DC Field | Value | Language |
---|---|---|
dc.contributor.author | Park, Y.B. | - |
dc.contributor.author | Hohl, M. | - |
dc.contributor.author | Padjasek, M. | - |
dc.contributor.author | Jeong, E. | - |
dc.contributor.author | Jin, K.S. | - |
dc.contributor.author | Kr?zel, A. | - |
dc.contributor.author | Petrini, J.H.J. | - |
dc.contributor.author | Cho, Y. | - |
dc.date.accessioned | 2018-07-17T10:47:02Z | - |
dc.date.available | 2018-07-17T10:47:02Z | - |
dc.date.created | 2017-12-21 | - |
dc.date.issued | 2017-03 | - |
dc.identifier.issn | 1545-9993 | - |
dc.identifier.uri | https://oasis.postech.ac.kr/handle/2014.oak/92122 | - |
dc.description.abstract | The Rad50 hook interface is crucial for assembly and various functions of the Mre11 complex. Previous analyses suggested that Rad50 molecules interact within (intracomplex) or between (intercomplex) dimeric complexes. In this study, we determined the structure of the human Rad50 hook and coiled-coil domains. The data suggest that the predominant structure is the intracomplex, in which the two parallel coiled coils proximal to the hook form a rod shape, and that a novel interface within the coiled-coil domains of Rad50 stabilizes the interaction of Rad50 protomers in the dimeric assembly. In yeast, removal of the coiled-coil interface compromised Tel1 activation without affecting DNA repair, while simultaneous disruption of that interface and the hook phenocopied a null mutation. The results demonstrate that the hook and coiled-coil interfaces coordinately promote intracomplex assembly and define the intracomplex as the functional form of the Mre11 complex. ? 2017 Nature America, Inc., part of Springer Nature. All rights reserved. | - |
dc.language | English | - |
dc.publisher | Nature Publishing Group | - |
dc.relation.isPartOf | Nature Structural and Molecular Biology | - |
dc.subject | adenosine triphosphate | - |
dc.subject | ATM protein | - |
dc.subject | chromosome protein | - |
dc.subject | dimer | - |
dc.subject | Mre11 protein | - |
dc.subject | Rad50 protein | - |
dc.subject | DNA binding protein | - |
dc.subject | DNA ligase | - |
dc.subject | mutant protein | - |
dc.subject | Rad50 protein, human | - |
dc.subject | solution and solubility | - |
dc.subject | zinc | - |
dc.subject | Article | - |
dc.subject | cell survival | - |
dc.subject | coiled coil domain | - |
dc.subject | conformational transition | - |
dc.subject | controlled study | - |
dc.subject | crystal structure | - |
dc.subject | dimerization | - |
dc.subject | DNA binding | - |
dc.subject | DNA damage response | - |
dc.subject | DNA end joining repair | - |
dc.subject | DNA repair | - |
dc.subject | double stranded DNA break | - |
dc.subject | eukaryote | - |
dc.subject | hook domain | - |
dc.subject | in vivo study | - |
dc.subject | nonhuman | - |
dc.subject | priority journal | - |
dc.subject | protein cross linking | - |
dc.subject | protein function | - |
dc.subject | protein hydrolysis | - |
dc.subject | protein structure | - |
dc.subject | Pyrococcus furiosus | - |
dc.subject | Saccharomyces cerevisiae | - |
dc.subject | sporogenesis | - |
dc.subject | Thermotoga maritima | - |
dc.subject | amino acid sequence | - |
dc.subject | biological model | - |
dc.subject | cell cycle checkpoint | - |
dc.subject | chemistry | - |
dc.subject | DNA repair | - |
dc.subject | eukaryotic cell | - |
dc.subject | fluorescence resonance energy transfer | - |
dc.subject | human | - |
dc.subject | meiosis | - |
dc.subject | metabolism | - |
dc.subject | protein domain | - |
dc.subject | protein multimerization | - |
dc.subject | protein secondary structure | - |
dc.subject | signal transduction | - |
dc.subject | solution and solubility | - |
dc.subject | X ray crystallography | - |
dc.subject | Amino Acid Sequence | - |
dc.subject | Cell Cycle Checkpoints | - |
dc.subject | Crystallography, X-Ray | - |
dc.subject | DNA Breaks, Double-Stranded | - |
dc.subject | DNA Repair | - |
dc.subject | DNA Repair Enzymes | - |
dc.subject | DNA-Binding Proteins | - |
dc.subject | Eukaryotic Cells | - |
dc.subject | Fluorescence Resonance Energy Transfer | - |
dc.subject | Humans | - |
dc.subject | Meiosis | - |
dc.subject | Models, Biological | - |
dc.subject | Mutant Proteins | - |
dc.subject | Protein Domains | - |
dc.subject | Protein Multimerization | - |
dc.subject | Protein Structure, Secondary | - |
dc.subject | Saccharomyces cerevisiae | - |
dc.subject | Signal Transduction | - |
dc.subject | Solutions | - |
dc.subject | Zinc | - |
dc.title | Eukaryotic Rad50 functions as a rod-shaped dimer | - |
dc.type | Article | - |
dc.identifier.doi | 10.1038/nsmb.3369 | - |
dc.type.rims | ART | - |
dc.identifier.bibliographicCitation | Nature Structural and Molecular Biology, v.24, no.3, pp.248 - 257 | - |
dc.identifier.wosid | 000395826000009 | - |
dc.date.tcdate | 2019-02-01 | - |
dc.citation.endPage | 257 | - |
dc.citation.number | 3 | - |
dc.citation.startPage | 248 | - |
dc.citation.title | Nature Structural and Molecular Biology | - |
dc.citation.volume | 24 | - |
dc.contributor.affiliatedAuthor | Cho, Y. | - |
dc.identifier.scopusid | 2-s2.0-85010952331 | - |
dc.description.journalClass | 1 | - |
dc.description.journalClass | 1 | - |
dc.description.wostc | 8 | - |
dc.type.docType | Article | - |
dc.subject.keywordPlus | STRAND-BREAK REPAIR | - |
dc.subject.keywordPlus | DEPENDENT DNA-BINDING | - |
dc.subject.keywordPlus | MRE11 COMPLEX FUNCTIONS | - |
dc.subject.keywordPlus | COILED-COIL DOMAIN | - |
dc.subject.keywordPlus | MRE11-RAD50-NBS1 COMPLEX | - |
dc.subject.keywordPlus | SACCHAROMYCES-CEREVISIAE | - |
dc.subject.keywordPlus | CONFORMATIONAL-CHANGES | - |
dc.subject.keywordPlus | MRE11/RAD50 COMPLEX | - |
dc.subject.keywordPlus | PROTEIN COMPLEX | - |
dc.subject.keywordPlus | KINASE-ACTIVITY | - |
dc.relation.journalWebOfScienceCategory | Biochemistry & Molecular Biology | - |
dc.relation.journalWebOfScienceCategory | Biophysics | - |
dc.relation.journalWebOfScienceCategory | Cell Biology | - |
dc.description.journalRegisteredClass | scie | - |
dc.description.journalRegisteredClass | scopus | - |
dc.relation.journalResearchArea | Biochemistry & Molecular Biology | - |
dc.relation.journalResearchArea | Biophysics | - |
dc.relation.journalResearchArea | Cell Biology | - |
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