Recombinant Escherichia coli Chemotaxis protein CheY (cheY)

1. study identified K91 and K109 as the major sites whose acetylation level in vivo increases in response to acetate PMID: 25388160
2. the enhanced reactivity of CheY DR reflected partial acquisition of catalytic and structural features of HAD phosphatases. PMID: 25928369
3. Authors observe an apparent decrease and redistribution of mus-ms dynamics of allosteric response upon phosphorylation (and accompanying Mg(2+) saturation) of CheY. PMID: 23648838
4. The flagellar motor adapts to changes in steady-state level of chemotaxis response regulator CheY-P by adjusting the number of FliM molecules to which CheY-P binds. Extreme motor ultrasensitivity broadens our understanding of allostery mechanisms PMID: 23454041
5. F214A substitution in P2 of CheA caused 1,000-fold reduction in CheA-CheY binding affinity. PMID: 21642453
6. motor switching: the largest variations are in the mean counter-clockwise interval, and are attributable to variations in the concentration of the internal signaling molecule CheY-P PMID: 21422514
7. These results suggest that both phosphorylation and acetylation determine CheY's ability to bind to its target proteins, thus providing two levels of regulation, fast and slow respectively. PMID: 20398208
8. Chemotaxis signaling protein CheY binds to the rotor protein FliN to control the direction of flagellar rotation in Escherichia coli. PMID: 20439729
9. turnover of FliM molecules depends on the presence of active CheY, suggesting a potential role in the process of motor switching PMID: 20498085
10. Data show that CheY is partially acetylated in spite of the absence of acetyl-CoA synthetase, suggesting that CheY can be post-translationally acetylated in vivo by additional means. PMID: 16630631
11. crystallographic structure of unphosphorylated, magnesium(II)-bound CheY in complex with a synthetic peptide corresponding to the target region of FliM (the 16 N-terminal residues of FliM [FliM(16)]) PMID: 17050923
12. Study succeeded in detecting CheY acetylation in vivo by three means--Western blotting with a specific anti-acetyl-lysine antibody, mass spectrometry, and radiolabeling with [(14)C]acetate in the presence of protein-synthesis inhibitor. PMID: 18234227
13. The authors demonstrate that substitutions at two variable active site positions decreased CheY autodephosphorylation up to 40-fold and increased the Spo0F rate up to 110-fold. PMID: 18557815
14. Data suggest that CheY initially misfolds before accessing the native conformation. PMID: 18619461
15. Results describe the subdomain competition, cooperativity, and topological frustration in the folding of CheY. PMID: 18644380
16. Comparison of X-ray crystal structures of five CheY mutants gave strong evidence for steric obstruction of the phosphoryl group from the attacking water molecule as one mechanism to enhance phosphoryl group stability. PMID: 19646451

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KEGG: ecj:JW1871

STRING: 316385.ECDH10B_2023