NDLI: Human and yeast Rad52 proteins promote DNA strand exchange

Content Provider	PubMed Central
Author	Bi, Baoyuan Rybalchenko, Nataliya Golub, Efim I. Radding, Charles M.
Copyright Year	2004
Abstract	Studies of rad52 mutants in Saccharomyces cerevisiae have revealed a critical role of Rad52 protein in double-strand break repair and meiosis, and roles in both RAD51-dependent and -independent pathways of recombination. In vitro, both yeast and human Rad52 proteins play auxiliary roles with RPA in the action of Rad51. Rad52 also has annealing activity and promotes the formation of D-loops in superhelical DNA. The experiments described here show that Homo sapiens (Hs)Rad52 and yeast Rad52 proteins promote strand exchange as well. Strand exchange was promoted by the N-terminal domain of HsRad52 that contains residues 1–237, which includes the residues required to form rings of Rad52, whereas other truncated domains, both N-terminal and C-terminal, were inactive. For both yeast Rad52 and HsRad52, the yield of strand-exchange reactions was proportional to the fractional A·T content of the DNA substrates, but both enzymes catalyzed exchange with substrates that contained up to at least 50% G·C. Observations made on S. cerevisiae Rad52 protein from mutants with severe recombination deficiencies indicate that the strand-exchange activity measured in vitro reflects a biologically significant property of Rad52 protein.
Related Links	http://dx.doi.org/10.1073/pnas.0403205101
Ending Page	9572
Page Count	5
Starting Page	9568
File Format	PDF
ISSN	00278424
e-ISSN	10916490
Journal	Proceedings of the National Academy of Sciences of the United States of America
Issue Number	26
Volume Number	101
Language	English
Publisher	National Academy of Sciences
Publisher Date	2004-06-29
Access Restriction	Open
Rights Holder	National Academy of Sciences
Subject Keyword	General Research in Higher Education
Content Type	Text
Resource Type	Article
Subject	Multidisciplinary

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Human and yeast Rad52 proteins promote DNA strand exchange.

Strand exchange activity of human recombination protein Rad52

DNA strand annealing is promoted by the yeast Rad52 protein.

The RecA proteins of Deinococcus radiodurans and Escherichia coli promote DNA strand exchange via inverse pathways

Complex formation in yeast double-strand break repair: participation of Rad51, Rad52, Rad55, and Rad57 proteins.

DNA strand annealing is promoted by the yeast Rad52 protein.

Strand exchange activity of human recombination protein Rad52.

Structure of the single-strand annealing domain of human RAD52 protein

Occurrence of crossed strand-exchange forms in yeast DNA during meiosis.

Human and yeast Rad52 proteins promote DNA strand exchange

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Human and yeast Rad52 proteins promote DNA strand exchange