Cohesin SA2 is a sequence-independent DNA-binding protein that recognizes DNA replication and repair intermediates
DC Element | Wert | Sprache |
---|---|---|
dc.contributor.author | Countryman, Preston | |
dc.contributor.author | Fan, Yanlin | |
dc.contributor.author | Gorthi, Aparna | |
dc.contributor.author | Pan, Hai | |
dc.contributor.author | Strickland, Jack | |
dc.contributor.author | Kaur, Parminder | |
dc.contributor.author | Wang, Xuechun | |
dc.contributor.author | Lin, Jiangguo | |
dc.contributor.author | Lei, Xiaoying | |
dc.contributor.author | White, Christian | |
dc.contributor.author | You, Changjiang | |
dc.contributor.author | Wirth, Nicolas | |
dc.contributor.author | Tessmer, Ingrid | |
dc.contributor.author | Piehler, Jacob | |
dc.contributor.author | Riehn, Robert | |
dc.contributor.author | Bishop, Alexander J. R. | |
dc.contributor.author | Tao, Yizhi Jane | |
dc.contributor.author | Wang, Hong | |
dc.date.accessioned | 2021-12-23T16:23:33Z | - |
dc.date.available | 2021-12-23T16:23:33Z | - |
dc.date.issued | 2018 | |
dc.identifier.uri | https://osnascholar.ub.uni-osnabrueck.de/handle/unios/14576 | - |
dc.description.abstract | Proper chromosome alignment and segregation during mitosis depend on cohesion between sister chromatids, mediated by the cohesin protein complex, which also plays crucial roles in diverse genome maintenance pathways. Current models attribute DNA binding by cohesin to entrapment of dsDNA by the cohesin ring subunits (SMC1, SMC3, and RAD21 in humans). However, the biophysical properties and activities of the fourth core cohesin subunit SA2 (STAG2) are largely unknown. Here, using single-molecule atomic force and fluorescence microscopy imaging as well as fluorescence anisotropy measurements, we established that SA2 binds to both dsDNA and ssDNA, albeit with a higher binding affinity for ssDNA. We observed that SA2 can switch between the 1D diffusing (search) mode on dsDNA and stable binding (recognition) mode at ssDNA gaps. Although SA2 does not specifically bind to centromeric or telomeric sequences, it does recognize DNA structures often associated with DNA replication and double-strand break repair, such as a double-stranded end, single-stranded overhang, flap, fork, and ssDNA gap. SA2 loss leads to a defect in homologous recombination-mediated DNA double-strand break repair. These results suggest that SA2 functions at intermediate DNA structures during DNA transactions in genome maintenance pathways. These findings have important implications for understanding the function of cohesin in these pathways. | |
dc.description.sponsorship | National Institutes of HealthUnited States Department of Health & Human ServicesNational Institutes of Health (NIH) - USA [ES027641, R01GM107559, K22ES012264, 1R15ES019128, 1R01CA152063, NCI T32 CA 148724, P30 ES025128, R01-GM107559]; Voelcker Fund Young Investigator Award; CPRIT [RP150445]; Deutsche ForschungsgemeinschaftGerman Research Foundation (DFG) [Forschungszentrum FZ82]; Welch FoundationThe Welch Foundation [C-1565]; NATIONAL CANCER INSTITUTEUnited States Department of Health & Human ServicesNational Institutes of Health (NIH) - USANIH National Cancer Institute (NCI) [R01CA152063, T32CA148724] Funding Source: NIH RePORTER; NATIONAL INSTITUTE OF ENVIRONMENTAL HEALTH SCIENCESUnited States Department of Health & Human ServicesNational Institutes of Health (NIH) - USANIH National Institute of Environmental Health Sciences (NIEHS) [P30ES025128, R21ES027641, K22ES012264, R15ES019128] Funding Source: NIH RePORTER; NATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCESUnited States Department of Health & Human ServicesNational Institutes of Health (NIH) - USANIH National Institute of General Medical Sciences (NIGMS) [R01GM107559] Funding Source: NIH RePORTER; This work was supported by National Institutes of Health Grants ES027641 (to H.W.), R01GM107559 (to H.W. and R.R.), K22ES012264, 1R15ES019128, and 1R01CA152063 (to A.J.R.B.), NCI T32 CA 148724 (to A.G.), and P30 ES025128 (through a pilot project grant to H.W. by the Center for Human Health and the Environment (CHHE) at North Carolina State University); a Voelcker Fund Young Investigator Award and CPRIT Grant RP150445 (to A.J.R.B.); Deutsche Forschungsgemeinschaft Forschungszentrum FZ82 (to I.T.); and Welch Foundation Grant C-1565 (to Y.J.T.). This work was also supported by National Institutes of Health Grant R01-GM107559. The authors declare that they have no conflicts of interest with the contents of this article. The content is solely the responsibility of the authors and does not necessarily represent the official views of the National Institutes of Health. | |
dc.language.iso | en | |
dc.publisher | AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC | |
dc.relation.ispartof | JOURNAL OF BIOLOGICAL CHEMISTRY | |
dc.subject | ATOMIC-FORCE MICROSCOPY | |
dc.subject | Biochemistry & Molecular Biology | |
dc.subject | COMPLEX | |
dc.subject | GENE-EXPRESSION | |
dc.subject | HOMOLOGY-DIRECTED REPAIR | |
dc.subject | ONE-DIMENSIONAL DIFFUSION | |
dc.subject | QUANTUM-DOT | |
dc.subject | SACCHAROMYCES-CEREVISIAE | |
dc.subject | SISTER-CHROMATID COHESION | |
dc.subject | STRAND-BREAK REPAIR | |
dc.subject | TELOMERIC DNA | |
dc.title | Cohesin SA2 is a sequence-independent DNA-binding protein that recognizes DNA replication and repair intermediates | |
dc.type | journal article | |
dc.identifier.doi | 10.1074/jbc.M117.806406 | |
dc.identifier.isi | ISI:000422864500025 | |
dc.description.volume | 293 | |
dc.description.issue | 3 | |
dc.description.startpage | 1054 | |
dc.description.endpage | 1069 | |
dc.contributor.orcid | 0000-0003-0165-3559 | |
dc.contributor.orcid | 0000-0002-4408-3560 | |
dc.contributor.orcid | 0000-0002-7839-6397 | |
dc.contributor.orcid | 0000-0002-5742-4387 | |
dc.contributor.orcid | 0000-0002-8353-6315 | |
dc.contributor.orcid | 0000-0001-5935-4098 | |
dc.contributor.orcid | 0000-0001-9183-4315 | |
dc.contributor.orcid | 0000-0003-0799-1321 | |
dc.contributor.researcherid | F-3164-2014 | |
dc.contributor.researcherid | A-7195-2011 | |
dc.contributor.researcherid | O-2810-2013 | |
dc.contributor.researcherid | L-3901-2014 | |
dc.identifier.eissn | 1083351X | |
dc.publisher.place | 9650 ROCKVILLE PIKE, BETHESDA, MD 20814-3996 USA | |
dcterms.isPartOf.abbreviation | J. Biol. Chem. | |
dcterms.oaStatus | Green Published, hybrid | |
crisitem.author.dept | Sonderforschungsbereich 944: Physiologie und Dynamik zellulärer Mikrokompartimente | - |
crisitem.author.dept | FB 05 - Biologie/Chemie | - |
crisitem.author.deptid | organisation19 | - |
crisitem.author.deptid | fb05 | - |
crisitem.author.orcid | 0000-0002-7839-6397 | - |
crisitem.author.orcid | 0000-0002-2143-2270 | - |
crisitem.author.parentorg | FB 05 - Biologie/Chemie | - |
crisitem.author.parentorg | Universität Osnabrück | - |
crisitem.author.grandparentorg | Universität Osnabrück | - |
crisitem.author.netid | YoCh745 | - |
crisitem.author.netid | PiJa938 | - |
Seitenaufrufe
2
Letzte Woche
0
0
Letzter Monat
0
0
geprüft am 16.05.2024