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
相关论文
共 34 条
  • [11] LOWRY DF, 1994, J BIOL CHEM, V269, P26358
  • [12] LUKAT GS, 1991, J BIOL CHEM, V266, P8348
  • [13] Crystal structure of a phosphatase-resistant mutant of sporulation response regulator Spo0F from Bacillus subtilis
    Madhusudan
    Zapf, J
    Whiteley, JM
    Hoch, JA
    Xuong, NH
    Varughese, KI
    [J]. STRUCTURE, 1996, 4 (06) : 679 - 690
  • [14] Structural and functional analyses of activating amino acid substitutions in the receiver domain of NtrC: Evidence for an activating surface
    Nohaile, M
    Kern, D
    Wemmer, D
    Stedman, K
    Kustu, S
    [J]. JOURNAL OF MOLECULAR BIOLOGY, 1997, 273 (01) : 299 - 316
  • [15] Parkinson JS, 1995, 2 COMPONENT SIGNAL T, P9
  • [16] Cell-cell communication regulates the effects of protein aspartate phosphatases on the phosphorelay controlling development in Bacillus subtilis
    Perego, M
    Hoch, JA
    [J]. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1996, 93 (04) : 1549 - 1553
  • [17] Aspartyl-phosphate phosphatases deactivate the response regulator components of the sporulation signal transduction system in Bacillus subtilis
    Perego, M
    Glaser, P
    Hoch, JA
    [J]. MOLECULAR MICROBIOLOGY, 1996, 19 (06) : 1151 - 1157
  • [18] Yeast HOG1 MAP kinase cascade is regulated by a multistep phosphorelay mechanism in the SLN1-YPD1-SSK1 ''two-component'' osmosensor
    Posas, F
    WurglerMurphy, SM
    Maeda, T
    Witten, EA
    Thai, TC
    Saito, H
    [J]. CELL, 1996, 86 (06) : 865 - 875
  • [19] ROMAN SJ, 1992, J BACTERIOL, V174, P6237
  • [20] Structural basis of cyclin-dependent kinase activation by phosphorylation
    Russo, AA
    Jeffrey, PD
    Pavletich, NP
    [J]. NATURE STRUCTURAL BIOLOGY, 1996, 3 (08): : 696 - 700