Identification of communication networks in Spo0F: a model for phosphorylation-induced conformational change and implications for activation of multiple domain bacterial response regulators

FEBS Letters
V A FeherJohn Cavanagh

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.

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Citations

Mar 9, 1999·Trends in Microbiology·R E Silversmith, R B Bourret
Jun 18, 2002·Molecular Microbiology·Sophie J Stephenson, Marta Perego
Mar 29, 2014·Current Opinion in Structural Biology·Victoria A FeherRommie E Amaro
May 10, 2000·The Journal of Biological Chemistry·M A Cervin, G B Spiegelman
Dec 8, 2005·Biometals : an International Journal on the Role of Metal Ions in Biology, Biochemistry, and Medicine·Douglas J KojetinJohn Cavanagh
Jan 11, 2008·Molecular Plant-microbe Interactions : MPMI·Wei QianChaozu He
Mar 25, 2000·Journal of Molecular Biology·R J LewisA J Wilkinson

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