Abstract
Rad52 protein plays a central role in double strand break repair and homologous recombination in Saccharomyces cerevisiae. We have identified a new mechanism by which Rad52 protein stimulates Rad51 protein-promoted DNA strand exchange. This function of Rad52 protein is revealed when subsaturating amounts (relative to the single-stranded DNA concentration) of replication protein-A (RPA) are used. Under these conditions, Rad52 protein is needed for extensive DNA strand exchange. Interestingly, in this new role, Rad52 protein neither acts simply as a single strand DNA-binding protein per se nor, in contrast to its previously identified stimulatory roles, does it require physical interaction with RPA because it can be substituted by the Escherichia coli single strand DNA-binding protein. We propose that Rad52 protein acts by stabilizing the Rad51 presynaptic filament.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 26171-26176 |
| Number of pages | 6 |
| Journal | Journal of Biological Chemistry |
| Volume | 277 |
| Issue number | 29 |
| DOIs | |
| State | Published - Jul 19 2002 |
Fingerprint
ASJC Scopus subject areas
- Biochemistry
Cite this
Rad52 protein has a second stimulatory role in DNA strand exchange that complements replication protein-A function. / New, James H.; Kowalczykowski, Stephen C.
In: Journal of Biological Chemistry, Vol. 277, No. 29, 19.07.2002, p. 26171-26176.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Rad52 protein has a second stimulatory role in DNA strand exchange that complements replication protein-A function
AU - New, James H.
AU - Kowalczykowski, Stephen C.
PY - 2002/7/19
Y1 - 2002/7/19
N2 - Rad52 protein plays a central role in double strand break repair and homologous recombination in Saccharomyces cerevisiae. We have identified a new mechanism by which Rad52 protein stimulates Rad51 protein-promoted DNA strand exchange. This function of Rad52 protein is revealed when subsaturating amounts (relative to the single-stranded DNA concentration) of replication protein-A (RPA) are used. Under these conditions, Rad52 protein is needed for extensive DNA strand exchange. Interestingly, in this new role, Rad52 protein neither acts simply as a single strand DNA-binding protein per se nor, in contrast to its previously identified stimulatory roles, does it require physical interaction with RPA because it can be substituted by the Escherichia coli single strand DNA-binding protein. We propose that Rad52 protein acts by stabilizing the Rad51 presynaptic filament.
AB - Rad52 protein plays a central role in double strand break repair and homologous recombination in Saccharomyces cerevisiae. We have identified a new mechanism by which Rad52 protein stimulates Rad51 protein-promoted DNA strand exchange. This function of Rad52 protein is revealed when subsaturating amounts (relative to the single-stranded DNA concentration) of replication protein-A (RPA) are used. Under these conditions, Rad52 protein is needed for extensive DNA strand exchange. Interestingly, in this new role, Rad52 protein neither acts simply as a single strand DNA-binding protein per se nor, in contrast to its previously identified stimulatory roles, does it require physical interaction with RPA because it can be substituted by the Escherichia coli single strand DNA-binding protein. We propose that Rad52 protein acts by stabilizing the Rad51 presynaptic filament.
UR - http://www.scopus.com/inward/record.url?scp=0037135538&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0037135538&partnerID=8YFLogxK
U2 - 10.1074/jbc.M203670200
DO - 10.1074/jbc.M203670200
M3 - Article
C2 - 12004070
AN - SCOPUS:0037135538
VL - 277
SP - 26171
EP - 26176
JO - Journal of Biological Chemistry
JF - Journal of Biological Chemistry
SN - 0021-9258
IS - 29
ER -