The goal of this research proposal is to determine and examine crystal structures of three """"""""Tra"""""""" proteins that comprise the """"""""relaxosome"""""""", a nucleoprotein complex which is responsible for the nicking and unwinding of the plasmid DNA during conjugative DNA transfer (CDT). CDT is the process by which a conjugative plasmid is transferred between bacterial cells and is therefore an important mechanism for the horizontal transfer of genetic information amongst bacterial populations. The transfer process includes the formation of a stable mating pair between donor and recipient cells, nicking and unwinding of donor plasmid DNA, and transfer into the recipient cell. This entire process is orchestrated via a host of protein-protein and DNA-protein interactions, and while most of the players involved in this process have been identified, our understanding of the interactions between these players and links between each step of CDT remain poorly defined. Structures of the """"""""relaxosome"""""""" proteins Tral, TraY and TraM both alone and in the presence of DNA will allow us to identify structural elements which are important for contact with plasmid DNA as well as drive subsequent biochemical and biophysical experiments aimed at understanding relaxosome protein contacts.

Agency
National Institute of Health (NIH)
Institute
National Institute of General Medical Sciences (NIGMS)
Type
Postdoctoral Individual National Research Service Award (F32)
Project #
1F32GM075588-01
Application #
6998637
Study Section
Special Emphasis Panel (ZRG1-F04B (20))
Program Officer
Flicker, Paula F
Project Start
2005-08-01
Project End
2008-07-31
Budget Start
2005-08-01
Budget End
2006-07-31
Support Year
1
Fiscal Year
2005
Total Cost
$43,976
Indirect Cost
Name
University of North Carolina Chapel Hill
Department
Chemistry
Type
Schools of Arts and Sciences
DUNS #
608195277
City
Chapel Hill
State
NC
Country
United States
Zip Code
27599