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Antimicrobial Agents and Chemotherapy, July 2000, p. 1961-1963, Vol. 44, No. 7
0066-4804/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.

Modulation of Erm Methyltransferase Activity by Peptides Derived from Phage Display

Robert B. Giannattasio and Bernard Weisblum*

Pharmacology Department, University of Wisconsin Medical School, Madison, Wisconsin 53706

Received 24 November 1999/Returned for modification 2 February 2000/Accepted 26 April 2000

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-NH2, inhibited methylation in vitro with a 50% inhibitory concentration of 20 µM. Interestingly, the set of six peptides which inhibited ErmC' stimulated ErmSF, a homologous methyltransferase from Streptomyces fradiae. Thus, Ac-LSGVIAT-NH2 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.

* Corresponding author. Mailing address: Pharmacology Department, University of Wisconsin Medical School, 1300 University Ave., Madison, WI 53706. Phone: (608) 262-0972. Fax: (608) 262-1257. E-mail: weisblum{at}facstaff.wisc.edu.

Antimicrobial Agents and Chemotherapy, July 2000, p. 1961-1963, Vol. 44, No. 7
0066-4804/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.


This article has been cited by other articles:

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  • Farrow, K. A., Lyras, D., Polekhina, G., Koutsis, K., Parker, M. W., Rood, J. I. (2002). Identification of Essential Residues in the Erm(B) rRNA Methyltransferase of Clostridium perfringens. Antimicrob. Agents Chemother. 46: 1253-1261 [Abstract] [Full Text]  


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