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- W2063221444 abstract "Structural Maintenance of Chromosomes (SMC) proteins are vital for a wide range of processes including chromosome structure and dynamics, gene regulation and DNA repair. Eukaryotes have three SMC complexes, consisting of heterodimeric pairs of six different SMC proteins along with several specific regulatory subunits. In addition to their other functions, all three SMC complexes play distinct roles in DNA repair. Cohesin (SMC1–SMC3) is involved in DNA double-strand break repair, condensin (SMC2–SMC4) participates in single-strand break (SSB) repair, and the SMC5–SMC6 complex functions in various DNA repair pathways. SMC proteins consist of N- and C-terminal domains that fold back onto each other to create an ATPase ‘head’ domain, connected to a central ‘hinge’ domain via long coiled-coils. The hinge domain mediates dimerization of SMC proteins and binds DNA, but it is not clear to what purpose this activity serves. We studied the structure and function of the condensin hinge domain from mouse. While the SMC hinge domain structure is largely conserved from prokaryotes to eukaryotes, its function seems to have diversified throughout the course of evolution. The condensin hinge domain preferentially binds single-stranded DNA. We propose that this activity plays a role in the SSB repair function of the condensin complex." @default.
- W2063221444 created "2016-06-24" @default.
- W2063221444 creator A5021746189 @default.
- W2063221444 creator A5041102731 @default.
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- W2063221444 date "2010-02-05" @default.
- W2063221444 modified "2023-10-18" @default.
- W2063221444 title "Structure and DNA binding activity of the mouse condensin hinge domain highlight common and diverse features of SMC proteins" @default.
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- W2063221444 doi "https://doi.org/10.1093/nar/gkq038" @default.
- W2063221444 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/2879519" @default.
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