title: Identification of communication networks in Spo0F: a model for phosphorylation-induced conformational change and implications for activation of multiple domain bacterial response regulators.
abstract: 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.
authors.affiliation: NMR Structural Biology Facility, Wadsworth Center, New York State Department of Health, Albany 12201, USA.
authors.forename: V A
authors.initials: VA
authors.lastname: Feher
authors.forename: Y L
authors.initials: YL
authors.lastname: Tzeng
authors.forename: J A
authors.initials: JA
authors.lastname: Hoch
authors.forename: J
authors.initials: J
authors.lastname: Cavanagh
mesh_terms: 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*
chemical_list: D001426:Bacterial Proteins; C080951:Spo0F protein, Bacillus subtilis