Identification of communication networks in Spo0F: a model for phosphorylation-induced conformational change and implications for activation of multiple domain bacterial response regulators.
Fundamental to understanding the mechanism by which phosphorylation activates bacterial signal transduction response regulator proteins is the identification of regions and residues that are responsible for the phosphorylation-induced conformational change. Here we review results from structural and protein dynamics investigations, and combine them with mutagenesis studies on the response regulator protein SpoOF to suggest a model in which a network of buried and surface residues link surface regions required for protein:protein interactions to the site of phosphorylation. The network described for SpoOF may provide pathways through which information is transmitted from the site of phosphorylation, propagating a conformational change many angstroms away. The general applicability of the communication network model for all bacterial response regulator proteins is discussed.
Feher
V A
VA
NMR Structural Biology Facility, Wadsworth Center, New York State Department of Health, Albany 12201, USA.
Tzeng
Y L
YL
Hoch
J A
JA
Cavanagh
J
J
D001426:Bacterial Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D008956:Models, Chemical; D016296:Mutagenesis; D010766:Phosphorylation; D011487:Protein Conformation; D015398:Signal Transduction; D013171:Spores, Bacterial / Q000378:metabolism*
D001426:Bacterial Proteins; C080951:Spo0F protein, Bacillus subtilis