Anti-HIV siamycin I directly inhibits autophosphorylation activity of the bacterial FsrC quorum sensor and other ATP-dependent enzyme activities
| Autor: | Kenzo Nishiguchi, Hayley M. Yuille, Pikyee Ma, Lianne M. Davis, Jiro Nakayama, Mary K. Phillips-Jones |
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| Rok vydání: | 2011 |
| Předmět: |
Bacterial two-component signal transduction system
Swine Protein subunit ATPase Biophysics Microbial Sensitivity Tests Rhodobacter sphaeroides Biology Biochemistry Enzyme activator Bacterial Proteins Structural Biology HIV inhibitor Siamycin I Genetics Gelatinase biosynthesis-activating pheromone Enterococcus faecalis Animals Enzyme Inhibitors Phosphorylation Protein kinase A Molecular Biology Adenosine Triphosphatases Kinase Autophosphorylation Quorum Sensing Cell Biology beta-Galactosidase Enzyme Activation Quorum sensing Kinetics FsrC biology.protein Intercellular Signaling Peptides and Proteins Cattle Peptides |
| Zdroj: | FEBS letters. 585(17) |
| ISSN: | 1873-3468 |
| Popis: | 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 interactionsPrrB phosphorylates PrrB by protein kinase assay (View interaction)FsrC phosphorylates FsrC by protein kinase assay (View interaction) |
| Databáze: | OpenAIRE |
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