| KREJCI, Lumir, Binwei SONG, Wendy BUSSEN, Rodney ROTHSTEIN, Uffe MORTENSEN and Patrick SUNG. Interaction with Rad51 is indispensable for recombination mediator function of Rad52. Online. Journal of Biological Chemistry. Bethesda, USA: Amer. Soc. Biochem. Mol. Biol., 2002, vol. 277, No 42, p. 40132-41, 9 pp. ISSN 0021-9258. [citováno 2024-04-24] |
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@article{708584,
author = {Krejci, Lumir and Song, Binwei and Bussen, Wendy and Rothstein, Rodney and Mortensen, Uffe and Sung, Patrick},
article_location = {Bethesda, USA},
article_number = {42},
keywords = {Recombination; repair; Rad52; mediator proteins},
language = {eng},
issn = {0021-9258},
journal = {Journal of Biological Chemistry},
title = {Interaction with Rad51 is indispensable for recombination mediator function of Rad52.},
volume = {277},
year = {2002}
}
TY - JOUR
ID - 708584
AU - Krejci, Lumir - Song, Binwei - Bussen, Wendy - Rothstein, Rodney - Mortensen, Uffe - Sung, Patrick
PY - 2002
TI - Interaction with Rad51 is indispensable for recombination mediator function of Rad52.
JF - Journal of Biological Chemistry
VL - 277
IS - 42
SP - 40132-41
EP - 40132-41
PB - Amer. Soc. Biochem. Mol. Biol.
SN - 00219258
KW - Recombination
KW - repair
KW - Rad52
KW - mediator proteins
N2 - In the yeast Saccharomyces cerevisiae, the RAD52 gene is indispensable for homologous recombination and DNA repair. Rad52 protein binds DNA, anneals complementary ssDNA strands, and self-associates to form multimeric complexes. Moreover, Rad52 physically interacts with the Rad51 recombinase and serves as a mediator in the Rad51-catalyzed DNA strand exchange reaction. Here, we examine the functional significance of the Rad51/Rad52 interaction. Through a series of deletions, we have identified residues 409-420 of Rad52 as being indispensable and likely sufficient for its interaction with Rad51. We have constructed a four-amino acid deletion mutation within this region of Rad52 to ablate its interaction with Rad51. We show that the rad52delta409-412 mutant protein is defective in the mediator function in vitro even though none of the other Rad52 activities, namely, DNA binding, ssDNA annealing, and protein oligomerization, are affected. We also show that the sensitivity of the rad52delta409-412 mutant to ionizing radiation can be complemented by overexpression of Rad51. These results thus demonstrate the significance of the Rad51-Rad52 interaction in homologous recombination
ER -
KREJCI, Lumir, Binwei SONG, Wendy BUSSEN, Rodney ROTHSTEIN, Uffe MORTENSEN and Patrick SUNG. Interaction with Rad51 is indispensable for recombination mediator function of Rad52. Online. \textit{Journal of Biological Chemistry}. Bethesda, USA: Amer. Soc. Biochem. Mol. Biol., 2002, vol.~277, No~42, p.~40132-41, 9 pp. ISSN~0021-9258. [citováno 2024-04-24]
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