Literature DB >> 8639527

Conserved C-terminus of the phosphatase CheZ is a binding domain for the chemotactic response regulator CheY.

Y Blat1, M Eisenbach.   

Abstract

CheZ is the phosphatase of the chemotactic response regulator, CheY. There are three conserved domains on CheZ. Here we determined the function of the C-terminal domain (residues 202-214). A truncated form of CheZ, missing residues 202-214, hardly bound to the phosphorylated form of CheY. Conversely, a peptide composed of the last 19 amino acid residues of the CheZ (residues 196-214), generated by tryptic digestion, bound specifically to the phosphorylated form of CheY. This was demonstrated by both fluorescence depolarization of the peptide (labeled with fluorescein) and cross-linking. It is concluded that the conserved C-terminus of CheZ functions as a CheY-binding domain.

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Year:  1996        PMID: 8639527     DOI: 10.1021/bi9530447

Source DB:  PubMed          Journal:  Biochemistry        ISSN: 0006-2960            Impact factor:   3.162


  16 in total

1.  Isolation and characterization of nonchemotactic CheZ mutants of Escherichia coli.

Authors:  K C Boesch; R E Silversmith; R B Bourret
Journal:  J Bacteriol       Date:  2000-06       Impact factor: 3.490

Review 2.  How signals are heard during bacterial chemotaxis: protein-protein interactions in sensory signal propagation.

Authors:  A Bren; M Eisenbach
Journal:  J Bacteriol       Date:  2000-12       Impact factor: 3.490

3.  Conformational coupling in the chemotaxis response regulator CheY.

Authors:  M Schuster; R E Silversmith; R B Bourret
Journal:  Proc Natl Acad Sci U S A       Date:  2001-05-15       Impact factor: 11.205

4.  The structures of T87I phosphono-CheY and T87I/Y106W phosphono-CheY help to explain their binding affinities to the FliM and CheZ peptides.

Authors:  Kenneth McAdams; Eric S Casper; R Matthew Haas; Bernard D Santarsiero; Aimee L Eggler; Andrew Mesecar; Christopher J Halkides
Journal:  Arch Biochem Biophys       Date:  2008-09-05       Impact factor: 4.013

5.  Computer-aided resolution of an experimental paradox in bacterial chemotaxis.

Authors:  W N Abouhamad; D Bray; M Schuster; K C Boesch; R E Silversmith; R B Bourret
Journal:  J Bacteriol       Date:  1998-08       Impact factor: 3.490

6.  Action at a distance: amino acid substitutions that affect binding of the phosphorylated CheY response regulator and catalysis of dephosphorylation can be far from the CheZ phosphatase active site.

Authors:  Ashalla M Freeman; Beth M Mole; Ruth E Silversmith; Robert B Bourret
Journal:  J Bacteriol       Date:  2011-07-15       Impact factor: 3.490

Review 7.  The two-component signaling pathway of bacterial chemotaxis: a molecular view of signal transduction by receptors, kinases, and adaptation enzymes.

Authors:  J J Falke; R B Bass; S L Butler; S A Chervitz; M A Danielson
Journal:  Annu Rev Cell Dev Biol       Date:  1997       Impact factor: 13.827

8.  In vivo and in vitro characterization of Escherichia coli protein CheZ gain- and loss-of-function mutants.

Authors:  M G Sanna; M I Simon
Journal:  J Bacteriol       Date:  1996-11       Impact factor: 3.490

9.  Helicobacter pylori CheZ(HP) and ChePep form a novel chemotaxis-regulatory complex distinct from the core chemotaxis signaling proteins and the flagellar motor.

Authors:  Paphavee Lertsethtakarn; Michael R Howitt; Juan Castellon; Manuel R Amieva; Karen M Ottemann
Journal:  Mol Microbiol       Date:  2015-07-04       Impact factor: 3.501

Review 10.  Diversity in chemotaxis mechanisms among the bacteria and archaea.

Authors:  Hendrik Szurmant; George W Ordal
Journal:  Microbiol Mol Biol Rev       Date:  2004-06       Impact factor: 11.056

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