Cohesin SA1 and SA2 are RNA binding proteins that localize to RNA containing regions on DNA
DC Element | Wert | Sprache |
---|---|---|
dc.contributor.author | Pan, Hai | |
dc.contributor.author | Jin, Miao | |
dc.contributor.author | Ghadiyaram, Ashwin | |
dc.contributor.author | Kaur, Parminder | |
dc.contributor.author | Miller, Henry E. | |
dc.contributor.author | Ta, Hai Minh | |
dc.contributor.author | Liu, Ming | |
dc.contributor.author | Fan, Yanlin | |
dc.contributor.author | Mahn, Chelsea | |
dc.contributor.author | Gorthi, Aparna | |
dc.contributor.author | You, Changjiang | |
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 | 2021-12-23T16:21:16Z | - |
dc.date.available | 2021-12-23T16:21:16Z | - |
dc.date.issued | 2020 | |
dc.identifier.issn | 03051048 | |
dc.identifier.uri | https://osnascholar.ub.uni-osnabrueck.de/handle/unios/13800 | - |
dc.description.abstract | Cohesin SA1 (STAG1) and SA2 (STAG2) are key components of the cohesin complex. Previous studies have highlighted the unique contributions by SA1 and SA2 to 3D chromatin organization, DNA replication fork progression, and DNA double-strand break (DSB) repair. Recently, we discovered that cohesin SA1 and SA2 are DNA binding proteins. Given the recently discovered link between SA2 and RNA-mediated biological pathways, we investigated whether or not SA1 and SA2 directly bind to RNA using a combination of bulk biochemical assays and single-molecule techniques, including atomic force microscopy (AFM) and the DNA tightrope assay. We discovered that both SA1 and SA2 bind to various RNA containing substrates, including ssRNA, dsRNA, RNA:DNA hybrids, and R-loops. Importantly, both SA1 and SA2 localize to regions on dsDNA that contain RNA. We directly compared the SA1/SA2 binding and R-loops sites extracted from Chromatin Immunoprecipitation sequencing (ChIP-seq) and DNA-RNA Immunoprecipitation sequencing (DRIP-Seq) data sets, respectively. This analysis revealed that SA1 and SA2 binding sites overlap significantly with R-loops. The majority of R-loop-localized SA1 and SA2 are also sites where other subunits of the cohesin complex bind. These results provide a new direction for future investigation of the diverse biological functions of SA1 and SA2. | |
dc.description.sponsorship | National Institutes of HealthUnited States Department of Health & Human ServicesNational Institutes of Health (NIH) - USA [R01GM107559, R01GM123246, P30 ES025128, R01CA152063, 1R01CA241554, T32CA148724, TL1TR002647]; Caner Prevention & Research Institute of Texas [CPRIT] [RP150445]; Welch FoundationThe Welch Foundation [C-1565]; American Association for Cancer Research-AstraZeneca [18-40-12-GORT]; National Institutes of Health [R01GM107559 to H.W., R.R., R01GM123246 to H.W., R.R., Y.J.T., P30 ES025128 through a Pilot Project Grant to H.W. through Center for Human Health and the Environment at NCSU, R01CA152063 and 1R01CA241554 to A.J.R.B., and NCI T32 postdoctoral training grant (T32CA148724) and NCATS TL1 (TL1TR002647) to A.G.]; Caner Prevention & Research Institute of Texas [CPRIT RP150445 to A.J.R.B.]; Welch Foundation [C-1565 to Y.J.T.]; American Association for Cancer Research-AstraZeneca [Stimulating Therapeutic Advancer through Research Training grant (18-40-12-GORT) to A.G.]. Funding for open access charge: National Institutes of Health [R01GM123246]. | |
dc.language.iso | en | |
dc.publisher | OXFORD UNIV PRESS | |
dc.relation.ispartof | NUCLEIC ACIDS RESEARCH | |
dc.subject | Biochemistry & Molecular Biology | |
dc.subject | BREAKS | |
dc.subject | DISCOVERY | |
dc.subject | DOMAINS | |
dc.subject | GENE | |
dc.subject | MUTATIONS | |
dc.subject | PREVENTS | |
dc.subject | R-LOOPS | |
dc.subject | REPLICATION | |
dc.subject | TELOMERIC DNA | |
dc.subject | TRANSCRIPTION | |
dc.title | Cohesin SA1 and SA2 are RNA binding proteins that localize to RNA containing regions on DNA | |
dc.type | journal article | |
dc.identifier.doi | 10.1093/nar/gkaa284 | |
dc.identifier.isi | ISI:000569071800037 | |
dc.description.volume | 48 | |
dc.description.issue | 10 | |
dc.description.startpage | 5639 | |
dc.description.endpage | 5655 | |
dc.contributor.orcid | 0000-0003-0165-3559 | |
dc.contributor.orcid | 0000-0002-7839-6397 | |
dc.contributor.orcid | 0000-0003-3756-3918 | |
dc.contributor.orcid | 0000-0002-4408-3560 | |
dc.contributor.orcid | 0000-0001-9183-4315 | |
dc.contributor.researcherid | F-3164-2014 | |
dc.contributor.researcherid | L-3901-2014 | |
dc.contributor.researcherid | A-7195-2011 | |
dc.identifier.eissn | 13624962 | |
dc.publisher.place | GREAT CLARENDON ST, OXFORD OX2 6DP, ENGLAND | |
dcterms.isPartOf.abbreviation | Nucleic Acids Res. | |
dcterms.oaStatus | Green Published, gold | |
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 | - |
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