The significance of distance and orientation of restriction endonuclease recognition sites in viral DNA genomes
Identifieur interne : 002B78 ( Main/Exploration ); précédent : 002B77; suivant : 002B79The significance of distance and orientation of restriction endonuclease recognition sites in viral DNA genomes
Auteurs : D. H. Krüger [Allemagne] ; D. Kupper ; A. Meisel ; M. Reuter ; C. SchroederSource :
- FEMS microbiology reviews [ 0168-6445 ] ; 1995.
Descripteurs français
- Pascal (Inist)
English descriptors
- KwdEn :
- Bacteriophage T3 (genetics), Bacteriophage T7 (genetics), Base Sequence, Binding Sites, DNA, DNA, Viral (metabolism), Deoxyribonucleases, Type II Site-Specific (chemistry), Deoxyribonucleases, Type III Site-Specific (chemistry), Endodeoxyribonuclease EcoRII, Genome, Viral, Molecular Sequence Data, Phage T3, Phage T7, Recognition, Restriction modification, Review, Sequence specificity, Site.
- 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.
Affiliations:
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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. 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H." last="Krüger">D. H. Krüger</name><affiliation wicri:level="1"><inist:fA14 i1="01"><s1>Humboldt univ., Charité medical school, inst. virology</s1><s2>10098 Berlin</s2><s3>DEU</s3></inist:fA14><country>Allemagne</country><wicri:noRegion>10098 Berlin</wicri:noRegion><placeName><settlement type="city">Berlin</settlement><region type="land" nuts="2">Berlin</region></placeName></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" type="main">FEMS microbiology reviews</title><title level="j" type="abbreviated">FEMS microbiol. rev.</title><idno type="ISSN">0168-6445</idno><imprint><date when="1995">1995</date></imprint></series></biblStruct></sourceDesc><seriesStmt><title level="j" type="main">FEMS microbiology reviews</title><title level="j" type="abbreviated">FEMS microbiol. rev.</title><idno type="ISSN">0168-6445</idno></seriesStmt></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</term><term>DNA, Viral (metabolism)</term><term>Deoxyribonucleases, Type II Site-Specific (chemistry)</term><term>Deoxyribonucleases, Type III Site-Specific (chemistry)</term><term>Endodeoxyribonuclease EcoRII</term><term>Genome, Viral</term><term>Molecular Sequence Data</term><term>Phage T3</term><term>Phage T7</term><term>Recognition</term><term>Restriction modification</term><term>Review</term><term>Sequence specificity</term><term>Site</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><keywords scheme="Pascal" xml:lang="fr"><term>Bactériophage T7</term><term>Bactériophage T3</term><term>DNA</term><term>Site</term><term>Reconnaissance</term><term>Spécificité séquence</term><term>Endodeoxyribonuclease EcoRII</term><term>Restriction modification</term><term>Article synthèse</term><term>Endodeoxyribonuclease EcoP15</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><affiliations><list><country><li>Allemagne</li></country><region><li>Berlin</li></region><settlement><li>Berlin</li></settlement></list><tree><noCountry><name sortKey="Kupper, D" sort="Kupper, D" uniqKey="Kupper D" first="D." last="Kupper">D. Kupper</name><name sortKey="Meisel, A" sort="Meisel, A" uniqKey="Meisel A" first="A." last="Meisel">A. Meisel</name><name sortKey="Reuter, M" sort="Reuter, M" uniqKey="Reuter M" first="M." last="Reuter">M. Reuter</name><name sortKey="Schroeder, C" sort="Schroeder, C" uniqKey="Schroeder C" first="C." last="Schroeder">C. Schroeder</name></noCountry><country name="Allemagne"><region name="Berlin"><name sortKey="Kruger, D H" sort="Kruger, D H" uniqKey="Kruger D" first="D. H." last="Krüger">D. H. Krüger</name></region></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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