Binding of nucleic acids to E.coli RNase HI observed by NMR and CD spectroscopy
Identifieur interne : 000444 ( Istex/Curation ); précédent : 000443; suivant : 000445Binding 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.
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DOI: 10.1093/nar/21.20.4690
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060</wicri:regionArea></affiliation></author><author><name sortKey="Ikehara, Morio" sort="Ikehara, Morio" uniqKey="Ikehara M" first="Morio" last="Ikehara">Morio Ikehara</name><affiliation wicri:level="1"><mods:affiliation>Protein Engineering Research Institute, Furuedai, Suita, Osaka 565, Hokkaido University, Sapporo 060, Japan</mods:affiliation><country xml:lang="fr">Japon</country><wicri:regionArea>Protein Engineering Research Institute, Furuedai, Suita, Osaka 565, Hokkaido University, Sapporo 060</wicri:regionArea></affiliation></author><author><name sortKey="Nakamura, Haruki" sort="Nakamura, Haruki" uniqKey="Nakamura H" first="Haruki" last="Nakamura">Haruki Nakamura</name><affiliation wicri:level="1"><mods:affiliation>Protein Engineering Research Institute, Furuedai, Suita, Osaka 565, Hokkaido University, Sapporo 060, Japan</mods:affiliation><country xml:lang="fr">Japon</country><wicri:regionArea>Protein Engineering Research Institute, Furuedai, Suita, Osaka 565, Hokkaido 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Ohtsuka</name><affiliation wicri:level="1"><mods:affiliation>Faculty of Pharmaceutical Sciences Hokkaido University, Sapporo 060, Japan</mods:affiliation><country xml:lang="fr">Japon</country><wicri:regionArea>Faculty of Pharmaceutical Sciences Hokkaido University, Sapporo 060</wicri:regionArea></affiliation></author><author><name sortKey="Ishikawa, Momoyo" sort="Ishikawa, Momoyo" uniqKey="Ishikawa M" first="Momoyo" last="Ishikawa">Momoyo Ishikawa</name><affiliation wicri:level="1"><mods:affiliation>Protein Engineering Research Institute, Furuedai, Suita, Osaka 565, Hokkaido University, Sapporo 060, Japan</mods:affiliation><country xml:lang="fr">Japon</country><wicri:regionArea>Protein Engineering Research Institute, Furuedai, Suita, Osaka 565, Hokkaido University, Sapporo 060</wicri:regionArea></affiliation></author><author><name sortKey="Ikehara, Morio" sort="Ikehara, Morio" uniqKey="Ikehara M" first="Morio" last="Ikehara">Morio Ikehara</name><affiliation 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addressed</mods: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></record>Pour manipuler ce document sous Unix (Dilib)
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