Abstract:
:CheY, the response regulator of the chemotaxis system in Escherichia coli, can be regulated by two covalent modifications - phosphorylation and acetylation. Both covalent modifications are involved in chemotaxis, but the mechanism and role of the acetylation are still obscure. While acetylation was shown to repress the binding of CheY to its target proteins, the effect of acetylation on the ability of CheY to undergo autophosphorylate with AcP is not fully investigated. To obtain more information on the function of this acetylation, we successfully expressed and purified CheY protein with a 6 × His-tag on the C-terminus. Subsequently, acetylated CheY (AcCheY) was obtained with AcCoA as the acetyl donor, and the acetylation level of AcCheY was confirmed by Western blotting and then mass spectrometry. Using tryptophan fluorescence intensity measurements as a monitor of phosphorylation, we showed that acetylation reduces the ability of CheY to undergo autophosphorylation.
journal_name
FEMS Microbiol Lettjournal_title
FEMS microbiology lettersauthors
Li R,Chen P,Gu J,Deng JYdoi
10.1111/1574-6968.12224subject
Has Abstractpub_date
2013-10-01 00:00:00pages
70-6issue
1eissn
0378-1097issn
1574-6968journal_volume
347pub_type
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