Date of Completion
Victoria Robinson, David Knecht, Debra Kendall
Cell and Developmental Biology | Cell Biology | Molecular Biology
Bacterial GTPases regulate many cell functions, including the stress response, signal recognition, protein synthesis, and cell differentiation, through a molecular switch that is activated and deactivated depending on their nucleotide bound state (1). A member of the translational family of bacterial GTPases along with LepA and EF-G, BipA is a 67 kD protein that is essential for virulence and the stress response. Crystal structures from the Robinson lab have shown a unique C-terminal domain on BipA that has been implicated in ribosome binding. Using N-terminal deletion constructs, we have shown that the C-terminal domain is necessary, but not sufficient, to promote interaction of BipA with the ribosome. We have also identified key structural elements within the CTD that are required for ribosome association and have investigated amino acid residues within those elements. Because BipA exerts it function through interactions with the ribosome, these data serve as a preliminary step to elucidating BipA’s role in the cell.
Makanji, Heeren, "Contribution of the Novel C-terminal Domain to the Ribosome Binding Activities of Virulence Regulator BipA" (2009). Honors Scholar Theses. 85.