
RAD52 - Wikipedia
RAD52 homolog (S. cerevisiae), also known as RAD52, is a protein which in humans is encoded by the RAD52 gene. [5][6] The protein encoded by this gene shares similarity with Saccharomyces cerevisiae Rad52, a protein important for DNA double-strand break repair and homologous recombination.
Mechanism of single-stranded DNA annealing by RAD52–RPA ...
2024年4月24日 · RAD52 is important for the repair of DNA double-stranded breaks 1, 2, mitotic DNA synthesis 3, 4, 5 and alternative telomere length maintenance 6, 7. Central to these functions, RAD52 promotes...
New roles for RAD52 in DNA repair | Cell Research - Nature
2018年10月26日 · Rad52 is among the most important proteins for genome maintenance in yeast, but it seemed mysteriously inconsequential for DNA repair in higher eukaryotes. However, this viewpoint is quickly...
Current Understanding of RAD52 Functions: Fundamental and ...
At DNA double-strand breaks, RAD52 was demonstrated to spur alternative pathways to compensate for the loss of homologous recombination functions. At collapsed replication forks, RAD52 activates break-induced replication. In the M phase, RAD52 promotes the finalization of DNA replication.
Rad52: Current Biology - Cell Press
2009年8月25日 · What is the Rad52 protein? The Saccharomyces cerevisiae Rad52 protein is a key player in DNA double-strand break repair and homologous recombination. It forms a heptameric ring, catalyses DNA annealing and mediates Rad51-catalysed strand invasion.
RAD52: Paradigm of Synthetic Lethality and New Developments
2021年11月23日 · Rad52 is one of the key HR proteins in eukaryotes. Although it is critical for most DNA repair and recombination events in yeast, knockouts of mammalian RAD52 lack any discernable phenotypes. As a consequence, mammalian RAD52 has been long overlooked.
Physiological and Pathological Roles of RAD52 at DNA ...
2020年2月10日 · RAD52 is a gatekeeper that limits excessive replication fork reversal. Upon fork stalling, RAD52 can associate with parental ssDNA at fork. Binding of RAD52 at fork can induce a rearrangement of the DNA closing the Y structure to counteract recruitment of fork reversal enzymes such as SMARCAL1 or ZRANB3.