TY - JOUR
T1 - RAB22 and RAB163/mouse BRCA2
T2 - Proteins that specifically interact with the RAD51 protein
AU - Mizuta, Ryushin
AU - LaSalle, Janine M.
AU - Cheng, Hwei Ling
AU - Shinohara, Akira
AU - Ogawa, Hideyuki
AU - Copeland, Neal
AU - Jenkins, Nancy A.
AU - Lalande, Marc
AU - Alt, Frederick W.
N1 - Copyright:
Copyright 2007 Elsevier B.V., All rights reserved.
PY - 1997/6/24
Y1 - 1997/6/24
N2 - The human RAD51 protein is a homologue of the bacteria RecA and yeast RAD51 proteins that are involved in homologous recombination and DNA repair. RAD51 interacts with proteins involved in recombination and also with tumor suppressor proteins p53 and breast cancer susceptibility gene 1 (BRCA1). We have used the yeast two-hybrid system to clone murine cDNA sequences that encode two RAD51-associated molecules, RAB22 and RAB163. RAB163 encodes the C-terminal portion of mouse BRCA2, the homologue of the second breast cancer susceptibility gene protein in humans, demonstrating an in vitro association between RAD51 and BRCA2. RAB22 is a novel gene product that also interacts with RAD51 in vitro. To detect RAD51 interactions in vivo, we developed a transient nuclear focus assay that was used to demonstrate a complete colocalization of RAB22 with RAD51 in large nuclear foci.
AB - The human RAD51 protein is a homologue of the bacteria RecA and yeast RAD51 proteins that are involved in homologous recombination and DNA repair. RAD51 interacts with proteins involved in recombination and also with tumor suppressor proteins p53 and breast cancer susceptibility gene 1 (BRCA1). We have used the yeast two-hybrid system to clone murine cDNA sequences that encode two RAD51-associated molecules, RAB22 and RAB163. RAB163 encodes the C-terminal portion of mouse BRCA2, the homologue of the second breast cancer susceptibility gene protein in humans, demonstrating an in vitro association between RAD51 and BRCA2. RAB22 is a novel gene product that also interacts with RAD51 in vitro. To detect RAD51 interactions in vivo, we developed a transient nuclear focus assay that was used to demonstrate a complete colocalization of RAB22 with RAD51 in large nuclear foci.
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U2 - 10.1073/pnas.94.13.6927
DO - 10.1073/pnas.94.13.6927
M3 - Article
C2 - 9192668
AN - SCOPUS:0030966227
VL - 94
SP - 6927
EP - 6932
JO - Proceedings of the National Academy of Sciences of the United States of America
JF - Proceedings of the National Academy of Sciences of the United States of America
SN - 0027-8424
IS - 13
ER -