Open AccessBacterial chemotaxis signaling complexes: formation of a CheA/CheW complex enhances autophosphorylation and affinity for CheY.
Author(s) -
Dennis Francis. McNally,
Philip Matsumura
Publication year - 1991
Publication title -
proceedings of the national academy of sciences of the united states of america
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.011
H-Index - 771
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.88.14.6269
Subject(s) - autophosphorylation , chemotaxis , phosphorylation , biochemistry , mutant , microbiology and biotechnology , biology , chemistry , signaling proteins , biophysics , receptor , protein kinase a , gene
We have demonstrated that a complex of the proteins CheA (CheAL and CheAS) and CheW can be isolated and constitutes a functional unit that responds to the signaling state of the chemoreceptors. The autophosphorylation rate of CheAL is much greater when CheAL and CheAS are complexed with CheW. Moreover, the presence of mutant chemoreceptors that cause cells to tumble increases this rate. At wild-type levels of expression, the isolated CheAL/CheAS/CheW complex accounts for about 10% of the total number of CheAL, CheAS, and CheW molecules and exists in a 1:1:1 stoichiometry. This complex is also required for CheAL/CheAS and CheW binding to the phosphorylation substrate, CheY. A separate interaction between CheY and another chemotaxis component, CheZ, was also detected. The CheY-CheZ interaction does not require participation of the CheAL/CheAS/CheW complex.