Article: article from journal or magazin.
The human Rad52 protein exists as a heptameric ring.
Publication types: Journal Article ; Research Support, Non-U.S. Gov't ; Research Support, U.S. Gov't, P.H.S. Publication Status: ppublish
The RAD52 epistasis group was identified in yeast as a group of genes required to repair DNA damaged by ionizing radiation . Genetic evidence indicates that Rad52 functions in Rad51-dependent and Rad51-independent recombination pathways   . Consistent with this, purified yeast and human Rad52 proteins have been shown to promote single-strand DNA annealing    and to stimulate Rad51-mediated homologous pairing    . Electron microscopic examinations of the yeast  and human  Rad52 proteins have revealed their assembly into ring-like structures in vitro. Using both conventional transmission electron microscopy and scanning transmission electron microscopy (STEM), we found that the human Rad52 protein forms heptameric rings. A three-dimensional (3D) reconstruction revealed that the heptamer has a large central channel. Like the hexameric helicases such as Escherichia coli DnaB  , bacteriophage T7 gp4b  , simian virus 40 (SV40) large T antigen  and papilloma virus E1 , the Rad52 rings show a distinctly chiral arrangement of subunits. Thus, the structures formed by the hexameric helicases may be a more general property of other proteins involved in DNA metabolism, including those, such as Rad52, that do not bind and hydrolyze ATP.
Animals, Cell Line, DNA-Binding Proteins/ultrastructure, Humans, Rad52 DNA Repair and Recombination Protein, Recombinant Fusion Proteins/ultrastructure
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