Towards determination of the structure of the Saccharomyces cerevisiae a-factor: an acylated pentadecapeptide blocks a-factor activity.
Open Access
- 1 November 1987
- journal article
- research article
- Published by Taylor & Francis in Molecular and Cellular Biology
- Vol. 7 (11) , 4122-4124
- https://doi.org/10.1128/mcb.7.11.4122
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.This publication has 14 references indexed in Scilit:
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