The significance of distance and orientation of restriction endonuclease recognition sites in viral DNA genomes
Identifieur interne :
000947 ( PascalFrancis/Curation );
précédent :
000946;
suivant :
000948
The 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.
RBID : Pascal:95-0509893
Descripteurs français
English descriptors
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.
| pA |
| A01 | 01 | 1 | | @0 0168-6445 |
|---|
| A03 | | 1 | | @0 FEMS microbiol. rev. |
|---|
| A05 | | | | @2 17 |
|---|
| A06 | | | | @2 1-2 |
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| A08 | 01 | 1 | ENG | @1 The significance of distance and orientation of restriction endonuclease recognition sites in viral DNA genomes |
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| A11 | 01 | 1 | | @1 KRÜGER (D. H.) |
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| A11 | 02 | 1 | | @1 KUPPER (D.) |
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| A11 | 03 | 1 | | @1 MEISEL (A.) |
|---|
| A11 | 04 | 1 | | @1 REUTER (M.) |
|---|
| A11 | 05 | 1 | | @1 SCHROEDER (C.) |
|---|
| A12 | 01 | 1 | | @1 DEHO (Gianni) @9 ed. |
|---|
| A12 | 02 | 1 | | @1 BLÄSI (Udo) @9 ed. |
|---|
| A14 | 01 | | | @1 Humboldt univ., Charité medical school, inst. virology @2 10098 Berlin @3 DEU |
|---|
| A15 | 01 | | | @1 Univ. Milano, dip. genetica biologia microrganismi @2 20133 Milan @3 ITA @Z 1 aut. |
|---|
| A18 | 01 | 1 | | @1 European Molecular Biology Organization @2 Heidelberg @3 DEU @9 patr. |
|---|
| A18 | 02 | 1 | | @1 Federation of European Microbiological Societies @2 Basel @3 CHE @9 patr. |
|---|
| A20 | | | | @1 177-184 |
|---|
| A21 | | | | @1 1995 |
|---|
| A23 | 01 | | | @0 ENG |
|---|
| A43 | 01 | | | @1 INIST @2 17567D @5 354000054393940180 |
|---|
| A44 | | | | @0 0000 |
|---|
| A45 | | | | @0 34 ref. |
|---|
| A47 | 01 | 1 | | @0 95-0509893 |
|---|
| A60 | | | | @1 P @2 C |
|---|
| A61 | | | | @0 A |
|---|
| A64 | 01 | 1 | | @0 FEMS microbiology reviews |
|---|
| A66 | 01 | | | @0 NLD |
|---|
| C01 | 01 | | ENG | @0 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. |
|---|
| C02 | 01 | X | | @0 002A05C05 |
|---|
| C03 | 01 | X | FRE | @0 Bactériophage T7 @2 NW @5 01 |
|---|
| C03 | 01 | X | ENG | @0 Phage T7 @2 NW @5 01 |
|---|
| C03 | 01 | X | SPA | @0 Phage T7 @2 NW @5 01 |
|---|
| C03 | 02 | X | FRE | @0 Bactériophage T3 @2 NW @5 02 |
|---|
| C03 | 02 | X | ENG | @0 Phage T3 @2 NW @5 02 |
|---|
| C03 | 02 | X | SPA | @0 Phage T3 @2 NW @5 02 |
|---|
| C03 | 03 | X | FRE | @0 DNA @5 04 |
|---|
| C03 | 03 | X | ENG | @0 DNA @5 04 |
|---|
| C03 | 03 | X | SPA | @0 DNA @5 04 |
|---|
| C03 | 04 | X | FRE | @0 Site @5 05 |
|---|
| C03 | 04 | X | ENG | @0 Site @5 05 |
|---|
| C03 | 04 | X | GER | @0 Standort @5 05 |
|---|
| C03 | 04 | X | SPA | @0 Sitio @5 05 |
|---|
| C03 | 05 | X | FRE | @0 Reconnaissance @5 06 |
|---|
| C03 | 05 | X | ENG | @0 Recognition @5 06 |
|---|
| C03 | 05 | X | SPA | @0 Reconocimiento @5 06 |
|---|
| C03 | 06 | X | FRE | @0 Spécificité séquence @5 07 |
|---|
| C03 | 06 | X | ENG | @0 Sequence specificity @5 07 |
|---|
| C03 | 06 | X | SPA | @0 Espicificidad secuencia @5 07 |
|---|
| C03 | 07 | X | FRE | @0 Endodeoxyribonuclease EcoRII @2 FE @5 08 |
|---|
| C03 | 07 | X | ENG | @0 Endodeoxyribonuclease EcoRII @2 FE @5 08 |
|---|
| C03 | 07 | X | SPA | @0 Endodeoxyribonuclease EcoRII @2 FE @5 08 |
|---|
| C03 | 08 | X | FRE | @0 Restriction modification @5 09 |
|---|
| C03 | 08 | X | ENG | @0 Restriction modification @5 09 |
|---|
| C03 | 08 | X | SPA | @0 Restricción modificacíon @5 09 |
|---|
| C03 | 09 | X | FRE | @0 Article synthèse @5 68 |
|---|
| C03 | 09 | X | ENG | @0 Review @5 68 |
|---|
| C03 | 09 | X | SPA | @0 Artículo síntesis @5 68 |
|---|
| C03 | 10 | X | FRE | @0 Endodeoxyribonuclease EcoP15 @2 FE @4 INC @5 91 |
|---|
| C07 | 01 | X | FRE | @0 Podoviridae @2 NW |
|---|
| C07 | 01 | X | ENG | @0 Podoviridae @2 NW |
|---|
| C07 | 01 | X | SPA | @0 Podoviridae @2 NW |
|---|
| C07 | 02 | X | FRE | @0 Bactériophage @2 NW |
|---|
| C07 | 02 | X | ENG | @0 Phage @2 NW |
|---|
| C07 | 02 | X | SPA | @0 Phage @2 NW |
|---|
| C07 | 03 | X | FRE | @0 Virus @2 NW |
|---|
| C07 | 03 | X | ENG | @0 Virus @2 NW |
|---|
| C07 | 03 | X | SPA | @0 Virus @2 NW |
|---|
| C07 | 04 | X | FRE | @0 Esterases @2 FE |
|---|
| C07 | 04 | X | ENG | @0 Esterases @2 FE |
|---|
| C07 | 04 | X | SPA | @0 Esterases @2 FE |
|---|
| C07 | 05 | X | FRE | @0 Hydrolases @2 FE |
|---|
| C07 | 05 | X | ENG | @0 Hydrolases @2 FE |
|---|
| C07 | 05 | X | SPA | @0 Hydrolases @2 FE |
|---|
| C07 | 06 | X | FRE | @0 Enzyme |
|---|
| C07 | 06 | X | ENG | @0 Enzyme |
|---|
| C07 | 06 | X | SPA | @0 Enzima |
|---|
| N21 | | | | @1 289 |
|---|
|
|---|
| pR |
| A30 | 01 | 1 | ENG | @1 EMBO-FEMS meeting on bacterial viruses: molecular biology and biotechnology @3 Gargnano ITA @4 1994-03-27 |
|---|
|
|---|
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Pascal:95-0509893
Le document en format XML
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<author><name sortKey="Kruger, D H" sort="Kruger, D H" uniqKey="Kruger D" first="D. 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>
</affiliation><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>
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</publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en" level="a">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 wicri:level="1"><inist:fA14 i1="01"><s1>Humboldt univ., Charité medical school, inst. virology</s1>
<s2>10098 Berlin</s2>
<s3>DEU</s3>
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</affiliation><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><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><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><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>DNA</term>
<term>Endodeoxyribonuclease EcoRII</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="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><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><inist><standard h6="B"><pA><fA01 i1="01" i2="1"><s0>0168-6445</s0>
</fA01><fA03 i2="1"><s0>FEMS microbiol. rev.</s0>
</fA03><fA06><s2>1-2</s2>
</fA06><fA08 i1="01" i2="1" l="ENG"><s1>The significance of distance and orientation of restriction endonuclease recognition sites in viral DNA genomes</s1>
</fA08><fA11 i1="01" i2="1"><s1>KRÜGER (D. H.)</s1>
</fA11><fA11 i1="02" i2="1"><s1>KUPPER (D.)</s1>
</fA11><fA11 i1="03" i2="1"><s1>MEISEL (A.)</s1>
</fA11><fA11 i1="04" i2="1"><s1>REUTER (M.)</s1>
</fA11><fA11 i1="05" i2="1"><s1>SCHROEDER (C.)</s1>
</fA11><fA12 i1="01" i2="1"><s1>DEHO (Gianni)</s1>
<s9>ed.</s9>
</fA12><fA12 i1="02" i2="1"><s1>BLÄSI (Udo)</s1>
<s9>ed.</s9>
</fA12><fA14 i1="01"><s1>Humboldt univ., Charité medical school, inst. virology</s1>
<s2>10098 Berlin</s2>
<s3>DEU</s3>
</fA14><fA15 i1="01"><s1>Univ. Milano, dip. genetica biologia microrganismi</s1>
<s2>20133 Milan</s2>
<s3>ITA</s3>
<sZ>1 aut.</sZ>
</fA15><fA18 i1="01" i2="1"><s1>European Molecular Biology Organization</s1>
<s2>Heidelberg</s2>
<s3>DEU</s3>
<s9>patr.</s9>
</fA18><fA18 i1="02" i2="1"><s1>Federation of European Microbiological Societies</s1>
<s2>Basel</s2>
<s3>CHE</s3>
<s9>patr.</s9>
</fA18><fA20><s1>177-184</s1>
</fA20><fA21><s1>1995</s1>
</fA21><fA23 i1="01"><s0>ENG</s0>
</fA23><fA43 i1="01"><s1>INIST</s1>
<s2>17567D</s2>
<s5>354000054393940180</s5>
</fA43><fA44><s0>0000</s0>
</fA44><fA45><s0>34 ref.</s0>
</fA45><fA47 i1="01" i2="1"><s0>95-0509893</s0>
</fA47><fA60><s1>P</s1>
<s2>C</s2>
</fA60><fA64 i1="01" i2="1"><s0>FEMS microbiology reviews</s0>
</fA64><fA66 i1="01"><s0>NLD</s0>
</fA66><fC01 i1="01" l="ENG"><s0>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.</s0>
</fC01><fC02 i1="01" i2="X"><s0>002A05C05</s0>
</fC02><fC03 i1="01" i2="X" l="FRE"><s0>Bactériophage T7</s0>
<s2>NW</s2>
<s5>01</s5>
</fC03><fC03 i1="01" i2="X" l="ENG"><s0>Phage T7</s0>
<s2>NW</s2>
<s5>01</s5>
</fC03><fC03 i1="01" i2="X" l="SPA"><s0>Phage T7</s0>
<s2>NW</s2>
<s5>01</s5>
</fC03><fC03 i1="02" i2="X" l="FRE"><s0>Bactériophage T3</s0>
<s2>NW</s2>
<s5>02</s5>
</fC03><fC03 i1="02" i2="X" l="ENG"><s0>Phage T3</s0>
<s2>NW</s2>
<s5>02</s5>
</fC03><fC03 i1="02" i2="X" l="SPA"><s0>Phage T3</s0>
<s2>NW</s2>
<s5>02</s5>
</fC03><fC03 i1="03" i2="X" l="FRE"><s0>DNA</s0>
<s5>04</s5>
</fC03><fC03 i1="03" i2="X" l="ENG"><s0>DNA</s0>
<s5>04</s5>
</fC03><fC03 i1="03" i2="X" l="SPA"><s0>DNA</s0>
<s5>04</s5>
</fC03><fC03 i1="04" i2="X" l="FRE"><s0>Site</s0>
<s5>05</s5>
</fC03><fC03 i1="04" i2="X" l="ENG"><s0>Site</s0>
<s5>05</s5>
</fC03><fC03 i1="04" i2="X" l="GER"><s0>Standort</s0>
<s5>05</s5>
</fC03><fC03 i1="04" i2="X" l="SPA"><s0>Sitio</s0>
<s5>05</s5>
</fC03><fC03 i1="05" i2="X" l="FRE"><s0>Reconnaissance</s0>
<s5>06</s5>
</fC03><fC03 i1="05" i2="X" l="ENG"><s0>Recognition</s0>
<s5>06</s5>
</fC03><fC03 i1="05" i2="X" l="SPA"><s0>Reconocimiento</s0>
<s5>06</s5>
</fC03><fC03 i1="06" i2="X" l="FRE"><s0>Spécificité séquence</s0>
<s5>07</s5>
</fC03><fC03 i1="06" i2="X" l="ENG"><s0>Sequence specificity</s0>
<s5>07</s5>
</fC03><fC03 i1="06" i2="X" l="SPA"><s0>Espicificidad secuencia</s0>
<s5>07</s5>
</fC03><fC03 i1="07" i2="X" l="FRE"><s0>Endodeoxyribonuclease EcoRII</s0>
<s2>FE</s2>
<s5>08</s5>
</fC03><fC03 i1="07" i2="X" l="ENG"><s0>Endodeoxyribonuclease EcoRII</s0>
<s2>FE</s2>
<s5>08</s5>
</fC03><fC03 i1="07" i2="X" l="SPA"><s0>Endodeoxyribonuclease EcoRII</s0>
<s2>FE</s2>
<s5>08</s5>
</fC03><fC03 i1="08" i2="X" l="FRE"><s0>Restriction modification</s0>
<s5>09</s5>
</fC03><fC03 i1="08" i2="X" l="ENG"><s0>Restriction modification</s0>
<s5>09</s5>
</fC03><fC03 i1="08" i2="X" l="SPA"><s0>Restricción modificacíon</s0>
<s5>09</s5>
</fC03><fC03 i1="09" i2="X" l="FRE"><s0>Article synthèse</s0>
<s5>68</s5>
</fC03><fC03 i1="09" i2="X" l="ENG"><s0>Review</s0>
<s5>68</s5>
</fC03><fC03 i1="09" i2="X" l="SPA"><s0>Artículo síntesis</s0>
<s5>68</s5>
</fC03><fC03 i1="10" i2="X" l="FRE"><s0>Endodeoxyribonuclease EcoP15</s0>
<s2>FE</s2>
<s4>INC</s4>
<s5>91</s5>
</fC03><fC07 i1="01" i2="X" l="FRE"><s0>Podoviridae</s0>
<s2>NW</s2>
</fC07><fC07 i1="01" i2="X" l="ENG"><s0>Podoviridae</s0>
<s2>NW</s2>
</fC07><fC07 i1="01" i2="X" l="SPA"><s0>Podoviridae</s0>
<s2>NW</s2>
</fC07><fC07 i1="02" i2="X" l="FRE"><s0>Bactériophage</s0>
<s2>NW</s2>
</fC07><fC07 i1="02" i2="X" l="ENG"><s0>Phage</s0>
<s2>NW</s2>
</fC07><fC07 i1="02" i2="X" l="SPA"><s0>Phage</s0>
<s2>NW</s2>
</fC07><fC07 i1="03" i2="X" l="FRE"><s0>Virus</s0>
<s2>NW</s2>
</fC07><fC07 i1="03" i2="X" l="ENG"><s0>Virus</s0>
<s2>NW</s2>
</fC07><fC07 i1="03" i2="X" l="SPA"><s0>Virus</s0>
<s2>NW</s2>
</fC07><fC07 i1="04" i2="X" l="FRE"><s0>Esterases</s0>
<s2>FE</s2>
</fC07><fC07 i1="04" i2="X" l="ENG"><s0>Esterases</s0>
<s2>FE</s2>
</fC07><fC07 i1="04" i2="X" l="SPA"><s0>Esterases</s0>
<s2>FE</s2>
</fC07><fC07 i1="05" i2="X" l="FRE"><s0>Hydrolases</s0>
<s2>FE</s2>
</fC07><fC07 i1="05" i2="X" l="ENG"><s0>Hydrolases</s0>
<s2>FE</s2>
</fC07><fC07 i1="05" i2="X" l="SPA"><s0>Hydrolases</s0>
<s2>FE</s2>
</fC07><fC07 i1="06" i2="X" l="FRE"><s0>Enzyme</s0>
</fC07><fC07 i1="06" i2="X" l="ENG"><s0>Enzyme</s0>
</fC07><fC07 i1="06" i2="X" l="SPA"><s0>Enzima</s0>
</fC07><fN21><s1>289</s1>
</fN21><pR><fA30 i1="01" i2="1" l="ENG"><s1>EMBO-FEMS meeting on bacterial viruses: molecular biology and biotechnology</s1>
<s3>Gargnano ITA</s3>
<s4>1994-03-27</s4>
</fA30>
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