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Mol Cell Biol. 1987 November; 7(11): 4122-4124

Towards determination of the structure of the Saccharomyces cerevisiae a-factor: an acylated pentadecapeptide blocks a-factor activity.

J M Becker, S Marcus, B Kundu, P Shenbagamurthi and F Naider

Department of Microbiology, University of Tennessee, Knoxville 37996.

ABSTRACT

Putative a-factor peptides YIIKGVFWADP, YIIKGVFWANP, YIIKGLFWADP, YIIKGLFWANP, YIIKGVFWDPA, and YIIKGVFWDPACVIA and several peptide derivatives were synthesized and were found to be inactive in growth arrest assays, yet they blocked the activity of biological a-factor. Antagonism was greatest with YIIKGVFWDPAC(palmitoyl)VIA. Thus, the structure of a-factor may be a lipopeptide resembling this palmitoylated pentadecapeptide.

Mol Cell Biol. 1987 November; 7(11): 4122-4124






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