Avoidance of DNA methylation. A virus-encoded methylase inhibitor and evidence for counterselection of methylase recognition sites in viral genomes.
Identifieur interne : 000088 ( PubMed/Corpus ); précédent : 000087; suivant : 000089Avoidance of DNA methylation. A virus-encoded methylase inhibitor and evidence for counterselection of methylase recognition sites in viral genomes.
Auteurs : D H Krüger ; C. Schroeder ; M. Santibanez-Koref ; M. ReuterSource :
- Cell biophysics [ 0163-4992 ]
English descriptors
- KwdEn :
- MESH :
- chemical , antagonists & inhibitors : DNA Modification Methylases.
- chemical , genetics : Hydrolases.
- chemical , metabolism : DNA Modification Methylases, DNA, Viral, Hydrolases.
- enzymology : T-Phages.
- genetics : T-Phages.
- metabolism : T-Phages.
- Base Sequence, Genes, Viral, Methylation.
Abstract
The ocr+ gene of bacterial virus T7 codes for the first protein recognized to inhibit a specific group of DNA methylases. The recognition sequences of several other DNA methylases, not susceptible to Ocr inhibition, are significantly suppressed in the virus genome. The bacterial virus T3 encodes an Ado-Met hydrolase, destroying the methyl donor and causing T3 DNA to be totally unmethylated. These observations could stimulate analogous investigations into the regulation of DNA methylation patterns of eukaryotic viruses and cells. For instance, an underrepresentation of methylation sites (5'-CG) is also true for animal DNA viruses. Moreover, we were able to disclose some novel properties of DNA restriction-modification enzymes concerning the protection of DNA recognition sequences in which only one strand can be methylated (e.g., type III enzyme EcoP15) and the primary resistance of (unmethylated) DNA recognition sites towards type II restriction endonuclease EcoRII.
PubMed: 2476230
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pubmed:2476230Le document en format XML
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Reuter</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="????"><PubDate><MedlineDate>1989 Aug-Oct</MedlineDate></PubDate></date><idno type="RBID">pubmed:2476230</idno><idno type="pmid">2476230</idno><idno type="wicri:Area/PubMed/Corpus">000088</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Avoidance of DNA methylation. A virus-encoded methylase inhibitor and evidence for counterselection of methylase recognition sites in viral genomes.</title><author><name sortKey="Kruger, D H" sort="Kruger, D H" uniqKey="Kruger D" first="D H" last="Krüger">D H Krüger</name><affiliation><nlm:affiliation>Institute of Medical Virology, Humboldt University School of Medicine, Charité, Berlin, German Democratic Republic.</nlm:affiliation></affiliation></author><author><name sortKey="Schroeder, C" sort="Schroeder, C" uniqKey="Schroeder C" first="C" last="Schroeder">C. Schroeder</name></author><author><name sortKey="Santibanez Koref, M" sort="Santibanez Koref, M" uniqKey="Santibanez Koref M" first="M" last="Santibanez-Koref">M. Santibanez-Koref</name></author><author><name sortKey="Reuter, M" sort="Reuter, M" uniqKey="Reuter M" first="M" last="Reuter">M. Reuter</name></author></analytic><series><title level="j">Cell biophysics</title><idno type="ISSN">0163-4992</idno></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Base Sequence</term><term>DNA Modification Methylases (antagonists & inhibitors)</term><term>DNA Modification Methylases (metabolism)</term><term>DNA, Viral (metabolism)</term><term>Genes, Viral</term><term>Hydrolases (genetics)</term><term>Hydrolases (metabolism)</term><term>Methylation</term><term>T-Phages (enzymology)</term><term>T-Phages (genetics)</term><term>T-Phages (metabolism)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="antagonists & inhibitors" xml:lang="en"><term>DNA Modification Methylases</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Hydrolases</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>DNA Modification Methylases</term><term>DNA, Viral</term><term>Hydrolases</term></keywords><keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>T-Phages</term></keywords><keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>T-Phages</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>T-Phages</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Base Sequence</term><term>Genes, Viral</term><term>Methylation</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">The ocr+ gene of bacterial virus T7 codes for the first protein recognized to inhibit a specific group of DNA methylases. The recognition sequences of several other DNA methylases, not susceptible to Ocr inhibition, are significantly suppressed in the virus genome. The bacterial virus T3 encodes an Ado-Met hydrolase, destroying the methyl donor and causing T3 DNA to be totally unmethylated. These observations could stimulate analogous investigations into the regulation of DNA methylation patterns of eukaryotic viruses and cells. For instance, an underrepresentation of methylation sites (5'-CG) is also true for animal DNA viruses. Moreover, we were able to disclose some novel properties of DNA restriction-modification enzymes concerning the protection of DNA recognition sequences in which only one strand can be methylated (e.g., type III enzyme EcoP15) and the primary resistance of (unmethylated) DNA recognition sites towards type II restriction endonuclease EcoRII.</div></front></TEI><pubmed><MedlineCitation Owner="NLM" Status="MEDLINE"><PMID Version="1">2476230</PMID><DateCreated><Year>1989</Year><Month>10</Month><Day>26</Day></DateCreated><DateCompleted><Year>1989</Year><Month>10</Month><Day>26</Day></DateCompleted><DateRevised><Year>2006</Year><Month>11</Month><Day>15</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">0163-4992</ISSN><JournalIssue CitedMedium="Print"><Volume>15</Volume><Issue>1-2</Issue><PubDate><MedlineDate>1989 Aug-Oct</MedlineDate></PubDate></JournalIssue><Title>Cell biophysics</Title><ISOAbbreviation>Cell Biophys.</ISOAbbreviation></Journal><ArticleTitle>Avoidance of DNA methylation. A virus-encoded methylase inhibitor and evidence for counterselection of methylase recognition sites in viral genomes.</ArticleTitle><Pagination><MedlinePgn>87-95</MedlinePgn></Pagination><Abstract><AbstractText>The ocr+ gene of bacterial virus T7 codes for the first protein recognized to inhibit a specific group of DNA methylases. The recognition sequences of several other DNA methylases, not susceptible to Ocr inhibition, are significantly suppressed in the virus genome. The bacterial virus T3 encodes an Ado-Met hydrolase, destroying the methyl donor and causing T3 DNA to be totally unmethylated. These observations could stimulate analogous investigations into the regulation of DNA methylation patterns of eukaryotic viruses and cells. For instance, an underrepresentation of methylation sites (5'-CG) is also true for animal DNA viruses. Moreover, we were able to disclose some novel properties of DNA restriction-modification enzymes concerning the protection of DNA recognition sequences in which only one strand can be methylated (e.g., type III enzyme EcoP15) and the primary resistance of (unmethylated) DNA recognition sites towards type II restriction endonuclease EcoRII.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Krüger</LastName><ForeName>D H</ForeName><Initials>DH</Initials><AffiliationInfo><Affiliation>Institute of Medical Virology, Humboldt University School of Medicine, Charité, Berlin, German Democratic Republic.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Schroeder</LastName><ForeName>C</ForeName><Initials>C</Initials></Author><Author ValidYN="Y"><LastName>Santibanez-Koref</LastName><ForeName>M</ForeName><Initials>M</Initials></Author><Author ValidYN="Y"><LastName>Reuter</LastName><ForeName>M</ForeName><Initials>M</Initials></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D016454">Review</PublicationType></PublicationTypeList></Article><MedlineJournalInfo><Country>UNITED STATES</Country><MedlineTA>Cell Biophys</MedlineTA><NlmUniqueID>8002185</NlmUniqueID><ISSNLinking>0163-4992</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D004279">DNA, Viral</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 2.1.1.-</RegistryNumber><NameOfSubstance UI="D015254">DNA Modification Methylases</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.-</RegistryNumber><NameOfSubstance UI="D006867">Hydrolases</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.3.1.2</RegistryNumber><NameOfSubstance UI="C019614">adenosylmethionine hydrolase</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName MajorTopicYN="N" UI="D001483">Base Sequence</DescriptorName></MeshHeading><MeshHeading><DescriptorName MajorTopicYN="N" UI="D015254">DNA Modification Methylases</DescriptorName><QualifierName MajorTopicYN="Y" UI="Q000037">antagonists & inhibitors</QualifierName><QualifierName MajorTopicYN="N" UI="Q000378">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName MajorTopicYN="N" UI="D004279">DNA, Viral</DescriptorName><QualifierName MajorTopicYN="Y" UI="Q000378">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName MajorTopicYN="Y" UI="D005814">Genes, Viral</DescriptorName></MeshHeading><MeshHeading><DescriptorName MajorTopicYN="N" UI="D006867">Hydrolases</DescriptorName><QualifierName MajorTopicYN="N" UI="Q000235">genetics</QualifierName><QualifierName MajorTopicYN="Y" UI="Q000378">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName MajorTopicYN="N" UI="D008745">Methylation</DescriptorName></MeshHeading><MeshHeading><DescriptorName MajorTopicYN="N" UI="D013604">T-Phages</DescriptorName><QualifierName MajorTopicYN="N" UI="Q000201">enzymology</QualifierName><QualifierName MajorTopicYN="Y" UI="Q000235">genetics</QualifierName><QualifierName MajorTopicYN="N" UI="Q000378">metabolism</QualifierName></MeshHeading></MeshHeadingList><NumberOfReferences>38</NumberOfReferences></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>1989</Year><Month>8</Month><Day>1</Day></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>1989</Year><Month>8</Month><Day>1</Day><Hour>0</Hour><Minute>1</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>1989</Year><Month>8</Month><Day>1</Day><Hour>0</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">2476230</ArticleId></ArticleIdList></PubmedData></pubmed></record>Pour manipuler ce document sous Unix (Dilib)
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