The significance of distance and orientation of restriction endonuclease recognition sites in viral DNA genomes.
Identifieur interne : 000083 ( PubMed/Corpus ); précédent : 000082; suivant : 000084The significance of distance and orientation of restriction endonuclease recognition sites in viral DNA genomes.
Auteurs : D H Krüger ; D. Kupper ; A. Meisel ; M. Reuter ; C. SchroederSource :
- FEMS microbiology reviews [ 0168-6445 ] ; 1995.
English descriptors
- KwdEn :
- MESH :
- chemical , chemistry : Deoxyribonucleases, Type II Site-Specific, Deoxyribonucleases, Type III Site-Specific.
- chemical , metabolism : DNA, Viral.
- genetics : Bacteriophage T3, Bacteriophage T7.
- Base Sequence, Binding Sites, Genome, Viral, Molecular Sequence Data.
Abstract
Studies on phage T3 and T7 have shown that these viruses avoid restriction not only by the phage-coded Ocr (and S-adenosylmethionine hydrolase) protein functions or by the complete loss of specific recognition sites for certain restriction endonucleases from their genomes, but also that there are two additional modes: resistance towards EcoP15 (which recognizes a non-symmetrical sequence) is achieved by an identical orientation of all the recognition sites in the virus genome (strand bias) and in the case of EcoRII by the extreme reduction in number and thereby greater distance between recognition sites in the genome. These observations led to the discovery that certain restriction endonucleases require the simultaneous cooperation with two DNA sites for their function, as well as to the ongoing elucidation of the molecular modes of action of these enzymes. Type II and type III enzymes display fundamentally different mechanisms of protein-DNA interaction. For EcoRII we favor a model of simultaneous binding of two DNA sites to a dimeric enzyme molecule (neighbouring sites of the same, looping, DNA molecule or sites located on different DNA molecules), while the action of EcoP15 seems to conform with a tracking-collision model of two enzyme molecules bound to inversely oriented recognition sites. In addition to podoviruses T3 and T7, strand bias of recognition sequences for different type III DNA modification-restriction enzymes is also observed in the inoviruses M13, IKE and PF3.
PubMed: 7669344
Links to Exploration step
pubmed:7669344Le document en format XML
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Schroeder</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="1995">1995</date><idno type="RBID">pubmed:7669344</idno><idno type="pmid">7669344</idno><idno type="wicri:Area/PubMed/Corpus">000083</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">The significance of distance and orientation of restriction endonuclease recognition sites in viral DNA 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 Virology, Charité Medical School, Humboldt University, Berlin, Germany.</nlm:affiliation></affiliation></author><author><name sortKey="Kupper, D" sort="Kupper, D" uniqKey="Kupper D" first="D" last="Kupper">D. Kupper</name></author><author><name sortKey="Meisel, A" sort="Meisel, A" uniqKey="Meisel A" first="A" last="Meisel">A. Meisel</name></author><author><name sortKey="Reuter, M" sort="Reuter, M" uniqKey="Reuter M" first="M" last="Reuter">M. Reuter</name></author><author><name sortKey="Schroeder, C" sort="Schroeder, C" uniqKey="Schroeder C" first="C" last="Schroeder">C. Schroeder</name></author></analytic><series><title level="j">FEMS microbiology reviews</title><idno type="ISSN">0168-6445</idno><imprint><date when="1995" type="published">1995</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Bacteriophage T3 (genetics)</term><term>Bacteriophage T7 (genetics)</term><term>Base Sequence</term><term>Binding Sites</term><term>DNA, Viral (metabolism)</term><term>Deoxyribonucleases, Type II Site-Specific (chemistry)</term><term>Deoxyribonucleases, Type III Site-Specific (chemistry)</term><term>Genome, Viral</term><term>Molecular Sequence Data</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Deoxyribonucleases, Type II Site-Specific</term><term>Deoxyribonucleases, Type III Site-Specific</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>DNA, Viral</term></keywords><keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Bacteriophage T3</term><term>Bacteriophage T7</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Base Sequence</term><term>Binding Sites</term><term>Genome, Viral</term><term>Molecular Sequence Data</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Studies on phage T3 and T7 have shown that these viruses avoid restriction not only by the phage-coded Ocr (and S-adenosylmethionine hydrolase) protein functions or by the complete loss of specific recognition sites for certain restriction endonucleases from their genomes, but also that there are two additional modes: resistance towards EcoP15 (which recognizes a non-symmetrical sequence) is achieved by an identical orientation of all the recognition sites in the virus genome (strand bias) and in the case of EcoRII by the extreme reduction in number and thereby greater distance between recognition sites in the genome. These observations led to the discovery that certain restriction endonucleases require the simultaneous cooperation with two DNA sites for their function, as well as to the ongoing elucidation of the molecular modes of action of these enzymes. Type II and type III enzymes display fundamentally different mechanisms of protein-DNA interaction. For EcoRII we favor a model of simultaneous binding of two DNA sites to a dimeric enzyme molecule (neighbouring sites of the same, looping, DNA molecule or sites located on different DNA molecules), while the action of EcoP15 seems to conform with a tracking-collision model of two enzyme molecules bound to inversely oriented recognition sites. In addition to podoviruses T3 and T7, strand bias of recognition sequences for different type III DNA modification-restriction enzymes is also observed in the inoviruses M13, IKE and PF3.</div></front></TEI><pubmed><MedlineCitation Owner="NLM" Status="MEDLINE"><PMID Version="1">7669344</PMID><DateCreated><Year>1995</Year><Month>10</Month><Day>13</Day></DateCreated><DateCompleted><Year>1995</Year><Month>10</Month><Day>13</Day></DateCompleted><DateRevised><Year>2008</Year><Month>08</Month><Day>28</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">0168-6445</ISSN><JournalIssue CitedMedium="Print"><Volume>17</Volume><Issue>1-2</Issue><PubDate><Year>1995</Year><Month>Aug</Month></PubDate></JournalIssue><Title>FEMS microbiology reviews</Title><ISOAbbreviation>FEMS Microbiol. Rev.</ISOAbbreviation></Journal><ArticleTitle>The significance of distance and orientation of restriction endonuclease recognition sites in viral DNA genomes.</ArticleTitle><Pagination><MedlinePgn>177-84</MedlinePgn></Pagination><Abstract><AbstractText>Studies on phage T3 and T7 have shown that these viruses avoid restriction not only by the phage-coded Ocr (and S-adenosylmethionine hydrolase) protein functions or by the complete loss of specific recognition sites for certain restriction endonucleases from their genomes, but also that there are two additional modes: resistance towards EcoP15 (which recognizes a non-symmetrical sequence) is achieved by an identical orientation of all the recognition sites in the virus genome (strand bias) and in the case of EcoRII by the extreme reduction in number and thereby greater distance between recognition sites in the genome. These observations led to the discovery that certain restriction endonucleases require the simultaneous cooperation with two DNA sites for their function, as well as to the ongoing elucidation of the molecular modes of action of these enzymes. Type II and type III enzymes display fundamentally different mechanisms of protein-DNA interaction. For EcoRII we favor a model of simultaneous binding of two DNA sites to a dimeric enzyme molecule (neighbouring sites of the same, looping, DNA molecule or sites located on different DNA molecules), while the action of EcoP15 seems to conform with a tracking-collision model of two enzyme molecules bound to inversely oriented recognition sites. In addition to podoviruses T3 and T7, strand bias of recognition sequences for different type III DNA modification-restriction enzymes is also observed in the inoviruses M13, IKE and PF3.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Krüger</LastName><ForeName>D H</ForeName><Initials>DH</Initials><AffiliationInfo><Affiliation>Institute of Virology, Charité Medical School, Humboldt University, Berlin, Germany.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Kupper</LastName><ForeName>D</ForeName><Initials>D</Initials></Author><Author ValidYN="Y"><LastName>Meisel</LastName><ForeName>A</ForeName><Initials>A</Initials></Author><Author ValidYN="Y"><LastName>Reuter</LastName><ForeName>M</ForeName><Initials>M</Initials></Author><Author ValidYN="Y"><LastName>Schroeder</LastName><ForeName>C</ForeName><Initials>C</Initials></Author></AuthorList><Language>eng</Language><DataBankList CompleteYN="Y"><DataBank><DataBankName>GENBANK</DataBankName><AccessionNumberList><AccessionNumber>J02459</AccessionNumber><AccessionNumber>J02518</AccessionNumber><AccessionNumber>L10328</AccessionNumber><AccessionNumber>M11912</AccessionNumber><AccessionNumber>M14784</AccessionNumber><AccessionNumber>M17233</AccessionNumber><AccessionNumber>V01146</AccessionNumber><AccessionNumber>X00411</AccessionNumber><AccessionNumber>X02139</AccessionNumber><AccessionNumber>X17255</AccessionNumber></AccessionNumberList></DataBank></DataBankList><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType><PublicationType UI="D016454">Review</PublicationType></PublicationTypeList></Article><MedlineJournalInfo><Country>NETHERLANDS</Country><MedlineTA>FEMS Microbiol Rev</MedlineTA><NlmUniqueID>8902526</NlmUniqueID><ISSNLinking>0168-6445</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D004279">DNA, Viral</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.1.21.-</RegistryNumber><NameOfSubstance UI="C023451">endodeoxyribonuclease EcoP15I</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.1.21.4</RegistryNumber><NameOfSubstance UI="C046545">CCWGG-specific type II deoxyribonucleases</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.1.21.4</RegistryNumber><NameOfSubstance UI="D015252">Deoxyribonucleases, Type II Site-Specific</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.1.21.5</RegistryNumber><NameOfSubstance UI="D015263">Deoxyribonucleases, Type III Site-Specific</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName MajorTopicYN="N" UI="D017903">Bacteriophage T3</DescriptorName><QualifierName MajorTopicYN="Y" UI="Q000235">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName MajorTopicYN="N" UI="D017123">Bacteriophage T7</DescriptorName><QualifierName MajorTopicYN="Y" UI="Q000235">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName MajorTopicYN="N" UI="D001483">Base Sequence</DescriptorName></MeshHeading><MeshHeading><DescriptorName MajorTopicYN="N" UI="D001665">Binding Sites</DescriptorName></MeshHeading><MeshHeading><DescriptorName MajorTopicYN="N" UI="D004279">DNA, Viral</DescriptorName><QualifierName MajorTopicYN="Y" UI="Q000378">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName MajorTopicYN="N" UI="D015252">Deoxyribonucleases, Type II Site-Specific</DescriptorName><QualifierName MajorTopicYN="Y" UI="Q000737">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName MajorTopicYN="N" UI="D015263">Deoxyribonucleases, Type III Site-Specific</DescriptorName><QualifierName MajorTopicYN="Y" UI="Q000737">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName MajorTopicYN="Y" UI="D016679">Genome, Viral</DescriptorName></MeshHeading><MeshHeading><DescriptorName MajorTopicYN="N" UI="D008969">Molecular Sequence Data</DescriptorName></MeshHeading></MeshHeadingList><NumberOfReferences>34</NumberOfReferences></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>1995</Year><Month>8</Month><Day>1</Day></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>1995</Year><Month>8</Month><Day>1</Day><Hour>0</Hour><Minute>1</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>1995</Year><Month>8</Month><Day>1</Day><Hour>0</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">7669344</ArticleId><ArticleId IdType="pii">0168-6445(94)00066-2</ArticleId></ArticleIdList></PubmedData></pubmed></record>Pour manipuler ce document sous Unix (Dilib)
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