Abstract:
:Siamycin I disrupts growth and quorum sensing in Enterococcus faecalis. Using purified intact protein, we demonstrate here that quorum membrane sensor kinase FsrC is a direct target of siamycin I, reducing pheromone-stimulated autophosphorylation activity by up to 91%. Inhibition was non-competitive with ATP as substrate. Other ATP-binding enzymes were also inhibited, including nine other membrane sensor kinases of E. faecalis, Rhodobacter sphaeroides PrrB, porcine Na(+)-dependent ATPase and the catalytic subunit of bovine protein kinase A, but not bacterial β-galactosidase, confirming targeted inhibition of a wide range of ATP dependent reactions, and elucidating a likely mechanism underlying the lethality of the inhibitor.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Ma P,Nishiguchi K,Yuille HM,Davis LM,Nakayama J,Phillips-Jones MKdoi
10.1016/j.febslet.2011.07.026subject
Has Abstractpub_date
2011-09-02 00:00:00pages
2660-4issue
17eissn
0014-5793issn
1873-3468pii
S0014-5793(11)00555-2journal_volume
585pub_type
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