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Mol Cell Biol

Title:		Towards determination of the structure of the Saccharomyces cerevisiae a-factor: an acylated pentadecapeptide blocks a-factor activity
Author(s):		Becker JM; Marcus S; Kundu B; Shenbagamurthi P; Naider F;
Address:		"Department of Microbiology, University of Tennessee, Knoxville 37996"
Journal Title:		Mol Cell Biol
Year:		1987
Volume:		7
Issue:		11
Page Number:		4122 - 4124
DOI:		10.1128/mcb.7.11.4122-4124.1987
ISSN/ISBN:		0270-7306 (Print) 1098-5549 (Electronic) 0270-7306 (Linking)
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"
Keywords:		Acylation Amino Acid Sequence Mating Factor Oligopeptides/pharmacology *Peptides/antagonists & inhibitors/physiology Saccharomyces cerevisiae/drug effects/*physiology Structure-Activity Relationship;
Notes:		"MedlineBecker, J M Marcus, S Kundu, B Shenbagamurthi, P Naider, F eng GM 22086/GM/NIGMS NIH HHS/ GM 22087/GM/NIGMS NIH HHS/ Comparative Study Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S. 1987/11/01 Mol Cell Biol. 1987 Nov; 7(11):4122-4. doi: 10.1128/mcb.7.11.4122-4124.1987"