Meiotic recombination is essential for the linkage of homologous chromosomes to prepare them for disjunction in meiosis I. This process is promoted by two recombinase enzymes, Rad51 and Dmc1 that have the ability to pair and exchange strands between homologous DNA molecules. While Rad51 has been characterized fairly well, little is known about the recombinase activity of Dmc1. This research project will employ a variety of biochemical methods and electron microscopy to (1) define the activities of a spliced form of hDmcl and examine whether this hDmcl variant physically and functionally interacts with the full length protein and (2) delineate the role that Rad54B plays in hDmcl-mediated recombination reactions. The proposed studies should shed some light on the action mechanism of hDmcl and make a significant contribution toward understanding meiotic recombination in humans. ? ?

Agency
National Institute of Health (NIH)
Institute
National Institute of General Medical Sciences (NIGMS)
Type
Postdoctoral Individual National Research Service Award (F32)
Project #
1F32GM074529-01
Application #
6936732
Study Section
Special Emphasis Panel (ZRG1-F08 (20))
Program Officer
Haynes, Susan R
Project Start
2005-07-01
Project End
2006-06-30
Budget Start
2005-07-01
Budget End
2006-06-30
Support Year
1
Fiscal Year
2005
Total Cost
$48,296
Indirect Cost
Name
Yale University
Department
Biochemistry
Type
Schools of Medicine
DUNS #
043207562
City
New Haven
State
CT
Country
United States
Zip Code
06520
Chi, Peter; Van Komen, Stephen; Sehorn, Michael G et al. (2006) Roles of ATP binding and ATP hydrolysis in human Rad51 recombinase function. DNA Repair (Amst) 5:381-91