Bacteriophage T4 Dam DNA-(N6-adenine)-methyltransferase. Processivity and orientation to the methylation target.
Identifieur interne : 002476 ( PubMed/Curation ); précédent : 002475; suivant : 002477Bacteriophage T4 Dam DNA-(N6-adenine)-methyltransferase. Processivity and orientation to the methylation target.
Auteurs : Victor V. Zinoviev [Russie] ; Alexey A. Evdokimov ; Ernst G. Malygin ; Samuel L. Schlagman ; Stanley HattmanSource :
- The Journal of biological chemistry [ 0021-9258 ] ; 2003.
Descripteurs français
- KwdFr :
- MESH :
- enzymologie : Bactériophage T4.
- métabolisme : Site-specific DNA-methyltransferase (adenine-specific).
- Amorces ADN, Cinétique, Protéines virales, Séquence nucléotidique.
English descriptors
- KwdEn :
- MESH :
- chemical , metabolism : Site-Specific DNA-Methyltransferase (Adenine-Specific).
- chemical : DNA Primers, Viral Proteins.
- enzymology : Bacteriophage T4.
- Base Sequence, Kinetics.
Abstract
We carried out steady state and pre-steady state (burst) kinetic analyses of the bacteriophage T4 Dam DNA-(N(6)-adenine)-methyltransferase (MTase)-mediated methyl group transfer from S-adenosyl-l-methionine (AdoMet) to Ade in oligonucleotide duplexes containing one or two specific GATC sites with different combinations of methylated and unmodified targets. We compared the results for ligated 40-mer duplexes with those of the mixtures of the two unligated duplexes used to generate the 40-mers. The salient results are as follows: (i) T4 Dam MTase modifies 40-mer duplexes in a processive fashion. (ii) During processive movement, T4 Dam rapidly exchanges product S-adenosyl-l-homocysteine (AdoHcy) for substrate AdoMet without dissociating from the DNA duplex. (iii) T4 Dam processivity is consistent with an ordered bi-bi mechanism AdoMet downward arrow DNA downward arrow DNA(Me) upward arrow AdoHcy upward arrow. However, in contrast to the steady state, here DNA(Me) upward arrow signifies departure from a methylated site GMTC upward arrow without physically dissociating from the DNA. (iv) Following methyl transfer at one site and linear diffusion to a hemimethylated site, a reconstituted T4 Dam-AdoMet complex rapidly reorients itself to the (productive) unmethylated strand. T4 Dam-AdoHcy cannot reorient at an enzymatically created GMTC site. (v) The inhibition potential of fully methylated sites 5'-GMTC/5'-GMTC is much lower for a long DNA molecule compared with short single-site duplexes.
DOI: 10.1074/jbc.M210769200
PubMed: 12501249
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Evdokimov</name></author><author><name sortKey="Malygin, Ernst G" sort="Malygin, Ernst G" uniqKey="Malygin E" first="Ernst G" last="Malygin">Ernst G. Malygin</name></author><author><name sortKey="Schlagman, Samuel L" sort="Schlagman, Samuel L" uniqKey="Schlagman S" first="Samuel L" last="Schlagman">Samuel L. Schlagman</name></author><author><name sortKey="Hattman, Stanley" sort="Hattman, Stanley" uniqKey="Hattman S" first="Stanley" last="Hattman">Stanley Hattman</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2003">2003</date><idno type="RBID">pubmed:12501249</idno><idno type="pmid">12501249</idno><idno type="doi">10.1074/jbc.M210769200</idno><idno type="wicri:Area/PubMed/Corpus">002476</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Corpus" wicri:corpus="PubMed">002476</idno><idno type="wicri:Area/PubMed/Curation">002476</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Curation">002476</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Bacteriophage T4 Dam DNA-(N6-adenine)-methyltransferase. Processivity and orientation to the methylation target.</title><author><name sortKey="Zinoviev, Victor V" sort="Zinoviev, Victor V" uniqKey="Zinoviev V" first="Victor V" last="Zinoviev">Victor V. Zinoviev</name><affiliation wicri:level="1"><nlm:affiliation>Institute of Molecular Biology, State Research Center of Virology and Biotechnology Vector, Novosibirsk 630559, Russia.</nlm:affiliation><country xml:lang="fr">Russie</country><wicri:regionArea>Institute of Molecular Biology, State Research Center of Virology and Biotechnology Vector, Novosibirsk 630559</wicri:regionArea></affiliation></author><author><name sortKey="Evdokimov, Alexey A" sort="Evdokimov, Alexey A" uniqKey="Evdokimov A" first="Alexey A" last="Evdokimov">Alexey A. Evdokimov</name></author><author><name sortKey="Malygin, Ernst G" sort="Malygin, Ernst G" uniqKey="Malygin E" first="Ernst G" last="Malygin">Ernst G. 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Schlagman</name></author><author><name sortKey="Hattman, Stanley" sort="Hattman, Stanley" uniqKey="Hattman S" first="Stanley" last="Hattman">Stanley Hattman</name></author></analytic><series><title level="j">The Journal of biological chemistry</title><idno type="ISSN">0021-9258</idno><imprint><date when="2003" type="published">2003</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Bacteriophage T4 (enzymology)</term><term>Base Sequence</term><term>DNA Primers</term><term>Kinetics</term><term>Site-Specific DNA-Methyltransferase (Adenine-Specific) (metabolism)</term><term>Viral Proteins</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Amorces ADN</term><term>Bactériophage T4 (enzymologie)</term><term>Cinétique</term><term>Protéines virales</term><term>Site-specific DNA-methyltransferase (adenine-specific) (métabolisme)</term><term>Séquence nucléotidique</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Site-Specific DNA-Methyltransferase (Adenine-Specific)</term></keywords><keywords scheme="MESH" type="chemical" xml:lang="en"><term>DNA Primers</term><term>Viral Proteins</term></keywords><keywords scheme="MESH" qualifier="enzymologie" xml:lang="fr"><term>Bactériophage T4</term></keywords><keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>Bacteriophage T4</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Site-specific DNA-methyltransferase (adenine-specific)</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Base Sequence</term><term>Kinetics</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Amorces ADN</term><term>Cinétique</term><term>Protéines virales</term><term>Séquence nucléotidique</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">We carried out steady state and pre-steady state (burst) kinetic analyses of the bacteriophage T4 Dam DNA-(N(6)-adenine)-methyltransferase (MTase)-mediated methyl group transfer from S-adenosyl-l-methionine (AdoMet) to Ade in oligonucleotide duplexes containing one or two specific GATC sites with different combinations of methylated and unmodified targets. We compared the results for ligated 40-mer duplexes with those of the mixtures of the two unligated duplexes used to generate the 40-mers. The salient results are as follows: (i) T4 Dam MTase modifies 40-mer duplexes in a processive fashion. (ii) During processive movement, T4 Dam rapidly exchanges product S-adenosyl-l-homocysteine (AdoHcy) for substrate AdoMet without dissociating from the DNA duplex. (iii) T4 Dam processivity is consistent with an ordered bi-bi mechanism AdoMet downward arrow DNA downward arrow DNA(Me) upward arrow AdoHcy upward arrow. However, in contrast to the steady state, here DNA(Me) upward arrow signifies departure from a methylated site GMTC upward arrow without physically dissociating from the DNA. (iv) Following methyl transfer at one site and linear diffusion to a hemimethylated site, a reconstituted T4 Dam-AdoMet complex rapidly reorients itself to the (productive) unmethylated strand. T4 Dam-AdoHcy cannot reorient at an enzymatically created GMTC site. (v) The inhibition potential of fully methylated sites 5'-GMTC/5'-GMTC is much lower for a long DNA molecule compared with short single-site duplexes.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">12501249</PMID><DateCompleted><Year>2003</Year><Month>04</Month><Day>23</Day></DateCompleted><DateRevised><Year>2007</Year><Month>11</Month><Day>14</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Print">0021-9258</ISSN><JournalIssue CitedMedium="Print"><Volume>278</Volume><Issue>10</Issue><PubDate><Year>2003</Year><Month>Mar</Month><Day>07</Day></PubDate></JournalIssue><Title>The Journal of biological chemistry</Title><ISOAbbreviation>J. Biol. Chem.</ISOAbbreviation></Journal><ArticleTitle>Bacteriophage T4 Dam DNA-(N6-adenine)-methyltransferase. Processivity and orientation to the methylation target.</ArticleTitle><Pagination><MedlinePgn>7829-33</MedlinePgn></Pagination><Abstract><AbstractText>We carried out steady state and pre-steady state (burst) kinetic analyses of the bacteriophage T4 Dam DNA-(N(6)-adenine)-methyltransferase (MTase)-mediated methyl group transfer from S-adenosyl-l-methionine (AdoMet) to Ade in oligonucleotide duplexes containing one or two specific GATC sites with different combinations of methylated and unmodified targets. We compared the results for ligated 40-mer duplexes with those of the mixtures of the two unligated duplexes used to generate the 40-mers. The salient results are as follows: (i) T4 Dam MTase modifies 40-mer duplexes in a processive fashion. (ii) During processive movement, T4 Dam rapidly exchanges product S-adenosyl-l-homocysteine (AdoHcy) for substrate AdoMet without dissociating from the DNA duplex. (iii) T4 Dam processivity is consistent with an ordered bi-bi mechanism AdoMet downward arrow DNA downward arrow DNA(Me) upward arrow AdoHcy upward arrow. However, in contrast to the steady state, here DNA(Me) upward arrow signifies departure from a methylated site GMTC upward arrow without physically dissociating from the DNA. (iv) Following methyl transfer at one site and linear diffusion to a hemimethylated site, a reconstituted T4 Dam-AdoMet complex rapidly reorients itself to the (productive) unmethylated strand. T4 Dam-AdoHcy cannot reorient at an enzymatically created GMTC site. (v) The inhibition potential of fully methylated sites 5'-GMTC/5'-GMTC is much lower for a long DNA molecule compared with short single-site duplexes.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Zinoviev</LastName><ForeName>Victor V</ForeName><Initials>VV</Initials><AffiliationInfo><Affiliation>Institute of Molecular Biology, State Research Center of Virology and Biotechnology Vector, Novosibirsk 630559, Russia.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Evdokimov</LastName><ForeName>Alexey A</ForeName><Initials>AA</Initials></Author><Author ValidYN="Y"><LastName>Malygin</LastName><ForeName>Ernst G</ForeName><Initials>EG</Initials></Author><Author ValidYN="Y"><LastName>Schlagman</LastName><ForeName>Samuel L</ForeName><Initials>SL</Initials></Author><Author ValidYN="Y"><LastName>Hattman</LastName><ForeName>Stanley</ForeName><Initials>S</Initials></Author></AuthorList><Language>eng</Language><GrantList CompleteYN="Y"><Grant><GrantID>GM29227</GrantID><Acronym>GM</Acronym><Agency>NIGMS NIH HHS</Agency><Country>United States</Country></Grant><Grant><GrantID>R03 TW05755</GrantID><Acronym>TW</Acronym><Agency>FIC NIH HHS</Agency><Country>United States</Country></Grant></GrantList><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType><PublicationType UI="D013487">Research Support, U.S. Gov't, P.H.S.</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2002</Year><Month>12</Month><Day>24</Day></ArticleDate></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>J Biol Chem</MedlineTA><NlmUniqueID>2985121R</NlmUniqueID><ISSNLinking>0021-9258</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D017931">DNA Primers</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D014764">Viral Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 2.1.1.72</RegistryNumber><NameOfSubstance UI="C058693">Dam methyltransferase</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 2.1.1.72</RegistryNumber><NameOfSubstance UI="D015265">Site-Specific DNA-Methyltransferase (Adenine-Specific)</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 2.1.1.72</RegistryNumber><NameOfSubstance UI="C499297">dam protein, Bacteriophage T4</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D017122" MajorTopicYN="N">Bacteriophage T4</DescriptorName><QualifierName UI="Q000201" MajorTopicYN="Y">enzymology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D001483" MajorTopicYN="N">Base Sequence</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D017931" MajorTopicYN="N">DNA Primers</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D007700" MajorTopicYN="N">Kinetics</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D015265" MajorTopicYN="N">Site-Specific DNA-Methyltransferase (Adenine-Specific)</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D014764" MajorTopicYN="N">Viral Proteins</DescriptorName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>2002</Year><Month>12</Month><Day>27</Day><Hour>4</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2003</Year><Month>4</Month><Day>24</Day><Hour>5</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2002</Year><Month>12</Month><Day>27</Day><Hour>4</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">12501249</ArticleId><ArticleId IdType="doi">10.1074/jbc.M210769200</ArticleId><ArticleId IdType="pii">M210769200</ArticleId></ArticleIdList></PubmedData></pubmed></record>Pour manipuler ce document sous Unix (Dilib)
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