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Comparative Study
. 1987 Nov;7(11):4122-4.
doi: 10.1128/mcb.7.11.4122-4124.1987.

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

J M Becker  1 , S Marcus, B Kundu, P Shenbagamurthi, F Naider
Affiliations
Comparative Study

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

J M Becker et al. Mol Cell Biol. 1987 Nov.

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.

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References

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    1. Cell. 1983 Sep;34(2):581-6 - PubMed
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