DC Field | Value | Language |
---|---|---|
dc.contributor.author | Masuda-Ozawa, Tokiha | ko |
dc.contributor.author | Hoang, Trish | ko |
dc.contributor.author | Seo, Yeon-Soo | ko |
dc.contributor.author | Chen, Lin-Feng | ko |
dc.contributor.author | Spies, Maria | ko |
dc.date.accessioned | 2013-08-08T02:05:44Z | - |
dc.date.available | 2013-08-08T02:05:44Z | - |
dc.date.created | 2013-06-05 | - |
dc.date.created | 2013-06-05 | - |
dc.date.issued | 2013-04 | - |
dc.identifier.citation | NUCLEIC ACIDS RESEARCH, v.41, no.6, pp.3576 - 3587 | - |
dc.identifier.issn | 0305-1048 | - |
dc.identifier.uri | http://hdl.handle.net/10203/174196 | - |
dc.description.abstract | DNA repair helicases function in the cell to separate DNA duplexes or remodel nucleoprotein complexes. These functions are influenced by sensing and signaling; the cellular pool of a DNA helicase may contain subpopulations of enzymes carrying different post-translational modifications and performing distinct biochemical functions. Here, we report a novel experimental strategy, single-molecule sorting, which overcomes difficulties associated with comprehensive analysis of heterologously modified pool of proteins. This methodology was applied to visualize human DNA helicase F-box-containing DNA helicase (FBH1) acting on the DNA structures resembling a stalled or collapsed replication fork and its interactions with RAD51 nucleoprotein filament. Individual helicase molecules isolated from human cells with their native post-translational modifications were analyzed using total internal reflection fluorescence microscopy. Separation of the activity trajectories originated from ubiquitylated and non-ubiquitylated FBH1 molecules revealed that ubiquitylation affects FBH1 interaction with the RAD51 nucleoprotein filament, but not its translocase and helicase activities. | - |
dc.language | English | - |
dc.publisher | OXFORD UNIV PRESS | - |
dc.subject | BOX DNA HELICASE | - |
dc.subject | HOMOLOGOUS RECOMBINATION | - |
dc.subject | STRAND EXCHANGE | - |
dc.subject | HUMAN RAD51 | - |
dc.subject | REPLICATION FORKS | - |
dc.subject | ATPASE ACTIVITY | - |
dc.subject | PROTEIN | - |
dc.subject | BINDING | - |
dc.subject | FILAMENTS | - |
dc.subject | REPAIR | - |
dc.title | Single-molecule sorting reveals how ubiquitylation affects substrate recognition and activities of FBH1 helicase | - |
dc.type | Article | - |
dc.identifier.wosid | 000318063400017 | - |
dc.identifier.scopusid | 2-s2.0-84876021636 | - |
dc.type.rims | ART | - |
dc.citation.volume | 41 | - |
dc.citation.issue | 6 | - |
dc.citation.beginningpage | 3576 | - |
dc.citation.endingpage | 3587 | - |
dc.citation.publicationname | NUCLEIC ACIDS RESEARCH | - |
dc.identifier.doi | 10.1093/nar/gkt056 | - |
dc.contributor.localauthor | Seo, Yeon-Soo | - |
dc.contributor.nonIdAuthor | Masuda-Ozawa, Tokiha | - |
dc.contributor.nonIdAuthor | Hoang, Trish | - |
dc.contributor.nonIdAuthor | Chen, Lin-Feng | - |
dc.contributor.nonIdAuthor | Spies, Maria | - |
dc.description.isOpenAccess | Y | - |
dc.type.journalArticle | Article | - |
dc.subject.keywordPlus | BOX DNA HELICASE | - |
dc.subject.keywordPlus | HOMOLOGOUS RECOMBINATION | - |
dc.subject.keywordPlus | STRAND EXCHANGE | - |
dc.subject.keywordPlus | HUMAN RAD51 | - |
dc.subject.keywordPlus | REPLICATION FORKS | - |
dc.subject.keywordPlus | ATPASE ACTIVITY | - |
dc.subject.keywordPlus | PROTEIN | - |
dc.subject.keywordPlus | BINDING | - |
dc.subject.keywordPlus | FILAMENTS | - |
dc.subject.keywordPlus | REPAIR | - |
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