DC Field | Value | Language |
---|---|---|
dc.contributor.author | Lee, Hyunjee | ko |
dc.contributor.author | Cho, HyeokJin | ko |
dc.contributor.author | Kim, Jooyoung | ko |
dc.contributor.author | Lee, Sua | ko |
dc.contributor.author | Yoo, Jungmin | ko |
dc.contributor.author | Park, Daeho | ko |
dc.contributor.author | Lee, Gwangrog | ko |
dc.date.accessioned | 2023-09-12T01:00:28Z | - |
dc.date.available | 2023-09-12T01:00:28Z | - |
dc.date.created | 2023-09-12 | - |
dc.date.issued | 2022-02 | - |
dc.identifier.citation | NUCLEIC ACIDS RESEARCH, v.50, no.4, pp.1801 - 1814 | - |
dc.identifier.issn | 0305-1048 | - |
dc.identifier.uri | http://hdl.handle.net/10203/312429 | - |
dc.description.abstract | RNase H is involved in fundamental cellular processes and is responsible for removing the short stretch of RNA from Okazaki fragments and the long stretch of RNA from R-loops. Defects in RNase H lead to embryo lethality in mice and Aicardi-Goutieres syndrome in humans, suggesting the importance of RNase H. To date, RNase H is known to be a non-sequence-specific endonuclease, but it is not known whether it performs other functions on the structural variants of RNA:DNA hybrids. Here, we used Escherichia coli RNase H as a model, and examined its catalytic mechanism and its substrate recognition modes, using single-molecule FRET. We discovered that RNase H acts as a processive exoribonuclease on the 3 ' DNA overhang side but as a distributive non-sequence-specific endonuclease on the 5 ' DNA overhang side of RNA:DNA hybrids or on blunt-ended hybrids. The high affinity of previously unidentified double-stranded (ds) and single-stranded (ss) DNA junctions flanking RNA:DNA hybrids may help RNase H find the hybrid substrates in long genomic DNA. Our study provides new insights into the multifunctionality of RNase H, elucidating unprecedented roles of junctions and ssDNA overhang on RNA:DNA hybrids. | - |
dc.language | English | - |
dc.publisher | OXFORD UNIV PRESS | - |
dc.title | RNase H is an exo- and endoribonuclease with asymmetric directionality, depending on the binding mode to the structural variants of RNA:DNA hybrids | - |
dc.type | Article | - |
dc.identifier.wosid | 000764136200001 | - |
dc.identifier.scopusid | 2-s2.0-85125550771 | - |
dc.type.rims | ART | - |
dc.citation.volume | 50 | - |
dc.citation.issue | 4 | - |
dc.citation.beginningpage | 1801 | - |
dc.citation.endingpage | 1814 | - |
dc.citation.publicationname | NUCLEIC ACIDS RESEARCH | - |
dc.identifier.doi | 10.1093/nar/gkab1064 | - |
dc.contributor.localauthor | Lee, Gwangrog | - |
dc.contributor.nonIdAuthor | Lee, Hyunjee | - |
dc.contributor.nonIdAuthor | Cho, HyeokJin | - |
dc.contributor.nonIdAuthor | Kim, Jooyoung | - |
dc.contributor.nonIdAuthor | Lee, Sua | - |
dc.contributor.nonIdAuthor | Yoo, Jungmin | - |
dc.contributor.nonIdAuthor | Park, Daeho | - |
dc.description.isOpenAccess | N | - |
dc.type.journalArticle | Article | - |
dc.subject.keywordPlus | COLI RIBONUCLEASE-H | - |
dc.subject.keywordPlus | RNA/DNA HYBRID | - |
dc.subject.keywordPlus | R-LOOPS | - |
dc.subject.keywordPlus | JUNCTION RIBONUCLEASE | - |
dc.subject.keywordPlus | CRYSTAL-STRUCTURES | - |
dc.subject.keywordPlus | METAL-IONS | - |
dc.subject.keywordPlus | DNA | - |
dc.subject.keywordPlus | RECOGNITION | - |
dc.subject.keywordPlus | MECHANISM | - |
dc.subject.keywordPlus | REPLICATION | - |
Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.