Alteration of a Nonconserved Active Site Residue in the Chemotaxis Response Regulator CheY Affects Phosphorylation and Interaction with CheZ
Open Access
- 1 May 2001
- journal article
- Published by Elsevier
- Vol. 276 (21) , 18478-18484
- https://doi.org/10.1074/jbc.m011418200
Abstract
No abstract availableKeywords
This publication has 46 references indexed in Scilit:
- Two-Component Signal TransductionAnnual Review of Biochemistry, 2000
- NMR structure of activated CheYJournal of Molecular Biology, 2000
- Identification of the binding interfaces on CheY for two of its targets the phosphatase CheZ and the flagellar switch protein FliMJournal of Molecular Biology, 1999
- Kinetic Characterization of CheY Phosphorylation Reactions: Comparison of P-CheA and Small-Molecule PhosphodonorsBiochemistry, 1999
- Regulation of phosphatase activity in bacterial chemotaxisJournal of Molecular Biology, 1998
- THE TWO-COMPONENT SIGNALING PATHWAY OF BACTERIAL CHEMOTAXIS: A Molecular View of Signal Transduction by Receptors, Kinases, and Adaptation EnzymesAnnual Review of Cell and Developmental Biology, 1997
- Mutants with Defective Phosphatase Activity Show No Phosphorylation-dependent Oligomerization of CheZ: THE PHOSPHATASE OF BACTERIAL CHEMOTAXISPublished by Elsevier ,1996
- Oligomerization of the Phosphatase CheZ Upon Interaction with the Phosphorylated Form of CheY: THE SIGNAL PROTEIN OF BACTERIAL CHEMOTAXISPublished by Elsevier ,1996
- Structure of the Escherichia coli Response Regulator NarL,Biochemistry, 1996
- Magnesium Binding to the Bacterial Chemotaxis Protein CheY Results in Large Conformational Changes Involving its Functional SurfaceJournal of Molecular Biology, 1994