Detailed Information on Publication Record
2018
Human RAD51 rapidly forms intrinsically dynamic nucleoprotein filaments modulated by nucleotide binding state
ŠPÍREK, Mário, Jarmila MLČOUŠKOVÁ, Ondrej BELÁŇ, Máté GYIMESI, Gábor M. HARAMI et. al.Basic information
Original name
Human RAD51 rapidly forms intrinsically dynamic nucleoprotein filaments modulated by nucleotide binding state
Authors
ŠPÍREK, Mário (703 Slovakia, belonging to the institution), Jarmila MLČOUŠKOVÁ (203 Czech Republic, belonging to the institution), Ondrej BELÁŇ (703 Slovakia, belonging to the institution), Máté GYIMESI (348 Hungary), Gábor M. HARAMI (348 Hungary), Eszter MOLNÁR (348 Hungary), Jiří NOVÁČEK (203 Czech Republic, belonging to the institution), Mihály KOVÁCS (348 Hungary) and Lumír KREJČÍ (203 Czech Republic, guarantor, belonging to the institution)
Edition
Nucleic Acids Research, Oxford, Oxford University Press, 2018, 0305-1048
Other information
Language
English
Type of outcome
Článek v odborném periodiku
Field of Study
10608 Biochemistry and molecular biology
Country of publisher
United Kingdom of Great Britain and Northern Ireland
Confidentiality degree
není předmětem státního či obchodního tajemství
Impact factor
Impact factor: 11.147
RIV identification code
RIV/00216224:14110/18:00101769
Organization unit
Faculty of Medicine
UT WoS
000431895800021
Keywords in English
RAD51
Tags
International impact, Reviewed
Změněno: 12/3/2019 10:37, Mgr. Pavla Foltynová, Ph.D.
Abstract
V originále
Formation of RAD51 filaments on single-stranded DNA is an essential event during homologous recombination, which is required for homology search, strand exchange and protection of replication forks. Formation of nucleoprotein filaments (NF) is required for development and genomic stability, and its failure is associated with developmental abnormalities and tumorigenesis. Here we describe the structure of the human RAD51 NFs and of its Walker box mutants using electron microscopy. Wild-type RAD51 filaments adopt an 'open' conformation when compared to a 'closed' structure formed by mutants, reflecting alterations in helical pitch. The kinetics of formation/disassembly of RAD51 filaments show rapid and high ssDNA coverage via low cooperativity binding of RAD51 units along the DNA. Subsequently, a series of isomerization or dissociation events mediated by nucleotide binding state creates intrinsically dynamic RAD51 NFs. Our findings highlight important a mechanistic divergence among recombinases from different organisms, in line with the diversity of biological mechanisms of HR initiation and quality control. These data reveal unexpected intrinsic dynamic properties of the RAD51 filament during assembly/disassembly, which may be important for the proper control of homologous recombination.
Links
GA17-17720S, research and development project |
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LM2015043, research and development project |
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206292/E/17/Z, interní kód MU |
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