Rad52

نویسندگان

  • Uffe H. Mortensen
  • Michael Lisby
  • Rodney Rothstein
چکیده

What is the Rad52 protein? The Saccharomyces cerevisiae Rad52 protein is a key player in DNA doublestrand break repair and homologous recombination. It forms a heptameric ring, catalyses DNA annealing and mediates Rad51-catalysed strand invasion. RAD52 is the defining member of an epistasis group of genes involved in repair of ionizing radiationinduced DNA double-strand breaks. Double-strand break repair catalysed by this group of proteins is generally error-free, because genetic information at the double-strand break is restored from an intact copy elsewhere in the genome. Rad52 homologues have been identified in eukaryotic organisms ranging from yeast to humans, but they appear to be absent in some life forms, such as plants and invertebrates. Although Rad52 plays a prominent role in homologous recombination and DNA double-strand break repair in S. cerevisiae, it plays a more modest role in vertebrates, where additional proteins like BRCA2 have evolved to perform similar functions. Nevertheless, the biochemical activities of Rad52 proteins from different species are very similar.

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منابع مشابه

DNA damage-inducible and RAD52-independent repair of DNA double-strand breaks in Saccharomyces cerevisiae.

Chromosomal repair was studied in stationary-phase Saccharomyces cerevisiae, including rad52/rad52 mutant strains deficient in repairing double-strand breaks (DSBs) by homologous recombination. Mutant strains suffered more chromosomal fragmentation than RAD52/RAD52 strains after treatments with cobalt-60 gamma irradiation or radiomimetic bleomycin, except after high bleomycin doses when chromos...

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Coordinated response of mammalian Rad51 and Rad52 to DNA damage.

Biochemical analysis has shown that mammalian Rad51 and Rad52 interact and synergize in DNA recombination reactions in vitro, but these proteins have not been shown to function together in response to DNA damage in vivo. By analysis of murine cells expressing murine Rad52 tagged with green fluorescent protein (GFP)-Rad52, we now show that DNA damage causes Rad51 and GFP-Rad52 to colocalize in d...

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A Saccharomyces cerevisiae RAD52 allele expressing a C-terminal truncation protein: activities and intragenic complementation of missense mutations.

A nonsense allele of the yeast RAD52 gene, rad52-327, which expresses the N-terminal 65% of the protein was compared to two missense alleles, rad52-1 and rad52-2, and to a deletion allele. While the rad52-1 and the deletion mutants have severe defects in DNA repair, recombination and sporulation, the rad52-327 and rad52-2 mutants retain either partial or complete capabilities in repair and reco...

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Identification of plant RAD52 homologs and characterization of the Arabidopsis thaliana RAD52-like genes.

RADiation sensitive52 (RAD52) mediates RAD51 loading onto single-stranded DNA ends, thereby initiating homologous recombination and catalyzing DNA annealing. RAD52 is highly conserved among eukaryotes, including animals and fungi. This article reports that RAD52 homologs are present in all plants whose genomes have undergone extensive sequencing. Computational analyses suggest a very early RAD5...

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Tyrosine phosphorylation enhances RAD52-mediated annealing by modulating its DNA binding

RAD52 protein has an important role in homology-directed DNA repair by mediating RAD51 nucleoprotein filament formation on single-stranded DNA (ssDNA) protected by replication protein-A (RPA) and annealing of RPA-coated ssDNA. In human, cellular response to DNA damage includes phosphorylation of RAD52 by c-ABL kinase at tyrosine 104. To address how this phosphorylation modulates RAD52 function,...

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A core activity associated with the N terminus of the yeast RAD52 protein is revealed by RAD51 overexpression suppression of C-terminal rad52 truncation alleles.

C-terminal rad52 truncation and internal deletion mutants were characterized for their ability to repair MMS-induced double-strand breaks and to produce viable spores during meiosis. The rad52-Delta251 allele, encoding the N-terminal 251 amino acids of the predicted 504-amino-acid polypeptide, supports partial activity for both functions. Furthermore, RAD51 overexpression completely suppresses ...

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عنوان ژورنال:
  • Current Biology

دوره 19  شماره 

صفحات  -

تاریخ انتشار 2009