Anti-HIV siamycin i directly inhibits autophosphorylation activity of the bacterial FsrC quorum sensor and other ATP-dependent enzyme activities

Pikyee Ma, Kenzo Nishiguchi, Hayley M. Yuille, Lianne M. Davis, Jiro Nakayama, Mary K. Phillips-Jones

Research output: Contribution to journalArticlepeer-review

25 Citations (Scopus)

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.

Original languageEnglish
Pages (from-to)2660-2664
Number of pages5
JournalFEBS Letters
Volume585
Issue number17
DOIs
Publication statusPublished - Sep 2 2011

All Science Journal Classification (ASJC) codes

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology

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