[HTML][HTML] Homologous recombination and the repair of DNA double-strand breaks
WD Wright, SS Shah, WD Heyer - Journal of Biological Chemistry, 2018 - ASBMB
Homologous recombination enables the cell to access and copy intact DNA sequence
information in trans, particularly to repair DNA damage affecting both strands of the double …
information in trans, particularly to repair DNA damage affecting both strands of the double …
The bacterial RecA protein and the recombinational DNA repair of stalled replication forks
SL Lusetti, MM Cox - Annual review of biochemistry, 2002 - annualreviews.org
▪ Abstract The primary function of bacterial recombination systems is the nonmutagenic
repair of stalled or collapsed replication forks. The RecA protein plays a central role in these …
repair of stalled or collapsed replication forks. The RecA protein plays a central role in these …
[HTML][HTML] Full‐length archaeal Rad51 structure and mutants: mechanisms for RAD51 assembly and control by BRCA2
DS Shin, L Pellegrini, DS Daniels, B Yelent… - The EMBO …, 2003 - embopress.org
To clarify RAD51 interactions controlling homologous recombination, we report here the
crystal structure of the full‐length RAD51 homolog from Pyrococcus furiosus. The structure …
crystal structure of the full‐length RAD51 homolog from Pyrococcus furiosus. The structure …
Domain structure and dynamics in the helical filaments formed by RecA and Rad51 on DNA
X Yu, SA Jacobs, SC West, T Ogawa… - Proceedings of the …, 2001 - National Acad Sciences
Both the bacterial RecA protein and the eukaryotic Rad51 protein form helical nucleoprotein
filaments on DNA that catalyze strand transfer between two homologous DNA molecules …
filaments on DNA that catalyze strand transfer between two homologous DNA molecules …
Mechanism of strand exchange from RecA–DNA synaptic and D-loop structures
H Yang, C Zhou, A Dhar, NP Pavletich - Nature, 2020 - nature.com
The strand-exchange reaction is central to homologous recombination. It is catalysed by the
RecA family of ATPases, which form a helical filament with single-stranded DNA (ssDNA) …
RecA family of ATPases, which form a helical filament with single-stranded DNA (ssDNA) …
[HTML][HTML] In vitro role of Rad54 in Rad51-ssDNA filament-dependent homology search and synaptic complexes formation
Homologous recombination (HR) uses a homologous template to accurately repair DNA
double-strand breaks and stalled replication forks to maintain genome stability. During …
double-strand breaks and stalled replication forks to maintain genome stability. During …
The N-terminal domain of the human Rad51 protein binds DNA: structure and a DNA binding surface as revealed by NMR
Human Rad51 protein (HsRad51) is a homolog of Escherichia coli RecA protein, and
functions in DNA repair and recombination. In higher eukaryotes, Rad51 protein is essential …
functions in DNA repair and recombination. In higher eukaryotes, Rad51 protein is essential …
Molecular design and functional organization of the RecA protein
DA McGrew, KL Knight - Critical reviews in biochemistry and …, 2003 - Taylor & Francis
The bacterial RecA protein participates in a remarkably diverse set of functions, all of which
are involved in the maintenance of genomic integrity. RecA is a central component in both …
are involved in the maintenance of genomic integrity. RecA is a central component in both …
BRCA2 BRC motifs bind RAD51–DNA filaments
Germ-line mutations in BRCA2 account for approximately half the cases of autosomal
dominant familial breast cancers. BRCA2 has been shown to interact directly with RAD51 …
dominant familial breast cancers. BRCA2 has been shown to interact directly with RAD51 …
[HTML][HTML] ATP-mediated conformational changes in the RecA filament
MS VanLoock, X Yu, S Yang, AL Lai, C Low… - Structure, 2003 - cell.com
The crystal structure of the E. coli RecA protein was solved more than 10 years ago, but it
has provided limited insight into the mechanism of homologous genetic recombination …
has provided limited insight into the mechanism of homologous genetic recombination …