Binding of nucleic acids to E.coli RNase HI observed by NMR and CD spectroscopy
Identifieur interne : 004590 ( Main/Exploration ); précédent : 004589; suivant : 004591Binding of nucleic acids to E.coli RNase HI observed by NMR and CD spectroscopy
Auteurs : Yasushi Oda [Japon] ; Shigenori Iwa [Japon] ; Eiko Ohtsuka [Japon] ; Momoyo Ishikawa [Japon] ; Morio Ikehara [Japon] ; Haruki Nakamura [Japon]Source :
- Nucleic Acids Research [ 0305-1048 ] ; 1993.
Abstract
To clarify the mechanism by which the RNA portion of a DNA/RNA hybrid is specifically hydrolyzed by ribonuclease H (RNase H), the binding of a DNA/RNA hybrid, a DNA/DNA duplex, or an RNA/RNA duplex to RNase HI from Escherichia coli was investigated by 1H-15N heteronuclear NMR. Chemical shift changes of backbone amide resonances were monitored while the substrate, a hybrid 9-mer duplex, a DNA/DNA 12-mer duplex, or an RNA/RNA 12-mer duplex was titrated. The amino acid residues affected by the addition of each 12-mer duplex were almost identical to those affected by the substrate hybrid binding, and resided close to the active site of the enzyme. The results reveal that all the duplexes, hybrid-, DNA-, and RNA-duplex, bind to the enzyme. From the linewidth analysis of the resonance peaks, it was found that the exchange rates for the binding were different between the hybrid and the other duplexes. The NMR and CD data suggest that conformational changes occur in the enzyme and the hybrid duplex upon binding.
Url:
DOI: 10.1093/nar/21.20.4690
Affiliations:
Links toward previous steps (curation, corpus...)
- to stream Istex, to step Corpus: 000444
- to stream Istex, to step Curation: 000444
- to stream Istex, to step Checkpoint: 001C01
- to stream Main, to step Merge: 004656
- to stream Main, to step Curation: 004590
Le document en format XML
<record><TEI wicri:istexFullTextTei="biblStruct"><teiHeader><fileDesc><titleStmt><title>Binding of nucleic acids to E.coli RNase HI observed by NMR and CD spectroscopy</title><author><name sortKey="Oda, Yasushi" sort="Oda, Yasushi" uniqKey="Oda Y" first="Yasushi" last="Oda">Yasushi Oda</name></author><author><name sortKey="Iwa, Shigenori" sort="Iwa, Shigenori" uniqKey="Iwa S" first="Shigenori" last="Iwa">Shigenori Iwa</name></author><author><name sortKey="Ohtsuka, Eiko" sort="Ohtsuka, Eiko" uniqKey="Ohtsuka E" first="Eiko" last="Ohtsuka">Eiko Ohtsuka</name></author><author><name sortKey="Ishikawa, Momoyo" sort="Ishikawa, Momoyo" uniqKey="Ishikawa M" first="Momoyo" last="Ishikawa">Momoyo Ishikawa</name></author><author><name sortKey="Ikehara, Morio" sort="Ikehara, Morio" uniqKey="Ikehara M" first="Morio" last="Ikehara">Morio Ikehara</name></author><author><name sortKey="Nakamura, Haruki" sort="Nakamura, Haruki" uniqKey="Nakamura H" first="Haruki" last="Nakamura">Haruki Nakamura</name></author></titleStmt><publicationStmt><idno type="wicri:source">ISTEX</idno><idno type="RBID">ISTEX:05B5A39DCF077A53A7E216A81835B0EE9F309AF9</idno><date when="1993" year="1993">1993</date><idno type="doi">10.1093/nar/21.20.4690</idno><idno type="url">https://api.istex.fr/ark:/67375/HXZ-1KBBL7Q3-9/fulltext.pdf</idno><idno type="wicri:Area/Istex/Corpus">000444</idno><idno type="wicri:explorRef" wicri:stream="Istex" wicri:step="Corpus" wicri:corpus="ISTEX">000444</idno><idno type="wicri:Area/Istex/Curation">000444</idno><idno type="wicri:Area/Istex/Checkpoint">001C01</idno><idno type="wicri:explorRef" wicri:stream="Istex" wicri:step="Checkpoint">001C01</idno><idno type="wicri:doubleKey">0305-1048:1993:Oda Y:binding:of:nucleic</idno><idno type="wicri:Area/Main/Merge">004656</idno><idno type="wicri:Area/Main/Curation">004590</idno><idno type="wicri:Area/Main/Exploration">004590</idno></publicationStmt><sourceDesc><biblStruct><analytic><title level="a" type="main">Binding of nucleic acids to E.coli RNase HI observed by NMR and CD spectroscopy</title><author><name sortKey="Oda, Yasushi" sort="Oda, Yasushi" uniqKey="Oda Y" first="Yasushi" last="Oda">Yasushi Oda</name><affiliation wicri:level="1"><country xml:lang="fr">Japon</country><wicri:regionArea>Protein Engineering Research Institute, Furuedai, Suita, Osaka 565, Hokkaido University, Sapporo 060</wicri:regionArea><wicri:noRegion>Sapporo 060</wicri:noRegion></affiliation></author><author><name sortKey="Iwa, Shigenori" sort="Iwa, Shigenori" uniqKey="Iwa S" first="Shigenori" last="Iwa">Shigenori Iwa</name><affiliation wicri:level="1"><country xml:lang="fr">Japon</country><wicri:regionArea>Faculty of Pharmaceutical Sciences Hokkaido University, Sapporo 060</wicri:regionArea><wicri:noRegion>Sapporo 060</wicri:noRegion></affiliation></author><author><name sortKey="Ohtsuka, Eiko" sort="Ohtsuka, Eiko" uniqKey="Ohtsuka E" first="Eiko" last="Ohtsuka">Eiko Ohtsuka</name><affiliation wicri:level="1"><country xml:lang="fr">Japon</country><wicri:regionArea>Faculty of Pharmaceutical Sciences Hokkaido University, Sapporo 060</wicri:regionArea><wicri:noRegion>Sapporo 060</wicri:noRegion></affiliation></author><author><name sortKey="Ishikawa, Momoyo" sort="Ishikawa, Momoyo" uniqKey="Ishikawa M" first="Momoyo" last="Ishikawa">Momoyo Ishikawa</name><affiliation wicri:level="1"><country xml:lang="fr">Japon</country><wicri:regionArea>Protein Engineering Research Institute, Furuedai, Suita, Osaka 565, Hokkaido University, Sapporo 060</wicri:regionArea><wicri:noRegion>Sapporo 060</wicri:noRegion></affiliation></author><author><name sortKey="Ikehara, Morio" sort="Ikehara, Morio" uniqKey="Ikehara M" first="Morio" last="Ikehara">Morio Ikehara</name><affiliation wicri:level="1"><country xml:lang="fr">Japon</country><wicri:regionArea>Protein Engineering Research Institute, Furuedai, Suita, Osaka 565, Hokkaido University, Sapporo 060</wicri:regionArea><wicri:noRegion>Sapporo 060</wicri:noRegion></affiliation></author><author><name sortKey="Nakamura, Haruki" sort="Nakamura, Haruki" uniqKey="Nakamura H" first="Haruki" last="Nakamura">Haruki Nakamura</name><affiliation wicri:level="1"><country xml:lang="fr">Japon</country><wicri:regionArea>Protein Engineering Research Institute, Furuedai, Suita, Osaka 565, Hokkaido University, Sapporo 060</wicri:regionArea><wicri:noRegion>Sapporo 060</wicri:noRegion></affiliation><affiliation></affiliation></author></analytic><monogr></monogr><series><title level="j" type="main">Nucleic Acids Research</title><idno type="eISSN">1362-4962</idno><idno type="ISSN">0305-1048</idno><imprint><publisher>Oxford University Press</publisher><date type="published">1993</date><biblScope unit="vol">21</biblScope><biblScope unit="issue">20</biblScope><biblScope unit="page" from="4690">4690</biblScope><biblScope unit="page" to="4695">4695</biblScope></imprint><idno type="ISSN">0305-1048</idno></series></biblStruct></sourceDesc><seriesStmt><idno type="ISSN">0305-1048</idno></seriesStmt></fileDesc><profileDesc><textClass></textClass></profileDesc></teiHeader><front><div type="abstract">To clarify the mechanism by which the RNA portion of a DNA/RNA hybrid is specifically hydrolyzed by ribonuclease H (RNase H), the binding of a DNA/RNA hybrid, a DNA/DNA duplex, or an RNA/RNA duplex to RNase HI from Escherichia coli was investigated by 1H-15N heteronuclear NMR. Chemical shift changes of backbone amide resonances were monitored while the substrate, a hybrid 9-mer duplex, a DNA/DNA 12-mer duplex, or an RNA/RNA 12-mer duplex was titrated. The amino acid residues affected by the addition of each 12-mer duplex were almost identical to those affected by the substrate hybrid binding, and resided close to the active site of the enzyme. The results reveal that all the duplexes, hybrid-, DNA-, and RNA-duplex, bind to the enzyme. From the linewidth analysis of the resonance peaks, it was found that the exchange rates for the binding were different between the hybrid and the other duplexes. The NMR and CD data suggest that conformational changes occur in the enzyme and the hybrid duplex upon binding.</div></front></TEI><affiliations><list><country><li>Japon</li></country></list><tree><country name="Japon"><noRegion><name sortKey="Oda, Yasushi" sort="Oda, Yasushi" uniqKey="Oda Y" first="Yasushi" last="Oda">Yasushi Oda</name></noRegion><name sortKey="Ikehara, Morio" sort="Ikehara, Morio" uniqKey="Ikehara M" first="Morio" last="Ikehara">Morio Ikehara</name><name sortKey="Ishikawa, Momoyo" sort="Ishikawa, Momoyo" uniqKey="Ishikawa M" first="Momoyo" last="Ishikawa">Momoyo Ishikawa</name><name sortKey="Iwa, Shigenori" sort="Iwa, Shigenori" uniqKey="Iwa S" first="Shigenori" last="Iwa">Shigenori Iwa</name><name sortKey="Nakamura, Haruki" sort="Nakamura, Haruki" uniqKey="Nakamura H" first="Haruki" last="Nakamura">Haruki Nakamura</name><name sortKey="Ohtsuka, Eiko" sort="Ohtsuka, Eiko" uniqKey="Ohtsuka E" first="Eiko" last="Ohtsuka">Eiko Ohtsuka</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
EXPLOR_STEP=$WICRI_ROOT/Sante/explor/MersV1/Data/Main/Exploration
HfdSelect -h $EXPLOR_STEP/biblio.hfd -nk 004590 | SxmlIndent | more
Ou
HfdSelect -h $EXPLOR_AREA/Data/Main/Exploration/biblio.hfd -nk 004590 | SxmlIndent | more
Pour mettre un lien sur cette page dans le réseau Wicri
{{Explor lien
|wiki= Sante
|area= MersV1
|flux= Main
|étape= Exploration
|type= RBID
|clé= ISTEX:05B5A39DCF077A53A7E216A81835B0EE9F309AF9
|texte= Binding of nucleic acids to E.coli RNase HI observed by NMR and CD spectroscopy
}}
| This area was generated with Dilib version V0.6.33. |  |