DC Field | Value | Language |
---|---|---|
dc.contributor.author | Heo, SD | - |
dc.contributor.author | Ku, JK | - |
dc.contributor.author | Ban, C | - |
dc.date.accessioned | 2016-04-01T08:23:36Z | - |
dc.date.available | 2016-04-01T08:23:36Z | - |
dc.date.created | 2009-07-30 | - |
dc.date.issued | 2009-07-24 | - |
dc.identifier.issn | 0006-291X | - |
dc.identifier.other | 2009-OAK-0000019216 | - |
dc.identifier.uri | https://oasis.postech.ac.kr/handle/2014.oak/27869 | - |
dc.description.abstract | The effect of wild-type and mutant MULL on the steady-state ATPase activity of MutS from Escherichia coli has been investigated in the absence and presence of 22, 50, and 75 base pair hetero- and homoduplex DNAs with open and blocked ends. The steady-state ATPase activity of MutS has been measured at 37 degrees C using a spectrophotometric method. The presence Of MutL did not affect appreciably on the ATPase activity of MutS in the absence of DNA or in the presence of blocked end homoduplex DNAs. However, the addition of MULL affected oppositely on the ATPase activity of MutS in the presence of G-T mismatched DNAs depending on their end status. We have also found that only the ATPase active forms of MutL increased the ATPase activity of MutS in the presence of G-T mismatched DNAs with blocked ends. The results suggest that MutL ATPase activity is required to catalyze dissociation of the MutS sliding clamps. (C) 2009 Elsevier Inc. All rights reserved. | - |
dc.description.statementofresponsibility | X | - |
dc.language | English | - |
dc.publisher | ACADEMIC PRESS INC ELSEVIER SCIENCE | - |
dc.relation.isPartOf | BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | - |
dc.subject | MutL | - |
dc.subject | MutS | - |
dc.subject | MMR mechanism | - |
dc.subject | ATPase activity | - |
dc.subject | Blocked heteroduplex DNA | - |
dc.subject | MISMATCH REPAIR | - |
dc.subject | HYDROLYSIS | - |
dc.subject | MODULATION | - |
dc.subject | DOMAINS | - |
dc.subject | BINDING | - |
dc.subject | SWITCH | - |
dc.title | Effect of E. coli MutL on the steady-state ATPase activity of MutS in the presence of short blocked end DNAs | - |
dc.type | Article | - |
dc.contributor.college | 화학과 | - |
dc.identifier.doi | 10.1016/j.bbrc.2009.05.042 | - |
dc.author.google | Heo, SD | - |
dc.author.google | Ku, JK | - |
dc.author.google | Ban, C | - |
dc.relation.volume | 385 | - |
dc.relation.issue | 2 | - |
dc.relation.startpage | 225 | - |
dc.relation.lastpage | 229 | - |
dc.contributor.id | 10085220 | - |
dc.relation.journal | BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | - |
dc.relation.index | SCI급, SCOPUS 등재논문 | - |
dc.relation.sci | SCI | - |
dc.collections.name | Journal Papers | - |
dc.type.rims | ART | - |
dc.identifier.bibliographicCitation | BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, v.385, no.2, pp.225 - 229 | - |
dc.identifier.wosid | 000267037300019 | - |
dc.date.tcdate | 2019-02-01 | - |
dc.citation.endPage | 229 | - |
dc.citation.number | 2 | - |
dc.citation.startPage | 225 | - |
dc.citation.title | BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | - |
dc.citation.volume | 385 | - |
dc.contributor.affiliatedAuthor | Ku, JK | - |
dc.contributor.affiliatedAuthor | Ban, C | - |
dc.identifier.scopusid | 2-s2.0-67349149025 | - |
dc.description.journalClass | 1 | - |
dc.description.journalClass | 1 | - |
dc.description.wostc | 2 | - |
dc.type.docType | Article | - |
dc.subject.keywordPlus | MISMATCH REPAIR | - |
dc.subject.keywordPlus | HYDROLYSIS | - |
dc.subject.keywordPlus | MODULATION | - |
dc.subject.keywordPlus | DOMAINS | - |
dc.subject.keywordPlus | BINDING | - |
dc.subject.keywordPlus | SWITCH | - |
dc.subject.keywordAuthor | MutL | - |
dc.subject.keywordAuthor | MutS | - |
dc.subject.keywordAuthor | MMR mechanism | - |
dc.subject.keywordAuthor | ATPase activity | - |
dc.subject.keywordAuthor | Blocked heteroduplex DNA | - |
dc.relation.journalWebOfScienceCategory | Biochemistry & Molecular Biology | - |
dc.relation.journalWebOfScienceCategory | Biophysics | - |
dc.description.journalRegisteredClass | scie | - |
dc.description.journalRegisteredClass | scopus | - |
dc.relation.journalResearchArea | Biochemistry & Molecular Biology | - |
dc.relation.journalResearchArea | Biophysics | - |
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