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RPA-like single-stranded DNA-binding protein complexes including CST serve as specialized processivity factors for polymerases |
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| Institution: | 1. Mitchell Cancer Institute, University of South Alabama, Mobile, AL 36604, USA;2. Department of Pharmacology, College of Medicine, University of South Alabama, Mobile, AL 36688, USA;3. Department of Biochemistry and Molecular Biology, College of Medicine, University of South Alabama, Mobile, AL 36688, USA;4. Department of Pathology and Laboratory Medicine, Warren Alpert Medical School & Legorreta Cancer Center, Brown University, Providence, RI 02912, USA;1. Toxicology Program, North Carolina State University, Raleigh, NC, USA;2. Physics Department, North Carolina State University, Raleigh, NC, USA;3. Center for Human Health and the Environment, North Carolina State University, Raleigh, NC, USA;1. Institut Curie Research Center, CNRS UMR3244, PSL Research University, 26 rue d’Ulm, 75248 Paris Cedex 05, France;2. IRCAN, CNRS UMR7284, INSERM U1081, Université Côte d’Azur, 28 avenue de Valombrose, 06107 Nice, France;1. Lady Davis Institute for Medical Research, Jewish General Hospital, Montréal, Canada;2. Department of Anatomy and Cell Biology, McGill University, Montréal, Canada;3. Department of Medicine, McGill University, Montréal, Canada |
| Abstract: | Telomeres and other single-stranded regions of the genome require specialized management to maintain stability and for proper progression of DNA metabolism pathways. Human Replication Protein A and CTC1-STN1-TEN1 are structurally similar heterotrimeric protein complexes that have essential ssDNA-binding roles in DNA replication, repair, and telomeres. Yeast and ciliates have related ssDNA-binding proteins with strikingly conserved structural features to these human heterotrimeric protein complexes. Recent breakthrough structures have extended our understanding of these commonalities by illuminating a common mechanism used by these proteins to act as processivity factors for their partner polymerases through their ability to manage ssDNA. |
| Keywords: | ssDNA"} {"#name":"keyword" "$":{"id":"pc_Q9THdrGG2r"} "$$":[{"#name":"text" "_":"single-stranded DNA CST"} {"#name":"keyword" "$":{"id":"pc_fpuMXr51Bg"} "$$":[{"#name":"text" "_":"CTC1-STN1-TEN1 RPA"} {"#name":"keyword" "$":{"id":"pc_LGLV8e2Drm"} "$$":[{"#name":"text" "_":"Replication Protein A OB fold"} {"#name":"keyword" "$":{"id":"pc_DH0CO1ToJd"} "$$":[{"#name":"text" "_":"oligonucleotide/oligosaccharide binding fold wHTH"} {"#name":"keyword" "$":{"id":"pc_MWWDX5LL7B"} "$$":[{"#name":"text" "_":"winged helix-turn-helix motif DBD"} {"#name":"keyword" "$":{"id":"pc_8clx7olS2d"} "$$":[{"#name":"text" "_":"DNA-binding domain PARP"} {"#name":"keyword" "$":{"id":"pc_lTqiZyJoii"} "$$":[{"#name":"text" "_":"Poly-(ADP)-ribose-polymerase RD"} {"#name":"keyword" "$":{"id":"pc_t1xpJJ7fYY"} "$$":[{"#name":"text" "_":"recruitment domain |
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