Bacillus subtilis hydrolyzes CheY-P at the location of its action, the flagellar switch
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Identified FliY as a CheY-P phosphatase at the flagellar switch
"In particular we have identified the phosphatase as FliY"
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Demonstrated FliY increases CheY-P hydrolysis rate in vitro
"We showed that FliY increases the rate of CheY-P hydrolysis in vitro"
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FliY has N-terminal CheY-binding region homologous to FliM residues 6-15
"These residues are almost identical to the residues 6-15 in both B. subtilis FliM and FliY"
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Both FliM and FliY can bind CheY-P in vitro
"We were able to show that both of these proteins are capable of binding CheY-P in vitro"
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Deletion of CheY-binding region in fliY causes opposite phenotype to cheY mutant
"Deletion of this binding region in B. subtilis mutant fliM caused the same phenotype as a cheY mutant (clockwise flagellar rotation), whereas deletion of it in fliY caused the opposite"
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FliY C-terminus is homologous to E. coli FliN
"FliY, which resembles E. coli switch protein FliN only in its C-terminal part"
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FliY performs the role of E. coli CheZ but is localized at the motor, not receptors
"This task is performed in Escherichia coli by CheZ, which interestingly enough is primarily located at the receptors, not at the switch"