YtqI from Bacillus subtilis has both oligoribonuclease and pAp-phosphatase activity
Identifieur interne : 001407 ( Pmc/Checkpoint ); précédent : 001406; suivant : 001408YtqI from Bacillus subtilis has both oligoribonuclease and pAp-phosphatase activity
Auteurs : Undine Mechold ; Gang Fang ; Saravuth Ngo ; Vasily Ogryzko [France] ; Antoine DanchinSource :
- Nucleic Acids Research [ 0305-1048 ] ; 2007.
Abstract
Oligoribonuclease is the only RNase in
Url:
DOI: 10.1093/nar/gkm462
PubMed: 17586819
PubMed Central: 1935014
Affiliations:
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<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">YtqI from <italic>Bacillus subtilis</italic> has both oligoribonuclease and pAp-phosphatase activity</title><author><name sortKey="Mechold, Undine" sort="Mechold, Undine" uniqKey="Mechold U" first="Undine" last="Mechold">Undine Mechold</name><affiliation><nlm:aff wicri:cut=" and" id="AFF1">Institut Pasteur, URA 2171, Unité de Génétique des Génomes Bactériens, 75724 Paris Cedex 15</nlm:aff><wicri:noCountry code="subfield">75724 Paris Cedex 15</wicri:noCountry></affiliation></author><author><name sortKey="Fang, Gang" sort="Fang, Gang" uniqKey="Fang G" first="Gang" last="Fang">Gang Fang</name><affiliation><nlm:aff wicri:cut=" and" id="AFF1">Institut Pasteur, URA 2171, Unité de Génétique des Génomes Bactériens, 75724 Paris Cedex 15</nlm:aff><wicri:noCountry code="subfield">75724 Paris Cedex 15</wicri:noCountry></affiliation></author><author><name sortKey="Ngo, Saravuth" sort="Ngo, Saravuth" uniqKey="Ngo S" first="Saravuth" last="Ngo">Saravuth Ngo</name><affiliation><nlm:aff wicri:cut=" and" id="AFF1">Institut Pasteur, URA 2171, Unité de Génétique des Génomes Bactériens, 75724 Paris Cedex 15</nlm:aff><wicri:noCountry code="subfield">75724 Paris Cedex 15</wicri:noCountry></affiliation></author><author><name sortKey="Ogryzko, Vasily" sort="Ogryzko, Vasily" uniqKey="Ogryzko V" first="Vasily" last="Ogryzko">Vasily Ogryzko</name><affiliation wicri:level="3"><nlm:aff id="AFF1">Institut Gustave Roussy, UMR 8126, Unité Interactions Moléculaires et Cancer, 94805 Villejuif, France</nlm:aff><country xml:lang="fr">France</country><wicri:regionArea>Institut Gustave Roussy, UMR 8126, Unité Interactions Moléculaires et Cancer, 94805 Villejuif</wicri:regionArea><placeName><region type="region" nuts="2">Île-de-France</region><settlement type="city">Villejuif</settlement></placeName></affiliation></author><author><name sortKey="Danchin, Antoine" sort="Danchin, Antoine" uniqKey="Danchin A" first="Antoine" last="Danchin">Antoine Danchin</name><affiliation><nlm:aff wicri:cut=" and" id="AFF1">Institut Pasteur, URA 2171, Unité de Génétique des Génomes Bactériens, 75724 Paris Cedex 15</nlm:aff><wicri:noCountry code="subfield">75724 Paris Cedex 15</wicri:noCountry></affiliation></author></titleStmt><publicationStmt><idno type="wicri:source">PMC</idno><idno type="pmid">17586819</idno><idno type="pmc">1935014</idno><idno type="url">http://www.ncbi.nlm.nih.gov/pmc/articles/PMC1935014</idno><idno type="RBID">PMC:1935014</idno><idno type="doi">10.1093/nar/gkm462</idno><date when="2007">2007</date><idno type="wicri:Area/Pmc/Corpus">000F40</idno><idno type="wicri:explorRef" wicri:stream="Pmc" wicri:step="Corpus" wicri:corpus="PMC">000F40</idno><idno type="wicri:Area/Pmc/Curation">000F40</idno><idno type="wicri:explorRef" wicri:stream="Pmc" wicri:step="Curation">000F40</idno><idno type="wicri:Area/Pmc/Checkpoint">001407</idno><idno type="wicri:explorRef" wicri:stream="Pmc" wicri:step="Checkpoint">001407</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en" level="a" type="main">YtqI from <italic>Bacillus subtilis</italic> has both oligoribonuclease and pAp-phosphatase activity</title><author><name sortKey="Mechold, Undine" sort="Mechold, Undine" uniqKey="Mechold U" first="Undine" last="Mechold">Undine Mechold</name><affiliation><nlm:aff wicri:cut=" and" id="AFF1">Institut Pasteur, URA 2171, Unité de Génétique des Génomes Bactériens, 75724 Paris Cedex 15</nlm:aff><wicri:noCountry code="subfield">75724 Paris Cedex 15</wicri:noCountry></affiliation></author><author><name sortKey="Fang, Gang" sort="Fang, Gang" uniqKey="Fang G" first="Gang" last="Fang">Gang Fang</name><affiliation><nlm:aff wicri:cut=" and" id="AFF1">Institut Pasteur, URA 2171, Unité de Génétique des Génomes Bactériens, 75724 Paris Cedex 15</nlm:aff><wicri:noCountry code="subfield">75724 Paris Cedex 15</wicri:noCountry></affiliation></author><author><name sortKey="Ngo, Saravuth" sort="Ngo, Saravuth" uniqKey="Ngo S" first="Saravuth" last="Ngo">Saravuth Ngo</name><affiliation><nlm:aff wicri:cut=" and" id="AFF1">Institut Pasteur, URA 2171, Unité de Génétique des Génomes Bactériens, 75724 Paris Cedex 15</nlm:aff><wicri:noCountry code="subfield">75724 Paris Cedex 15</wicri:noCountry></affiliation></author><author><name sortKey="Ogryzko, Vasily" sort="Ogryzko, Vasily" uniqKey="Ogryzko V" first="Vasily" last="Ogryzko">Vasily Ogryzko</name><affiliation wicri:level="3"><nlm:aff id="AFF1">Institut Gustave Roussy, UMR 8126, Unité Interactions Moléculaires et Cancer, 94805 Villejuif, France</nlm:aff><country xml:lang="fr">France</country><wicri:regionArea>Institut Gustave Roussy, UMR 8126, Unité Interactions Moléculaires et Cancer, 94805 Villejuif</wicri:regionArea><placeName><region type="region" nuts="2">Île-de-France</region><settlement type="city">Villejuif</settlement></placeName></affiliation></author><author><name sortKey="Danchin, Antoine" sort="Danchin, Antoine" uniqKey="Danchin A" first="Antoine" last="Danchin">Antoine Danchin</name><affiliation><nlm:aff wicri:cut=" and" id="AFF1">Institut Pasteur, URA 2171, Unité de Génétique des Génomes Bactériens, 75724 Paris Cedex 15</nlm:aff><wicri:noCountry code="subfield">75724 Paris Cedex 15</wicri:noCountry></affiliation></author></analytic><series><title level="j">Nucleic Acids Research</title><idno type="ISSN">0305-1048</idno><idno type="eISSN">1362-4962</idno><imprint><date when="2007">2007</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en"><p>Oligoribonuclease is the only RNase in <italic>Escherichia coli</italic> that is able to degrade RNA oligonucleotides five residues and shorter in length. Firmicutes including <italic>Bacillus subtilis</italic> do not have an Oligoribonuclease (Orn) homologous protein and it is not yet understood which proteins accomplish the equivalent function in these organisms. We had previously identified oligoribonucleases Orn from <italic>E. coli</italic> and its human homolog Sfn in a screen for proteins that are regulated by 3′-phosphoadenosine 5′-phosphate (pAp). Here, we identify YtqI as a potential functional analog of Orn through its interaction with pAp. YtqI degrades RNA oligonucleotides <italic>in vitro</italic> with preference for 3-mers. In addition, YtqI has pAp-phosphatase activity <italic>in vitro</italic>. In agreement with these data, YtqI is able to complement both <italic>orn</italic> and <italic>cysQ</italic> mutants in <italic>E. coli</italic>. An <italic>ytqI</italic> mutant in <italic>B. subtilis</italic> shows impairment of growth in the absence of cysteine, a phenotype resembling that of a <italic>cysQ</italic> mutant in <italic>E. coli</italic>. Phylogenetic distribution of YtqI, Orn and CysQ supports bifunctionality of YtqI.</p></div></front><back><div1 type="bibliography"><listBibl><biblStruct><analytic><author><name sortKey="Hollams, Em" uniqKey="Hollams E">EM Hollams</name></author><author><name sortKey="Giles, Km" uniqKey="Giles K">KM Giles</name></author><author><name sortKey="Thomson, Am" uniqKey="Thomson A">AM Thomson</name></author><author><name sortKey="Leedman, Pj" uniqKey="Leedman P">PJ Leedman</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Condon, C" uniqKey="Condon C">C Condon</name></author><author><name sortKey="Putzer, H" uniqKey="Putzer H">H Putzer</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Zuo, Y" uniqKey="Zuo Y">Y Zuo</name></author><author><name sortKey="Deutscher, Mp" uniqKey="Deutscher M">MP Deutscher</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Condon, C" uniqKey="Condon C">C 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<front><journal-meta><journal-id journal-id-type="nlm-ta">Nucleic Acids Res</journal-id><journal-id journal-id-type="iso-abbrev">Nucleic Acids Res</journal-id><journal-id journal-id-type="publisher-id">nar</journal-id><journal-id journal-id-type="hwp">nar</journal-id><journal-title-group><journal-title>Nucleic Acids Research</journal-title></journal-title-group><issn pub-type="ppub">0305-1048</issn><issn pub-type="epub">1362-4962</issn><publisher><publisher-name>Oxford University Press</publisher-name></publisher></journal-meta><article-meta><article-id pub-id-type="pmid">17586819</article-id><article-id pub-id-type="pmc">1935014</article-id><article-id pub-id-type="doi">10.1093/nar/gkm462</article-id><article-categories><subj-group subj-group-type="heading"><subject>Nucleic Acid Enzymes</subject></subj-group></article-categories><title-group><article-title>YtqI from <italic>Bacillus subtilis</italic> has both oligoribonuclease and pAp-phosphatase activity</article-title></title-group><contrib-group><contrib contrib-type="author"><name><surname>Mechold</surname><given-names>Undine</given-names></name><xref ref-type="aff" rid="AFF1"><sup>1</sup></xref><xref ref-type="corresp" rid="COR1">*</xref></contrib><contrib contrib-type="author"><name><surname>Fang</surname><given-names>Gang</given-names></name><xref ref-type="aff" rid="AFF1"><sup>1</sup></xref></contrib><contrib contrib-type="author"><name><surname>Ngo</surname><given-names>Saravuth</given-names></name><xref ref-type="aff" rid="AFF1"><sup>1</sup></xref></contrib><contrib contrib-type="author"><name><surname>Ogryzko</surname><given-names>Vasily</given-names></name><xref ref-type="aff" rid="AFF1"><sup>2</sup></xref></contrib><contrib contrib-type="author"><name><surname>Danchin</surname><given-names>Antoine</given-names></name><xref ref-type="aff" rid="AFF1"><sup>1</sup></xref></contrib></contrib-group><aff id="AFF1"><sup>1</sup>Institut Pasteur, URA 2171, Unité de Génétique des Génomes Bactériens, 75724 Paris Cedex 15 and<sup>2</sup>Institut Gustave Roussy, UMR 8126, Unité Interactions Moléculaires et Cancer, 94805 Villejuif, France</aff><author-notes><corresp id="COR1">*To whom correspondence should be addressed. <phone>33 140613870</phone><fax>33 145688948</fax><email>umechold@pasteur.fr</email></corresp></author-notes><pub-date pub-type="ppub"><month>7</month><year>2007</year></pub-date><pub-date pub-type="epub"><day>22</day><month>6</month><year>2007</year></pub-date><pub-date pub-type="pmc-release"><day>22</day><month>6</month><year>2007</year></pub-date><pmc-comment> PMC Release delay is 0 months and 0 days and was based on the
<volume>35</volume><issue>13</issue><fpage>4552</fpage><lpage>4561</lpage><history><date date-type="received"><day>2</day><month>4</month><year>2007</year></date><date date-type="rev-recd"><day>25</day><month>5</month><year>2007</year></date><date date-type="accepted"><day>25</day><month>5</month><year>2007</year></date></history><permissions><copyright-statement>© 2007 The Author(s)</copyright-statement><copyright-year>2007</copyright-year><license license-type="open-access" xlink:href="http://creativecommons.org/licenses/by-nc/2.0/uk/"><license-p><pmc-comment>CREATIVE COMMONS</pmc-comment>This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (<ext-link ext-link-type="uri" xlink:href="http://creativecommons.org/licenses/by-nc/2.0/uk/">http://creativecommons.org/licenses/by-nc/2.0/uk/</ext-link>) which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.</license-p></license></permissions><abstract><p>Oligoribonuclease is the only RNase in <italic>Escherichia coli</italic> that is able to degrade RNA oligonucleotides five residues and shorter in length. Firmicutes including <italic>Bacillus subtilis</italic> do not have an Oligoribonuclease (Orn) homologous protein and it is not yet understood which proteins accomplish the equivalent function in these organisms. We had previously identified oligoribonucleases Orn from <italic>E. coli</italic> and its human homolog Sfn in a screen for proteins that are regulated by 3′-phosphoadenosine 5′-phosphate (pAp). Here, we identify YtqI as a potential functional analog of Orn through its interaction with pAp. YtqI degrades RNA oligonucleotides <italic>in vitro</italic> with preference for 3-mers. In addition, YtqI has pAp-phosphatase activity <italic>in vitro</italic>. In agreement with these data, YtqI is able to complement both <italic>orn</italic> and <italic>cysQ</italic> mutants in <italic>E. coli</italic>. An <italic>ytqI</italic> mutant in <italic>B. subtilis</italic> shows impairment of growth in the absence of cysteine, a phenotype resembling that of a <italic>cysQ</italic> mutant in <italic>E. coli</italic>. Phylogenetic distribution of YtqI, Orn and CysQ supports bifunctionality of YtqI.</p></abstract></article-meta></front></pmc><affiliations><list><country><li>France</li></country><region><li>Île-de-France</li></region><settlement><li>Villejuif</li></settlement></list><tree><noCountry><name sortKey="Danchin, Antoine" sort="Danchin, Antoine" uniqKey="Danchin A" first="Antoine" last="Danchin">Antoine Danchin</name><name sortKey="Fang, Gang" sort="Fang, Gang" uniqKey="Fang G" first="Gang" last="Fang">Gang Fang</name><name sortKey="Mechold, Undine" sort="Mechold, Undine" uniqKey="Mechold U" first="Undine" last="Mechold">Undine Mechold</name><name sortKey="Ngo, Saravuth" sort="Ngo, Saravuth" uniqKey="Ngo S" first="Saravuth" last="Ngo">Saravuth Ngo</name></noCountry><country name="France"><region name="Île-de-France"><name sortKey="Ogryzko, Vasily" sort="Ogryzko, Vasily" uniqKey="Ogryzko V" first="Vasily" last="Ogryzko">Vasily Ogryzko</name></region></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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