Functional interplay between SA1 and TRF1 in telomeric DNA binding and DNA–DNA pairing

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dc.citation.journalTitleNucleic Acids Researchen_US
dc.contributor.authorLin, Jiangguoen_US
dc.contributor.authorCountryman, Prestonen_US
dc.contributor.authorChen, Haijiangen_US
dc.contributor.authorPan, Haien_US
dc.contributor.authorFan, Yanlinen_US
dc.contributor.authorJiang, Yunyunen_US
dc.contributor.authorKaur, Parminderen_US
dc.contributor.authorMiao, Wangen_US
dc.contributor.authorGurgel, Giseleen_US
dc.contributor.authorYou, Changjiangen_US
dc.contributor.authorPiehler, Jacoben_US
dc.contributor.authorKad, Neil M.en_US
dc.contributor.authorRiehn, Roberten_US
dc.contributor.authorOpresko, Patricia L.en_US
dc.contributor.authorSmith, Susanen_US
dc.contributor.authorTao, Yizhi Janeen_US
dc.contributor.authorWang, Hongen_US
dc.date.accessioned2016-06-22T16:28:31Zen_US
dc.date.available2016-06-22T16:28:31Zen_US
dc.date.issued2016en_US
dc.description.abstractProper chromosome alignment and segregation during mitosis depend on cohesion between sister chromatids. Cohesion is thought to occur through the entrapment of DNA within the tripartite ring (Smc1, Smc3 and Rad21) with enforcement from a fourth subunit (SA1/SA2). Surprisingly, cohesin rings do not play a major role in sister telomere cohesion. Instead, this role is replaced by SA1 and telomere binding proteins (TRF1 and TIN2). Neither the DNA binding property of SA1 nor this unique telomere cohesion mechanism is understood. Here, using single-molecule fluorescence imaging, we discover that SA1 displays two-state binding on DNA: searching by one-dimensional (1D) free diffusion versus recognition through subdiffusive sliding at telomeric regions. The AT-hook motif in SA1 plays dual roles in modulating non-specific DNA binding and subdiffusive dynamics over telomeric regions. TRF1 tethers SA1 within telomeric regions that SA1 transiently interacts with. SA1 and TRF1 together form longer DNA–DNA pairing tracts than with TRF1 alone, as revealed by atomic force microscopy imaging. These results suggest that at telomeres cohesion relies on the molecular interplay between TRF1 and SA1 to promote DNA–DNA pairing, while along chromosomal arms the core cohesin assembly might also depend on SA1 1D diffusion on DNA and sequence-specific DNA binding.en_US
dc.identifier.citationLin, Jiangguo, Countryman, Preston, Chen, Haijiang, et al.. "Functional interplay between SA1 and TRF1 in telomeric DNA binding and DNA–DNA pairing." <i>Nucleic Acids Research,</i> (2016) Oxford University Press: http://dx.doi.org/10.1093/nar/gkw518.en_US
dc.identifier.doihttp://dx.doi.org/10.1093/nar/gkw518en_US
dc.identifier.urihttps://hdl.handle.net/1911/90514en_US
dc.language.isoengen_US
dc.publisherOxford University Pressen_US
dc.rightsThis is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License, which permits non-commercial re-use, distribution, and reproduction in any medium, provided the original work is properly cited.en_US
dc.rights.urihttp://creativecommons.org/licenses/by-nc/4.0/en_US
dc.titleFunctional interplay between SA1 and TRF1 in telomeric DNA binding and DNA–DNA pairingen_US
dc.typeJournal articleen_US
dc.type.dcmiTexten_US
dc.type.publicationpublisher versionen_US
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