denmark</mods:affiliation>
</affiliation>
</author>
<author>
<name sortKey="Cenatiempo, Y" sort="Cenatiempo, Y" uniqKey="Cenatiempo Y" first="Y." last="Cenatiempo">Y. Cenatiempo</name>
<affiliation>
<mods:affiliation>Laboratoire de Biologie Moléculaire, URA CNRS 1172, Université de Poitiers, 40, avenue du Recteur Pineau, 86022 PoitiersCedex, France</mods:affiliation>
</affiliation>
</author>
<author>
<name sortKey="Grunberg Manago, M" sort="Grunberg Manago, M" uniqKey="Grunberg Manago M" first="M." last="Grunberg-Manago">M. Grunberg-Manago</name>
<affiliation>
<mods:affiliation>Correspondence and reprints</mods:affiliation>
</affiliation>
<affiliation>
<mods:affiliation>Institut de Biologie Physico-Chimique, 13 rue Pierre et Marie Curie, 75005 Paris, France</mods:affiliation>
</affiliation>
</author>
</analytic>
<monogr></monogr>
<series>
<title level="j">Biochimie</title>
<title level="j" type="abbrev">BIOCHI</title>
<idno type="ISSN">0300-9084</idno>
<imprint>
<publisher>ELSEVIER</publisher>
<date type="published" when="1991">1991</date>
<biblScope unit="volume">73</biblScope>
<biblScope unit="issue">12</biblScope>
<biblScope unit="page" from="1557">1557</biblScope>
<biblScope unit="page" to="1566">1566</biblScope>
</imprint>
<idno type="ISSN">0300-9084</idno>
</series>
<idno type="istex">6EB34AF27D0525F2BA115036672D32A805678944</idno>
<idno type="DOI">10.1016/0300-9084(91)90191-3</idno>
<idno type="PII">0300-9084(91)90191-3</idno>
</biblStruct>
</sourceDesc>
<seriesStmt>
<idno type="ISSN">0300-9084</idno>
</seriesStmt>
</fileDesc>
<profileDesc>
<textClass></textClass>
<langUsage>
<language ident="en">en</language>
</langUsage>
</profileDesc>
</teiHeader>
<front>
<div type="abstract" xml:lang="en">Initiation of translation in prokaryotes requires the participation of at least three soluble proteins: the initiation factors IF1, IF2 and IF3. Initiation factor 2, which is one of the largest proteins involved in translation (97.3 kDa) has been shown to stimulate in vitro the binding of fMet-tRNAfMet to the 30S ribosomal subunit. After formation of 70S translation intiation complex, IF2 is believed to participate in GTP hydrolysis, thereby promoting its own release. Here we review evidence which indicates the functional importance of the different structural domains of IF2, emphasizing new information obtained by in vivo experiments.</div>
</front>
</TEI>
<istex>
<corpusName>elsevier</corpusName>
<author>
<json:item>
<name>S. Laalami</name>
<affiliations>
<json:string>Institut de Biologie Physico-Chimique, 13 rue Pierre et Marie Curie, 75005 Paris, France</json:string>
</affiliations>
</json:item>
<json:item>
<name>C. Sacerdot</name>
<affiliations>
<json:string>Institut de Biologie Physico-Chimique, 13 rue Pierre et Marie Curie, 75005 Paris, France</json:string>
</affiliations>
</json:item>
<json:item>
<name>G. Vachon</name>
<affiliations>
<json:string>Laboratoire de Biologie Moléculaire, URA CNRS 1172, Université de Poitiers, 40, avenue du Recteur Pineau, 86022 PoitiersCedex, France</json:string>
</affiliations>
</json:item>
<json:item>
<name>K. Mortensen</name>
<affiliations>
<json:string>Laboratory of Biodesign, Department of Chemistry, Aarhus University, DK-8000 Aarhus, Denmark</json:string>
</affiliations>
</json:item>
<json:item>
<name>H.U. Sperling-Petersen</name>
<affiliations>
<json:string>Laboratory of Biodesign, Department of Chemistry, Aarhus University, DK-8000 Aarhus, Denmark</json:string>
</affiliations>
</json:item>
<json:item>
<name>Y. Cenatiempo</name>
<affiliations>
<json:string>Laboratoire de Biologie Moléculaire, URA CNRS 1172, Université de Poitiers, 40, avenue du Recteur Pineau, 86022 PoitiersCedex, France</json:string>
</affiliations>
</json:item>
<json:item>
<name>M. Grunberg-Manago</name>
<affiliations>
<json:string>Correspondence and reprints</json:string>
<json:string>Institut de Biologie Physico-Chimique, 13 rue Pierre et Marie Curie, 75005 Paris, France</json:string>
</affiliations>
</json:item>
</author>
<subject>
<json:item>
<lang>
<json:string>eng</json:string>
</lang>
<value>translation initiation factor 2</value>
</json:item>
<json:item>
<lang>
<json:string>eng</json:string>
</lang>
<value>IF2α and IF2β</value>
</json:item>
<json:item>
<lang>
<json:string>eng</json:string>
</lang>
<value>G binding protein</value>
</json:item>
<json:item>
<lang>
<json:string>eng</json:string>
</lang>
<value>G domain</value>
</json:item>
</subject>
<language>
<json:string>eng</json:string>
</language>
<originalGenre>
<json:string>Full-length article</json:string>
</originalGenre>
<abstract>Initiation of translation in prokaryotes requires the participation of at least three soluble proteins: the initiation factors IF1, IF2 and IF3. Initiation factor 2, which is one of the largest proteins involved in translation (97.3 kDa) has been shown to stimulate in vitro the binding of fMet-tRNAfMet to the 30S ribosomal subunit. After formation of 70S translation intiation complex, IF2 is believed to participate in GTP hydrolysis, thereby promoting its own release. Here we review evidence which indicates the functional importance of the different structural domains of IF2, emphasizing new information obtained by in vivo experiments.</abstract>
<qualityIndicators>
<score>6.152</score>
<pdfVersion>1.2</pdfVersion>
<pdfPageSize>605 x 764 pts</pdfPageSize>
<refBibsNative>true</refBibsNative>
<keywordCount>4</keywordCount>
<abstractCharCount>643</abstractCharCount>
<pdfWordCount>6361</pdfWordCount>
<pdfCharCount>36714</pdfCharCount>
<pdfPageCount>10</pdfPageCount>
<abstractWordCount>96</abstractWordCount>
</qualityIndicators>
<title>Structural and functional domains of E coli initiation factor IF2</title>
<pii>
<json:string>0300-9084(91)90191-3</json:string>
</pii>
<refBibs>
<json:item>
<host>
<pages>
<last>647</last>
<first>613</first>
</pages>
<author></author>
<title>Protein Biosynthesis</title>
</host>
</json:item>
<json:item>
<author>
<json:item>
<name>K. Shiba</name>
</json:item>
<json:item>
<name>K. Ito</name>
</json:item>
<json:item>
<name>Y. Nakamura</name>
</json:item>
<json:item>
<name>J. Dondon</name>
</json:item>
<json:item>
<name>M. Grunberg-Manago</name>
</json:item>
</author>
<host>
<volume>5</volume>
<pages>
<last>3006</last>
<first>3001</first>
</pages>
<author></author>
<title>EMBO J</title>
</host>
<title>Altered translational initiation factor 2 in the cold sensitive ssyG mutant effects protein export in Escherichia coli</title>
</json:item>
<json:item>
<author>
<json:item>
<name>J.S. Butler</name>
</json:item>
<json:item>
<name>M. Springer</name>
</json:item>
<json:item>
<name>J. Dondon</name>
</json:item>
<json:item>
<name>M. Graffe</name>
</json:item>
<json:item>
<name>M. Grunberg-Manago</name>
</json:item>
</author>
<host>
<volume>192</volume>
<pages>
<last>780</last>
<first>767</first>
</pages>
<author></author>
<title>J Mol Biol</title>
</host>
<title>Escherichia coli protein synthesis initiation factor IF3 controls its own gene expression at the translational level in vivo</title>
</json:item>
<json:item>
<author>
<json:item>
<name>J.A. Plumbridge</name>
</json:item>
<json:item>
<name>J.G. Howe</name>
</json:item>
<json:item>
<name>M. Springer</name>
</json:item>
<json:item>
<name>D. Touati-Schwartz</name>
</json:item>
<json:item>
<name>J.W.B. Hershey</name>
</json:item>
<json:item>
<name>M. Grunberg-Manago</name>
</json:item>
</author>
<host>
<author></author>
<title>Proc Natl Acad Sci USA</title>
</host>
<serie>
<author></author>
<title>Proc Natl Acad Sci USA</title>
</serie>
<title>Cloning and mapping of a gene for translational initiation factor IF2 in Escherichia coli</title>
</json:item>
<json:item>
<author>
<json:item>
<name>S. Ishii</name>
</json:item>
<json:item>
<name>K. Kuroki</name>
</json:item>
<json:item>
<name>F. Imamoto</name>
</json:item>
</author>
<host>
<author></author>
<title>Proc Natl Acad Sci USA</title>
</host>
<serie>
<author></author>
<title>Proc Natl Acad Sci USA</title>
</serie>
<title>tRNAf2met gene in the leader region of the nusA operon in Escherichia coli</title>
</json:item>
<json:item>
<author>
<json:item>
<name>T. Kurihara</name>
</json:item>
<json:item>
<name>Y. Nakamura</name>
</json:item>
</author>
<host>
<volume>190</volume>
<pages>
<last>195</last>
<first>189</first>
</pages>
<author></author>
<title>Mol Gen Genet</title>
</host>
<title>Cloning of the nusA gene of Escherichia coli</title>
</json:item>
<json:item>
<author>
<json:item>
<name>J.F. Sands</name>
</json:item>
<json:item>
<name>P. Regnier</name>
</json:item>
<json:item>
<name>H.S. Cummings</name>
</json:item>
<json:item>
<name>M. Grunberg-Manago</name>
</json:item>
<json:item>
<name>J.W.B. Hershey</name>
</json:item>
</author>
<host>
<volume>16</volume>
<pages>
<last>10816</last>
<first>10803</first>
</pages>
<author></author>
<title>Nucleic Acids Res</title>
</host>
<title>The existence of two genes between infB and rpsO in the Escherichia coli genome: DNA sequencing and S1 nuclease mapping</title>
</json:item>
<json:item>
<author>
<json:item>
<name>K. Shazand</name>
</json:item>
<json:item>
<name>J. Tucker</name>
</json:item>
<json:item>
<name>R. Chiang</name>
</json:item>
<json:item>
<name>K. Stansmore</name>
</json:item>
<json:item>
<name>H.U. Sperling-Petersen</name>
</json:item>
<json:item>
<name>M. Grunberg-Manago</name>
</json:item>
<json:item>
<name>J.C. Rabinowitz</name>
</json:item>
<json:item>
<name>T. Leighton</name>
</json:item>
</author>
<host>
<volume>172</volume>
<pages>
<last>2687</last>
<first>2675</first>
</pages>
<author></author>
<title>J Bacteriol</title>
</host>
<title>Isolation and molecular genetic characterization of the Bacillus subtilis gene (infB) encoding protein synthesis initiation factor IF2</title>
</json:item>
<json:item>
<author>
<json:item>
<name>H.R. Bourne</name>
</json:item>
<json:item>
<name>D.A. Sanders</name>
</json:item>
<json:item>
<name>F. McCormick</name>
</json:item>
</author>
<host>
<volume>348</volume>
<pages>
<last>132</last>
<first>125</first>
</pages>
<author></author>
<title>Nature (Lond)</title>
</host>
<title>The GTPase superfamily: a conserved switch for diverse cell functions</title>
</json:item>
<json:item>
<author>
<json:item>
<name>F. Jurnak</name>
</json:item>
</author>
<host>
<volume>230</volume>
<pages>
<last>36</last>
<first>32</first>
</pages>
<author></author>
<title>Science</title>
</host>
<title>Structure of the GDP domain of EF-Tu and location of the aminoacids homologous to ras oncogene proteins</title>
</json:item>
<json:item>
<author>
<json:item>
<name>T.F.M. La Cour</name>
</json:item>
<json:item>
<name>J. Nyborg</name>
</json:item>
<json:item>
<name>S. Thirup</name>
</json:item>
<json:item>
<name>B.F.C. Clark</name>
</json:item>
</author>
<host>
<volume>4</volume>
<pages>
<last>2388</last>
<first>2385</first>
</pages>
<author></author>
<title>EMBO J</title>
</host>
<title>Structural studies of the binding of elongation factor Tu from E coli as studied by X-ray crystallography</title>
</json:item>
<json:item>
<author>
<json:item>
<name>R. Leberman</name>
</json:item>
<json:item>
<name>U. Egner</name>
</json:item>
</author>
<host>
<volume>3</volume>
<pages>
<last>341</last>
<first>339</first>
</pages>
<author></author>
<title>EMBO J</title>
</host>
<title>Homologies in the primary structure of GTP-binding proteins: the nucleotide-binding site of EF-Tu and p21</title>
</json:item>
<json:item>
<author>
<json:item>
<name>P.E. March</name>
</json:item>
<json:item>
<name>M. Inoute</name>
</json:item>
</author>
<host>
<volume>260</volume>
<pages>
<last>7213</last>
<first>7206</first>
</pages>
<author></author>
<title>J Biol Chem</title>
</host>
<title>Characterisation of the lep operon of Escherichia coli</title>
</json:item>
<json:item>
<author>
<json:item>
<name>J. Ahnn</name>
</json:item>
<json:item>
<name>P.E. March</name>
</json:item>
<json:item>
<name>H.E. Takiff</name>
</json:item>
<json:item>
<name>M. Inouye</name>
</json:item>
</author>
<host>
<author></author>
<title>Proc Natl Acad Sci USA</title>
</host>
<serie>
<author></author>
<title>Proc Natl Acad Sci USA</title>
</serie>
<title>A GTP-binding protein of Escherichia coli has homology to yeast RAS proteins</title>
</json:item>
<json:item>
<author>
<json:item>
<name>A. Parmeggiani</name>
</json:item>
<json:item>
<name>G.W.M. Swart</name>
</json:item>
<json:item>
<name>K.K. Mortensen</name>
</json:item>
<json:item>
<name>M. Jensen</name>
</json:item>
<json:item>
<name>B.F.C. Clark</name>
</json:item>
<json:item>
<name>L. Dente</name>
</json:item>
<json:item>
<name>R. Cortese</name>
</json:item>
</author>
<host>
<author></author>
<title>Proc Natl Acad Sci USA</title>
</host>
<serie>
<author></author>
<title>Proc Natl Acad Sci USA</title>
</serie>
<title>Properties of a genetically engineered G domain of elongation factor Tu</title>
</json:item>
<json:item>
<author>
<json:item>
<name>Y. Cenatiempo</name>
</json:item>
<json:item>
<name>F. Deville</name>
</json:item>
<json:item>
<name>J. Dondon</name>
</json:item>
<json:item>
<name>M. Grunberg-Manago</name>
</json:item>
<json:item>
<name>C. Sacerdot</name>
</json:item>
<json:item>
<name>J.W.B. Hershey</name>
</json:item>
<json:item>
<name>H.F. Hansen</name>
</json:item>
<json:item>
<name>H.U. Petersen</name>
</json:item>
<json:item>
<name>B.F.C. Clark</name>
</json:item>
<json:item>
<name>M. Kjeldgaard</name>
</json:item>
<json:item>
<name>T.F.M. La Cour</name>
</json:item>
<json:item>
<name>K.K. Mortensen</name>
</json:item>
<json:item>
<name>J. Nyborg</name>
</json:item>
</author>
<host>
<volume>26</volume>
<pages>
<last>5076</last>
<first>5070</first>
</pages>
<author></author>
<title>Biochemistry</title>
</host>
<title>The protein synthesis initiation factor 2 G-domain. Study of a functionally active C-terminal 65-kDa fragment of IF2 from Escherichia coli</title>
</json:item>
<json:item>
<author>
<json:item>
<name>J. Dondon</name>
</json:item>
<json:item>
<name>J.A. Plumbridge</name>
</json:item>
<json:item>
<name>J.W.B. Hershey</name>
</json:item>
<json:item>
<name>M. Grunberg-Manago</name>
</json:item>
</author>
<host>
<volume>67</volume>
<pages>
<last>649</last>
<first>643</first>
</pages>
<author></author>
<title>Biochimie</title>
</host>
<title>Overproduction and purification of Initiation Factor IF2 and pNusA proteins from a recombinant plasmid bearing strain</title>
</json:item>
<json:item>
<author>
<json:item>
<name>J.A. Plumbridge</name>
</json:item>
<json:item>
<name>F. Deville</name>
</json:item>
<json:item>
<name>C. Sacerdot</name>
</json:item>
<json:item>
<name>P. Petersen</name>
</json:item>
<json:item>
<name>Y. Cenatiempo</name>
</json:item>
<json:item>
<name>A. Cozzone</name>
</json:item>
<json:item>
<name>M. Grunberg-Manago</name>
</json:item>
<json:item>
<name>J.W.B. Hershey</name>
</json:item>
</author>
<host>
<volume>4</volume>
<pages>
<last>229</last>
<first>223</first>
</pages>
<author></author>
<title>EMBO J</title>
</host>
<title>Two translational initiation sites in the infB gene are used to express initiation factor IF2α and IF2β in Escherichia coli</title>
</json:item>
<json:item>
<author>
<json:item>
<name>F. Morel-Deville</name>
</json:item>
<json:item>
<name>G. Vachon</name>
</json:item>
<json:item>
<name>C. Sacerdot</name>
</json:item>
<json:item>
<name>A. Cozzone</name>
</json:item>
<json:item>
<name>M. Grunberg-Manago</name>
</json:item>
<json:item>
<name>Y. Cenatiempo</name>
</json:item>
</author>
<host>
<volume>188</volume>
<pages>
<last>614</last>
<first>605</first>
</pages>
<author></author>
<title>Eur J Biochem</title>
</host>
<title>Characterisation of the translational start site for IF2β, a short form of Escherichia coli initiation factor IF2</title>
</json:item>
<json:item>
<author>
<json:item>
<name>C. Sacerdot</name>
</json:item>
<json:item>
<name>G. Vachon</name>
</json:item>
<json:item>
<name>S. Laalami</name>
</json:item>
<json:item>
<name>F. Morel-Deville</name>
</json:item>
<json:item>
<name>Y. Cenatiempo</name>
</json:item>
<json:item>
<name>M. Grunberg-Manago</name>
</json:item>
</author>
<host>
<author></author>
<title>J Mol Biol</title>
</host>
<title>Both forms of translational Initiation Factor IF2 (α and β) are required for maximal growth of E coli. Evidence for two translation initiation codons for IF2β</title>
</json:item>
<json:item>
<author>
<json:item>
<name>K.K. Mortensen</name>
</json:item>
<json:item>
<name>N.R. Nyengaard</name>
</json:item>
<json:item>
<name>J.W.B. Hershey</name>
</json:item>
<json:item>
<name>S. Laalami</name>
</json:item>
<json:item>
<name>H.U. Sperling-Petersen</name>
</json:item>
</author>
<host>
<volume>73</volume>
<pages>
<last>989</last>
<first>983</first>
</pages>
<author></author>
<title>Biochimie</title>
</host>
<title>Superexpression and fast purification of E coli initiation factor IF2</title>
</json:item>
<json:item>
<author>
<json:item>
<name>C. Sacerdot</name>
</json:item>
<json:item>
<name>P. Dessen</name>
</json:item>
<json:item>
<name>J.W.B. Hershey</name>
</json:item>
<json:item>
<name>J.A. Plumbridge</name>
</json:item>
<json:item>
<name>M. Grunberg-Manago</name>
</json:item>
</author>
<host>
<author></author>
<title>Proc Natl Acad Sci USA</title>
</host>
<serie>
<author></author>
<title>Proc Natl Acad Sci USA</title>
</serie>
<title>Sequence of the initiation factor IF2 gene: Unusual protein features and homologies with elongation factors</title>
</json:item>
<json:item>
<author>
<json:item>
<name>H.U. Sperling-Petersen</name>
</json:item>
<json:item>
<name>K.K.A. Mortensen</name>
</json:item>
</author>
<host>
<volume>3</volume>
<pages>
<last>344</last>
<first>343</first>
</pages>
<author></author>
<title>Protein Eng</title>
</host>
<title>Structural model for initiation factor IF2 from E coli</title>
</json:item>
<json:item>
<author>
<json:item>
<name>H.U. Petersen</name>
</json:item>
</author>
<host>
<volume>41</volume>
<pages>
<last>335</last>
<first>291</first>
</pages>
<author></author>
<title>Mat Fys Medd Dan Vid Selsk</title>
</host>
<title>Function of tRNA in initiation of procaryotic translation</title>
</json:item>
<json:item>
<host>
<author></author>
<title>J Bacteriol</title>
</host>
</json:item>
<json:item>
<author>
<json:item>
<name>F. McCormick</name>
</json:item>
<json:item>
<name>B.F.C. Clark</name>
</json:item>
<json:item>
<name>T.F.M. La Cour</name>
</json:item>
<json:item>
<name>M. Kjelgaard</name>
</json:item>
<json:item>
<name>L. Norskov-Lauristen</name>
</json:item>
<json:item>
<name>J. Nyberg</name>
</json:item>
</author>
<host>
<volume>230</volume>
<pages>
<last>82</last>
<first>78</first>
</pages>
<author></author>
<title>Science</title>
</host>
<title>A model for the tertiary structure of p21, the product of the ras oncogene</title>
</json:item>
<json:item>
<author>
<json:item>
<name>S. Laalami</name>
</json:item>
<json:item>
<name>H. Putzer</name>
</json:item>
<json:item>
<name>J.A. Plumbridge</name>
</json:item>
<json:item>
<name>M. Grunberg-Manago</name>
</json:item>
</author>
<host>
<volume>220</volume>
<pages>
<last>349</last>
<first>335</first>
</pages>
<author></author>
<title>J Mol Biol</title>
</host>
<title>A severly truncated form of translational Initiation Factor 2 supports growth of Escherichia coli</title>
</json:item>
<json:item>
<author>
<json:item>
<name>M. Grunberg-Manago</name>
</json:item>
<json:item>
<name>J. Dondon</name>
</json:item>
<json:item>
<name>M. Graffe</name>
</json:item>
</author>
<host>
<volume>22</volume>
<pages>
<last>221</last>
<first>217</first>
</pages>
<author></author>
<title>FEBS Lett</title>
</host>
<title>Inhibition by thiostrepton of the IF2 dependent ribosomal GTPase</title>
</json:item>
<json:item>
<author>
<json:item>
<name>G. Vachon</name>
</json:item>
<json:item>
<name>S. Laalami</name>
</json:item>
<json:item>
<name>M. Grunberg-Manago</name>
</json:item>
<json:item>
<name>R. Julien</name>
</json:item>
<json:item>
<name>Y. Cenatiempo</name>
</json:item>
</author>
<host>
<volume>29</volume>
<pages>
<last>9733</last>
<first>9728</first>
</pages>
<author></author>
<title>Biochemistry</title>
</host>
<title>Purified internal G-domain of translational initiation factor IF2 displays guanine nucleotide binding properties</title>
</json:item>
<json:item>
<author>
<json:item>
<name>R.A. Smith</name>
</json:item>
<json:item>
<name>J.S. Parkinson</name>
</json:item>
</author>
<host>
<author></author>
<title>Proc Natl Acad Sci USA</title>
</host>
<serie>
<author></author>
<title>Proc Natl Acad Sci USA</title>
</serie>
<title>Overlapping genes at the cheA locus of Escherichia coli</title>
</json:item>
<json:item>
<author>
<json:item>
<name>T.K. Ross</name>
</json:item>
<json:item>
<name>E.C. Achberger</name>
</json:item>
<json:item>
<name>D.H. Braymer</name>
</json:item>
</author>
<host>
<volume>171</volume>
<pages>
<last>1981</last>
<first>1974</first>
</pages>
<author></author>
<title>J Bacteriol</title>
</host>
<title>Nucleotide sequence of the McrB region of Escherichia coli K-12 and evidence for two independent translation initiation sites at the mcrB locus</title>
</json:item>
<json:item>
<author>
<json:item>
<name>C.L. Squires</name>
</json:item>
<json:item>
<name>S. Pedersen</name>
</json:item>
<json:item>
<name>B.M. Ross</name>
</json:item>
<json:item>
<name>C. Squires</name>
</json:item>
</author>
<host>
<volume>173</volume>
<pages>
<last>4262</last>
<first>4254</first>
</pages>
<author></author>
<title>J Bacteriol</title>
</host>
<title>ClpB is the Escherichia coli heat-shock protein F84.1</title>
</json:item>
<json:item>
<author>
<json:item>
<name>P.G. Jones</name>
</json:item>
<json:item>
<name>R.A. Van Bogelen</name>
</json:item>
<json:item>
<name>F.C. Neidhardt</name>
</json:item>
</author>
<host>
<volume>169</volume>
<pages>
<last>2095</last>
<first>2092</first>
</pages>
<author></author>
<title>J Bacteriol</title>
</host>
<title>Induction of proteins in response to low temperature in Escherichia coli</title>
</json:item>
<json:item>
<author>
<json:item>
<name>J.E. Shaw</name>
</json:item>
<json:item>
<name>H. Murialdo</name>
</json:item>
</author>
<host>
<volume>283</volume>
<pages>
<last>35</last>
<first>30</first>
</pages>
<author></author>
<title>Nature (Lond)</title>
</host>
<title>Morphogenic genes C and Nu3 overlap in bacteriophage λ</title>
</json:item>
<json:item>
<author>
<json:item>
<name>R.R. Isberg</name>
</json:item>
<json:item>
<name>A.L. Lazaar</name>
</json:item>
<json:item>
<name>M. Syvanen</name>
</json:item>
</author>
<host>
<volume>30</volume>
<pages>
<last>892</last>
<first>883</first>
</pages>
<author></author>
<title>Cell</title>
</host>
<title>Regulation of Tn5 by the right-repeat proteins: control at the level of the transposition reaction?</title>
</json:item>
<json:item>
<author>
<json:item>
<name>R.C. Johnson</name>
</json:item>
<json:item>
<name>J.C.P. Yin</name>
</json:item>
<json:item>
<name>W.S. Reznikoff</name>
</json:item>
</author>
<host>
<volume>30</volume>
<pages>
<last>882</last>
<first>873</first>
</pages>
<author></author>
<title>Cell</title>
</host>
<title>Control of Tn5 transposition in Escherichia coli is mediated by protein from the right repeat</title>
</json:item>
<json:item>
<author>
<json:item>
<name>A. Ishihama</name>
</json:item>
</author>
<host>
<volume>4</volume>
<pages>
<last>286</last>
<first>282</first>
</pages>
<author></author>
<title>Trends Genet</title>
</host>
<title>Promoter selectivity of prokaryotic RNA polymerases</title>
</json:item>
<json:item>
<author>
<json:item>
<name>J.G. Howe</name>
</json:item>
<json:item>
<name>J.W.B. Hershey</name>
</json:item>
</author>
<host>
<volume>140</volume>
<pages>
<last>192</last>
<first>187</first>
</pages>
<author></author>
<title>Arch Microbiol</title>
</host>
<title>The rate of evolutionary divergence of initiation factors IF2 and IF3 in various bacterial species determined quantitatively by immunoblotting</title>
</json:item>
</refBibs>
<genre>
<json:string>research-article</json:string>
</genre>
<serie>
<volume>79</volume>
<pages>
<last>5037</last>
<first>5033</first>
</pages>
<language>
<json:string>unknown</json:string>
</language>
<title>Proc Natl Acad Sci USA</title>
</serie>
<host>
<volume>73</volume>
<pii>
<json:string>S0300-9084(00)X0158-7</json:string>
</pii>
<pages>
<last>1566</last>
<first>1557</first>
</pages>
<issn>
<json:string>0300-9084</json:string>
</issn>
<issue>12</issue>
<genre>
<json:string>journal</json:string>
</genre>
<language>
<json:string>unknown</json:string>
</language>
<title>Biochimie</title>
<publicationDate>1991</publicationDate>
</host>
<categories>
<wos>
<json:string>science</json:string>
<json:string>biochemistry & molecular biology</json:string>
</wos>
<scienceMetrix>
<json:string>health sciences</json:string>
<json:string>biomedical research</json:string>
<json:string>biochemistry & molecular biology</json:string>
</scienceMetrix>
</categories>
<publicationDate>1991</publicationDate>
<copyrightDate>1991</copyrightDate>
<doi>
<json:string>10.1016/0300-9084(91)90191-3</json:string>
</doi>
<id>6EB34AF27D0525F2BA115036672D32A805678944</id>
<score>0.12183508</score>
<fulltext>
<json:item>
<extension>pdf</extension>
<original>true</original>
<mimetype>application/pdf</mimetype>
<uri>https://api.istex.fr/document/6EB34AF27D0525F2BA115036672D32A805678944/fulltext/pdf</uri>
</json:item>
<json:item>
<extension>zip</extension>
<original>false</original>
<mimetype>application/zip</mimetype>
<uri>https://api.istex.fr/document/6EB34AF27D0525F2BA115036672D32A805678944/fulltext/zip</uri>
</json:item>
<istex:fulltextTEI uri="https://api.istex.fr/document/6EB34AF27D0525F2BA115036672D32A805678944/fulltext/tei">
<teiHeader>
<fileDesc>
<titleStmt>
<title level="a">Structural and functional domains of E coli initiation factor IF2</title>
</titleStmt>
<publicationStmt>
<authority>ISTEX</authority>
<publisher>ELSEVIER</publisher>
<availability>
<p>ELSEVIER</p>
</availability>
<date>1991</date>
</publicationStmt>
<sourceDesc>
<biblStruct type="inbook">
<analytic>
<title level="a">Structural and functional domains of E coli initiation factor IF2</title>
<author xml:id="author-1">
<persName>
<forename type="first">S.</forename>
<surname>Laalami</surname>
</persName>
<affiliation>Institut de Biologie Physico-Chimique, 13 rue Pierre et Marie Curie, 75005 Paris, France</affiliation>
</author>
<author xml:id="author-2">
<persName>
<forename type="first">C.</forename>
<surname>Sacerdot</surname>
</persName>
<affiliation>Institut de Biologie Physico-Chimique, 13 rue Pierre et Marie Curie, 75005 Paris, France</affiliation>
</author>
<author xml:id="author-3">
<persName>
<forename type="first">G.</forename>
<surname>Vachon</surname>
</persName>
<affiliation>Laboratoire de Biologie Moléculaire, URA CNRS 1172, Université de Poitiers, 40, avenue du Recteur Pineau, 86022 PoitiersCedex, France</affiliation>
</author>
<author xml:id="author-4">
<persName>
<forename type="first">K.</forename>
<surname>Mortensen</surname>
</persName>
<affiliation>Laboratory of Biodesign, Department of Chemistry, Aarhus University, DK-8000 Aarhus, Denmark</affiliation>
</author>
<author xml:id="author-5">
<persName>
<forename type="first">H.U.</forename>
<surname>Sperling-Petersen</surname>
</persName>
<affiliation>Laboratory of Biodesign, Department of Chemistry, Aarhus University, DK-8000 Aarhus, Denmark</affiliation>
</author>
<author xml:id="author-6">
<persName>
<forename type="first">Y.</forename>
<surname>Cenatiempo</surname>
</persName>
<affiliation>Laboratoire de Biologie Moléculaire, URA CNRS 1172, Université de Poitiers, 40, avenue du Recteur Pineau, 86022 PoitiersCedex, France</affiliation>
</author>
<author xml:id="author-7">
<persName>
<forename type="first">M.</forename>
<surname>Grunberg-Manago</surname>
</persName>
<affiliation>Correspondence and reprints</affiliation>
<affiliation>Institut de Biologie Physico-Chimique, 13 rue Pierre et Marie Curie, 75005 Paris, France</affiliation>
</author>
</analytic>
<monogr>
<title level="j">Biochimie</title>
<title level="j" type="abbrev">BIOCHI</title>
<idno type="pISSN">0300-9084</idno>
<idno type="PII">S0300-9084(00)X0158-7</idno>
<imprint>
<publisher>ELSEVIER</publisher>
<date type="published" when="1991"></date>
<biblScope unit="volume">73</biblScope>
<biblScope unit="issue">12</biblScope>
<biblScope unit="page" from="1557">1557</biblScope>
<biblScope unit="page" to="1566">1566</biblScope>
</imprint>
</monogr>
<idno type="istex">6EB34AF27D0525F2BA115036672D32A805678944</idno>
<idno type="DOI">10.1016/0300-9084(91)90191-3</idno>
<idno type="PII">0300-9084(91)90191-3</idno>
</biblStruct>
</sourceDesc>
</fileDesc>
<profileDesc>
<creation>
<date>1991</date>
</creation>
<langUsage>
<language ident="en">en</language>
</langUsage>
<abstract xml:lang="en">
<p>Initiation of translation in prokaryotes requires the participation of at least three soluble proteins: the initiation factors IF1, IF2 and IF3. Initiation factor 2, which is one of the largest proteins involved in translation (97.3 kDa) has been shown to stimulate in vitro the binding of fMet-tRNAfMet to the 30S ribosomal subunit. After formation of 70S translation intiation complex, IF2 is believed to participate in GTP hydrolysis, thereby promoting its own release. Here we review evidence which indicates the functional importance of the different structural domains of IF2, emphasizing new information obtained by in vivo experiments.</p>
</abstract>
<textClass>
<keywords scheme="keyword">
<list>
<head>Keywords</head>
<item>
<term>translation initiation factor 2</term>
</item>
<item>
<term>IF2α and IF2β</term>
</item>
<item>
<term>G binding protein</term>
</item>
<item>
<term>G domain</term>
</item>
</list>
</keywords>
</textClass>
</profileDesc>
<revisionDesc>
<change when="1991">Published</change>
</revisionDesc>
</teiHeader>
</istex:fulltextTEI>
<json:item>
<extension>txt</extension>
<original>false</original>
<mimetype>text/plain</mimetype>
<uri>https://api.istex.fr/document/6EB34AF27D0525F2BA115036672D32A805678944/fulltext/txt</uri>
</json:item>
</fulltext>
<metadata>
<istex:metadataXml wicri:clean="Elsevier, elements deleted: tail">
<istex:xmlDeclaration>version="1.0" encoding="utf-8"</istex:xmlDeclaration>
<istex:docType PUBLIC="-//ES//DTD journal article DTD version 4.5.2//EN//XML" URI="art452.dtd" name="istex:docType"></istex:docType>
<istex:document>
<converted-article version="4.5.2" docsubtype="fla">
<item-info>
<jid>BIOCHI</jid>
<aid>91901913</aid>
<ce:pii>0300-9084(91)90191-3</ce:pii>
<ce:doi>10.1016/0300-9084(91)90191-3</ce:doi>
<ce:copyright type="unknown" year="1991"></ce:copyright>
</item-info>
<head>
<ce:title>Structural and functional domains of
<ce:italic>E coli</ce:italic>
initiation factor IF2</ce:title>
<ce:author-group>
<ce:author>
<ce:given-name>S.</ce:given-name>
<ce:surname>Laalami</ce:surname>
<ce:cross-ref refid="AFF1">
<ce:sup>1</ce:sup>
</ce:cross-ref>
</ce:author>
<ce:author>
<ce:given-name>C.</ce:given-name>
<ce:surname>Sacerdot</ce:surname>
<ce:cross-ref refid="AFF1">
<ce:sup>1</ce:sup>
</ce:cross-ref>
</ce:author>
<ce:author>
<ce:given-name>G.</ce:given-name>
<ce:surname>Vachon</ce:surname>
<ce:cross-ref refid="AFF2">
<ce:sup>2</ce:sup>
</ce:cross-ref>
</ce:author>
<ce:author>
<ce:given-name>K.</ce:given-name>
<ce:surname>Mortensen</ce:surname>
<ce:cross-ref refid="AFF3">
<ce:sup>3</ce:sup>
</ce:cross-ref>
</ce:author>
<ce:author>
<ce:given-name>H.U.</ce:given-name>
<ce:surname>Sperling-Petersen</ce:surname>
<ce:cross-ref refid="AFF3">
<ce:sup>3</ce:sup>
</ce:cross-ref>
</ce:author>
<ce:author>
<ce:given-name>Y.</ce:given-name>
<ce:surname>Cenatiempo</ce:surname>
<ce:cross-ref refid="AFF2">
<ce:sup>2</ce:sup>
</ce:cross-ref>
</ce:author>
<ce:author>
<ce:given-name>M.</ce:given-name>
<ce:surname>Grunberg-Manago</ce:surname>
<ce:cross-ref refid="COR1">
<ce:sup></ce:sup>
</ce:cross-ref>
<ce:cross-ref refid="AFF1">
<ce:sup>1</ce:sup>
</ce:cross-ref>
</ce:author>
<ce:affiliation id="AFF1">
<ce:label>a</ce:label>
<ce:textfn>Institut de Biologie Physico-Chimique, 13 rue Pierre et Marie Curie, 75005 Paris, France</ce:textfn>
</ce:affiliation>
<ce:affiliation id="AFF2">
<ce:label>b</ce:label>
<ce:textfn>Laboratoire de Biologie Moléculaire, URA CNRS 1172, Université de Poitiers, 40, avenue du Recteur Pineau, 86022 PoitiersCedex, France</ce:textfn>
</ce:affiliation>
<ce:affiliation id="AFF3">
<ce:label>c</ce:label>
<ce:textfn>Laboratory of Biodesign, Department of Chemistry, Aarhus University, DK-8000 Aarhus, Denmark</ce:textfn>
</ce:affiliation>
<ce:correspondence id="COR1">
<ce:label></ce:label>
<ce:text>Correspondence and reprints</ce:text>
</ce:correspondence>
</ce:author-group>
<ce:date-received day="9" month="10" year="1991"></ce:date-received>
<ce:date-accepted day="4" month="11" year="1991"></ce:date-accepted>
<ce:abstract>
<ce:section-title>Abstract</ce:section-title>
<ce:abstract-sec>
<ce:simple-para>Initiation of translation in prokaryotes requires the participation of at least three soluble proteins: the initiation factors IF1, IF2 and IF3. Initiation factor 2, which is one of the largest proteins involved in translation (97.3 kDa) has been shown to stimulate
<ce:italic>in vitro</ce:italic>
the binding of fMet-tRNA
<ce:inf>f</ce:inf>
<ce:sup>Met</ce:sup>
to the 30S ribosomal subunit. After formation of 70S translation intiation complex, IF2 is believed to participate in GTP hydrolysis, thereby promoting its own release. Here we review evidence which indicates the functional importance of the different structural domains of IF2, emphasizing new information obtained by
<ce:italic>in vivo</ce:italic>
experiments.</ce:simple-para>
</ce:abstract-sec>
</ce:abstract>
<ce:keywords>
<ce:section-title>Keywords</ce:section-title>
<ce:keyword>
<ce:text>translation initiation factor 2</ce:text>
</ce:keyword>
<ce:keyword>
<ce:text>IF2α and IF2β</ce:text>
</ce:keyword>
<ce:keyword>
<ce:text>G binding protein</ce:text>
</ce:keyword>
<ce:keyword>
<ce:text>G domain</ce:text>
</ce:keyword>
</ce:keywords>
</head>
</converted-article>
</istex:document>
</istex:metadataXml>
<mods version="3.6">
<titleInfo>
<title>Structural and functional domains of E coli initiation factor IF2</title>
</titleInfo>
<titleInfo type="alternative" contentType="CDATA">
<title>Structural and functional domains of</title>
</titleInfo>
<name type="personal">
<namePart type="given">S.</namePart>
<namePart type="family">Laalami</namePart>
<affiliation>Institut de Biologie Physico-Chimique, 13 rue Pierre et Marie Curie, 75005 Paris, France</affiliation>
<role>
<roleTerm type="text">author</roleTerm>
</role>
</name>
<name type="personal">
<namePart type="given">C.</namePart>
<namePart type="family">Sacerdot</namePart>
<affiliation>Institut de Biologie Physico-Chimique, 13 rue Pierre et Marie Curie, 75005 Paris, France</affiliation>
<role>
<roleTerm type="text">author</roleTerm>
</role>
</name>
<name type="personal">
<namePart type="given">G.</namePart>
<namePart type="family">Vachon</namePart>
<affiliation>Laboratoire de Biologie Moléculaire, URA CNRS 1172, Université de Poitiers, 40, avenue du Recteur Pineau, 86022 PoitiersCedex, France</affiliation>
<role>
<roleTerm type="text">author</roleTerm>
</role>
</name>
<name type="personal">
<namePart type="given">K.</namePart>
<namePart type="family">Mortensen</namePart>
<affiliation>Laboratory of Biodesign, Department of Chemistry, Aarhus University, DK-8000 Aarhus, Denmark</affiliation>
<role>
<roleTerm type="text">author</roleTerm>
</role>
</name>
<name type="personal">
<namePart type="given">H.U.</namePart>
<namePart type="family">Sperling-Petersen</namePart>
<affiliation>Laboratory of Biodesign, Department of Chemistry, Aarhus University, DK-8000 Aarhus, Denmark</affiliation>
<role>
<roleTerm type="text">author</roleTerm>
</role>
</name>
<name type="personal">
<namePart type="given">Y.</namePart>
<namePart type="family">Cenatiempo</namePart>
<affiliation>Laboratoire de Biologie Moléculaire, URA CNRS 1172, Université de Poitiers, 40, avenue du Recteur Pineau, 86022 PoitiersCedex, France</affiliation>
<role>
<roleTerm type="text">author</roleTerm>
</role>
</name>
<name type="personal">
<namePart type="given">M.</namePart>
<namePart type="family">Grunberg-Manago</namePart>
<affiliation>Correspondence and reprints</affiliation>
<affiliation>Institut de Biologie Physico-Chimique, 13 rue Pierre et Marie Curie, 75005 Paris, France</affiliation>
<role>
<roleTerm type="text">author</roleTerm>
</role>
</name>
<typeOfResource>text</typeOfResource>
<genre type="research-article" displayLabel="Full-length article"></genre>
<originInfo>
<publisher>ELSEVIER</publisher>
<dateIssued encoding="w3cdtf">1991</dateIssued>
<copyrightDate encoding="w3cdtf">1991</copyrightDate>
</originInfo>
<language>
<languageTerm type="code" authority="iso639-2b">eng</languageTerm>
<languageTerm type="code" authority="rfc3066">en</languageTerm>
</language>
<physicalDescription>
<internetMediaType>text/html</internetMediaType>
</physicalDescription>
<abstract lang="en">Initiation of translation in prokaryotes requires the participation of at least three soluble proteins: the initiation factors IF1, IF2 and IF3. Initiation factor 2, which is one of the largest proteins involved in translation (97.3 kDa) has been shown to stimulate in vitro the binding of fMet-tRNAfMet to the 30S ribosomal subunit. After formation of 70S translation intiation complex, IF2 is believed to participate in GTP hydrolysis, thereby promoting its own release. Here we review evidence which indicates the functional importance of the different structural domains of IF2, emphasizing new information obtained by in vivo experiments.</abstract>
<subject>
<genre>Keywords</genre>
<topic>translation initiation factor 2</topic>
<topic>IF2α and IF2β</topic>
<topic>G binding protein</topic>
<topic>G domain</topic>
</subject>
<relatedItem type="host">
<titleInfo>
<title>Biochimie</title>
</titleInfo>
<titleInfo type="abbreviated">
<title>BIOCHI</title>
</titleInfo>
<genre type="journal">journal</genre>
<originInfo>
<dateIssued encoding="w3cdtf">199112</dateIssued>
</originInfo>
<identifier type="ISSN">0300-9084</identifier>
<identifier type="PII">S0300-9084(00)X0158-7</identifier>
<part>
<date>199112</date>
<detail type="volume">
<number>73</number>
<caption>vol.</caption>
</detail>
<detail type="issue">
<number>12</number>
<caption>no.</caption>
</detail>
<extent unit="issue pages">
<start>1431</start>
<end>1579</end>
</extent>
<extent unit="pages">
<start>1557</start>
<end>1566</end>
</extent>
</part>
</relatedItem>
<identifier type="istex">6EB34AF27D0525F2BA115036672D32A805678944</identifier>
<identifier type="DOI">10.1016/0300-9084(91)90191-3</identifier>
<identifier type="PII">0300-9084(91)90191-3</identifier>
<recordInfo>
<recordContentSource>ELSEVIER</recordContentSource>
</recordInfo>
</mods>
</metadata>
</istex>
</record>

Pour manipuler ce document sous Unix (Dilib)

EXPLOR_STEP=$WICRI_ROOT/Wicri/Sante/explor/ParkinsonFranceV1/Data/Istex/Corpus
HfdSelect -h $EXPLOR_STEP/biblio.hfd -nk 000F57 | SxmlIndent | more

Ou

HfdSelect -h $EXPLOR_AREA/Data/Istex/Corpus/biblio.hfd -nk 000F57 | SxmlIndent | more

Pour mettre un lien sur cette page dans le réseau Wicri

{{Explor lien
   |wiki=    Wicri/Sante
   |area=    ParkinsonFranceV1
   |flux=    Istex
   |étape=   Corpus
   |type=    RBID
   |clé=     ISTEX:6EB34AF27D0525F2BA115036672D32A805678944
   |texte=   Structural and functional domains of E coli initiation factor IF2
}}

Wicri

This area was generated with Dilib version V0.6.29.
Data generation: Wed May 17 19:46:39 2017. Site generation: Mon Mar 4 15:48:15 2024