Single-molecule studies illuminate the function of RAD51 paralogs
نویسندگان
چکیده
In this issue of Molecular Cell, Roy et al. (2021) and Belan demonstrate that the yeast nematode RAD51 paralog complexes function as chaperones to promote assembly nucleoprotein filament on RPA-coated ssDNA.
منابع مشابه
Real-time single-molecule studies of the motions of DNA polymerase fingers illuminate DNA synthesis mechanisms
DNA polymerases maintain genomic integrity by copying DNA with high fidelity. A conformational change important for fidelity is the motion of the polymerase fingers subdomain from an open to a closed conformation upon binding of a complementary nucleotide. We previously employed intra-protein single-molecule FRET on diffusing molecules to observe fingers conformations in polymerase-DNA complexe...
متن کاملSingle-molecule imaging brings Rad51 nucleoprotein filaments into focus.
The Rad51 protein is essential for DNA repair by homologous recombination. After DNA damage, Rad51 localizes to nuclear foci that represent sites of DNA repair in vivo. In vitro, Rad51 self-assembles on single- or double-stranded DNA to form a nucleoprotein filament. Recently, the merging of innovative single-molecule techniques with ensemble methods has provided unique insights into the dynami...
متن کاملA Polar and Nucleotide-Dependent Mechanism of Action for RAD51 Paralogs in RAD51 Filament Remodeling
Central to homologous recombination in eukaryotes is the RAD51 recombinase, which forms helical nucleoprotein filaments on single-stranded DNA (ssDNA) and catalyzes strand invasion with homologous duplex DNA. Various regulatory proteins assist this reaction including the RAD51 paralogs. We recently discovered that a RAD51 paralog complex from C. elegans, RFS-1/RIP-1, functions predominantly dow...
متن کاملanalysis of reading comprehension needs of the students of paramedical studies: the case of the students of health information management (him)
چکیده ندارد.
15 صفحه اولSingle-molecule studies of the replisome.
Replication of DNA is carried out by the replisome, a multiprotein complex responsible for the unwinding of parental DNA and the synthesis of DNA on each of the two DNA strands. The impressive speed and processivity with which the replisome duplicates DNA are a result of a set of tightly regulated interactions between the replication proteins. The transient nature of these protein interactions ...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: Molecular Cell
سال: 2021
ISSN: ['1097-4164', '1097-2765']
DOI: https://doi.org/10.1016/j.molcel.2021.01.037