title: Modulation of erm methyltransferase activity by peptides derived from phage display.
abstract: Combinatorial peptide display on phage M13 protein pIII was used to discover peptide sequences that selectively bind to ErmC' methyltransferase from Bacillus subtilis. One peptide, Ac-LSGVIAT-NH(2), inhibited methylation in vitro with a 50% inhibitory concentration of 20 microM. Interestingly, the set of six peptides which inhibited ErmC' stimulated ErmSF, a homologous methyltransferase from Streptomyces fradiae. Thus, Ac-LSGVIAT-NH(2) may not act directly at the catalytic center of ErmC', but may modulate its activity by binding at a structurally unrelated, but functionally linked, site.
authors.affiliation: Pharmacology Department, University of Wisconsin Medical School, Madison, Wisconsin 53706, USA.
authors.forename: R B
authors.initials: RB
authors.lastname: Giannattasio
authors.forename: B
authors.initials: B
authors.lastname: Weisblum
mesh_terms: D001412:Bacillus subtilis / Q000187:drug effects / Q000201:enzymology*; D002384:Catalysis; D004305:Dose-Response Relationship, Drug; D004791:Enzyme Inhibitors / Q000032:analysis / Q000494:pharmacology*; D008745:Methylation; D008780:Methyltransferases / Q000037:antagonists & inhibitors / Q000378:metabolism*; D019151:Peptide Library; D010455:Peptides / Q000032:analysis / Q000494:pharmacology*
chemical_list: D004791:Enzyme Inhibitors; D019151:Peptide Library; D010455:Peptides; D008780:Methyltransferases; C035181:rRNA (adenosine-O-2'-)methyltransferase