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

Nucleic Acids Res.. 2016-07; 
Lin J, Countryman P, Chen H, Pan H, Fan Y, Jiang Y, Kaur P, Miao W, Gurgel G, You C, Piehler J, Kad NM, Riehn R, Opresko PL, Smith S, Tao YJ, Wang H .
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Catalog Antibody ... respectively. For labeling N-terminal 3X Flag-tagged WT SA1, SA1 R37A R39A (GenScript), or SUMO-tagged SA1-N (SA1-N, 1–72 AA), QDs (1 μl of 1 μM) were incubated with the primary antibodies (1 μl of 1 μM) for 20 min. ... Get A Quote

摘要

Proper 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 subdiffu... More

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