Towards determination of the structure of the Saccharomyces cerevisiae a-factor: an acylated pentadecapeptide blocks a-factor activity.
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.
Becker
J M
JM
Department of Microbiology, University of Tennessee, Knoxville 37996.
Marcus
S
S
Kundu
B
B
Shenbagamurthi
P
P
Naider
F
F
D000215:Acylation; D000595:Amino Acid Sequence; D000072235:Mating Factor; D009842:Oligopeptides / Q000494:pharmacology; D010455:Peptides / Q000037:antagonists & inhibitors / Q000502:physiology; D012441:Saccharomyces cerevisiae / Q000187:drug effects / Q000502:physiology*; D013329:Structure-Activity Relationship
D009842:Oligopeptides; D010455:Peptides; D000072235:Mating Factor