Phosphorylating and dephosphorylating protein complexes in bacterial chemotaxis.
During optimal motility conditions, a 1:1 stoichiometry of CheA(L) (654 amino acids) to CheA(S) (557 amino acids) was determined. It was also found that CheZ binding to CheA(S) was inhibited by CheA(L)-CheA(S)-CheW interaction. This suggests that CheA(S) has different functions in the phosphorylating complex (CheA(L)-CheA(S)-CheW) and in the dephosphorylating complex (CheA(S)-CheZ).
Wang
H
H
Department of Microbiology and Immunology, University of Illinois at Chicago, 60612-7344, USA.
Matsumura
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P
D001419:Bacteria / Q000166:cytology; D001426:Bacterial Proteins / Q000378:metabolism*; D002633:Chemotaxis / Q000502:physiology*; D008565:Membrane Proteins / Q000378:metabolism*; D000072236:Methyl-Accepting Chemotaxis Proteins; D010766:Phosphorylation; D011485:Protein Binding
D001426:Bacterial Proteins; D008565:Membrane Proteins; D000072236:Methyl-Accepting Chemotaxis Proteins