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

被引:21
作者
Feher, VA
Tzeng, YL
Hoch, JA
Cavanagh, J [1 ]
机构
[1] New York State Dept Hlth, Wadsworth Ctr, NMR Struct Biol Facil, Albany, NY 12201 USA
[2] Scripps Res Inst, Dept Mol & Expt Med, La Jolla, CA 92037 USA
关键词
phosphorylation; aspartyl phosphate; protein dynamics; response regulator; Spo0F;
D O I
10.1016/S0014-5793(98)00182-3
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
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. (C) 1998 Federation of European Biochemical Societies.
引用
收藏
页码:1 / 6
页数:6
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