Wang H, Matsumura P
Department of Microbiology and Immunology, University of Illinois at Chicago, 60612-7344, USA.
J Bacteriol. 1997 Jan;179(1):287-9. doi: 10.1128/jb.179.1.287-289.1997.
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).
在最佳运动条件下,确定了CheA(L)(654个氨基酸)与CheA(S)(557个氨基酸)的化学计量比为1:1。还发现CheZ与CheA(S)的结合受到CheA(L)-CheA(S)-CheW相互作用的抑制。这表明CheA(S)在磷酸化复合物(CheA(L)-CheA(S)-CheW)和去磷酸化复合物(CheA(S)-CheZ)中具有不同的功能。