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DC Field | Value | Language |
---|---|---|
dc.citation.endPage | 3563 | - |
dc.citation.number | 22 | - |
dc.citation.startPage | 3549 | - |
dc.citation.title | EMBO JOURNAL | - |
dc.citation.volume | 28 | - |
dc.contributor.author | Meier, Bettina | - |
dc.contributor.author | Barber, Louise J. | - |
dc.contributor.author | Liu, Yan | - |
dc.contributor.author | Shtessel, Ludmila | - |
dc.contributor.author | Boulton, Simon J. | - |
dc.contributor.author | Gartner, Anton | - |
dc.contributor.author | Ahmed, Shawn | - |
dc.date.accessioned | 2023-12-22T07:37:42Z | - |
dc.date.available | 2023-12-22T07:37:42Z | - |
dc.date.created | 2020-01-30 | - |
dc.date.issued | 2009-11 | - |
dc.description.abstract | The telomerase reverse transcriptase adds de novo DNA repeats to chromosome termini. Here we define Caenorhabditis elegans MRT-1 as a novel factor required for telomerase-mediated telomere replication and the DNA-damage response. MRT-1 is composed of an N-terminal domain homologous to the second OB-fold of POT1 telomere-binding proteins and a C-terminal SNM1 family nuclease domain, which confer single-strand DNA-binding and processive 3'-to-5' exonuclease activity, respectively. Furthermore, telomerase activity in vivo depends on a functional MRT-1 OB-fold. We show that MRT-1 acts in the same telomere replication pathway as telomerase and the 9-1-1 DNA-damage response complex. MRT-1 is dispensable for DNA double-strand break repair, but functions with the 9-1-1 complex to promote DNA interstrand cross-link (ICL) repair. Our data reveal MRT-1 as a dual-domain protein required for telomerase function and ICL repair, which raises the possibility that telomeres and ICL lesions may share a common feature that plays a critical role in de novo telomere repeat addition. | - |
dc.identifier.bibliographicCitation | EMBO JOURNAL, v.28, no.22, pp.3549 - 3563 | - |
dc.identifier.doi | 10.1038/emboj.2009.278 | - |
dc.identifier.issn | 0261-4189 | - |
dc.identifier.scopusid | 2-s2.0-70450222723 | - |
dc.identifier.uri | https://scholarworks.unist.ac.kr/handle/201301/31002 | - |
dc.identifier.url | https://www.embopress.org/doi/10.1038/emboj.2009.278 | - |
dc.identifier.wosid | 000271891700009 | - |
dc.language | 영어 | - |
dc.publisher | WILEY | - |
dc.title | The MRT-1 nuclease is required for DNA crosslink repair and telomerase activity in vivo in Caenorhabditis elegans | - |
dc.type | Article | - |
dc.description.isOpenAccess | FALSE | - |
dc.relation.journalWebOfScienceCategory | Biochemistry & Molecular Biology; Cell Biology | - |
dc.relation.journalResearchArea | Biochemistry & Molecular Biology; Cell Biology | - |
dc.type.docType | Article | - |
dc.description.journalRegisteredClass | scie | - |
dc.description.journalRegisteredClass | scopus | - |
dc.subject.keywordAuthor | C. elegans | - |
dc.subject.keywordAuthor | ICL | - |
dc.subject.keywordAuthor | POT1 | - |
dc.subject.keywordAuthor | SNM1 | - |
dc.subject.keywordAuthor | telomerase | - |
dc.subject.keywordPlus | REVERSE-TRANSCRIPTASE | - |
dc.subject.keywordPlus | FISSION YEAST | - |
dc.subject.keywordPlus | METALLO-BETA-LACTAMASE | - |
dc.subject.keywordPlus | END-BINDING-PROTEIN | - |
dc.subject.keywordPlus | DAMAGE CHECKPOINT PROTEIN | - |
dc.subject.keywordPlus | SINGLE-STRANDED-DNA | - |
dc.subject.keywordPlus | GENOME-WIDE SCREEN | - |
dc.subject.keywordPlus | SACCHAROMYCES-CEREVISIAE | - |
dc.subject.keywordPlus | TETRAHYMENA TELOMERASE | - |
dc.subject.keywordPlus | C-ELEGANS | - |
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