کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
2047942 | 1074046 | 2011 | 5 صفحه PDF | دانلود رایگان |
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.Structured summary of protein interactionsPrrBphosphorylatesPrrB by protein kinase assay(View interaction)FsrCphosphorylatesFsrC by protein kinase assay(View interaction)
► Quorum membrane sensor kinase FsrC is a direct target of siamycin I.
► Both GBAP-activated and non-activated FsrC activity is inhibited.
► Inhibition of FsrC by siamycin I is non-competitive with ATP substrate.
► Other membrane sensor kinases and ATP-binding enzymes from a range of sources are also inhibited, demonstrating targeted inhibition of ATP-dependent reactions.
► The likely mechanism underlying the lethality of the inhibitor has been elucidated.
Journal: FEBS Letters - Volume 585, Issue 17, 2 September 2011, Pages 2660–2664