Další formáty:
BibTeX
LaTeX
RIS
@article{792244,
author = {Seong, Changhyuan and Sehorn, Michael and Plate, Iben and Shi, Idina and Song, Binway and Chi, Peter and Mortensen, Uffe and Sung, Patrick and Krejčí, Lumír},
article_number = {283},
keywords = {Rad52; recombination mediator; DNA repair},
language = {eng},
issn = {0021-9258},
journal = {J. Biol. Chem.},
title = {Molecular anatomy of the recombination mediator function of Saccharomyces cerevisiae Rad52},
url = {http://www.jbc.org/cgi/content/full/283/18/12166},
volume = {18},
year = {2008}
}
TY - JOUR
ID - 792244
AU - Seong, Changhyuan - Sehorn, Michael - Plate, Iben - Shi, Idina - Song, Binway - Chi, Peter - Mortensen, Uffe - Sung, Patrick - Krejčí, Lumír
PY - 2008
TI - Molecular anatomy of the recombination mediator function of Saccharomyces cerevisiae Rad52
JF - J. Biol. Chem.
VL - 18
IS - 283
SP - 12166-74
EP - 12166-74
SN - 00219258
KW - Rad52
KW - recombination mediator
KW - DNA repair
UR - http://www.jbc.org/cgi/content/full/283/18/12166
N2 - A helical filament of Rad51 on single-strand DNA (ssDNA), called the presynaptic filament, catalyzes DNA joint formation during homologous recombination. Rad52 facilitates presynaptic filament assembly, and this recombination mediator activity is thought to rely on the interactions of Rad52 with Rad51, the ssDNA-binding protein RPA, and ssDNA. The N-terminal region of Rad52, which has DNA binding activity and an oligomeric structure, is thought to be crucial for mediator activity and recombination. Unexpectedly, we find that the C-terminal region of Rad52 also harbors a DNA binding function. Importantly, the Rad52 C-terminal portion alone can promote Rad51 presynaptic filament assembly. The middle portion of Rad52 associates with DNA-bound RPA and contributes to the recombination mediator activity. Accordingly, expression of a protein species that harbors the middle and C-terminal regions of Rad52 in the rad52 Delta327 background enhances the association of Rad51 protein with a HO-made DNA double-strand break and partially complements the methylmethane sulfonate sensitivity of the mutant cells. Our results provide a mechanistic framework for rationalizing the multi-faceted role of Rad52 in recombination and DNA repair.
ER -
SEONG, Changhyuan, Michael SEHORN, Iben PLATE, Idina SHI, Binway SONG, Peter CHI, Uffe MORTENSEN, Patrick SUNG a Lumír KREJČÍ. Molecular anatomy of the recombination mediator function of Saccharomyces cerevisiae Rad52. \textit{J. Biol. Chem.}. 2008, roč.~18, č.~283, s.~12166-74, 8 s. ISSN~0021-9258.
|
