| Title: | Antagonistic and synergistic peptide analogues of the tridecapeptide mating pheromone of Saccharomyces cerevisiae |
| Author(s): | Eriotou-Bargiota E; Xue CB; Naider F; Becker JM; |
| Address: | "Department of Microbiology, University of Tennessee, Knoxville 37996-0845" |
| ISSN/ISBN: | 0006-2960 (Print) 0006-2960 (Linking) |
| Abstract: | "Biologically inactive, truncated analogues of the Saccharomyces cerevisiae alpha-mating factor (WHWLQLKPGQPMY) either antagonized or synergized the activity of the native pheromone. An amino-terminal truncated pheromone [WLQLKPGQP(Nle)Y] had no activity by itself, but the analogue acted as an antagonist by competing with binding and activity of the mating factor. In contrast, a carboxyl-terminal truncated pheromone [WHWLQLKPGQP] was not active by itself nor did the peptide compete with alpha-factor for binding to the alpha-factor receptor, but it acted as a synergist by causing a marked increase in the activity of alpha-factor. The observation that residues near the amino terminus may be involved in signal transduction whereas those near the carboxyl terminus influence binding allows us to separate binding and signal transduction in the yeast pheromone response pathway. If found for other hormone-receptor systems, synergists may have potential as therapeutic compounds" |
| Keywords: | "Amino Acid Sequence Drug Synergism Mating Factor Molecular Sequence Data Peptides/*pharmacology Pheromones/*antagonists & inhibitors/isolation & purification Protein Binding/drug effects Receptors, Cell Surface/drug effects/metabolism Receptors, Mating Fa;" |
| Notes: | "MedlineEriotou-Bargiota, E Xue, C B Naider, F Becker, J M eng GM-22086/GM/NIGMS NIH HHS/ GM-22087/GM/NIGMS NIH HHS/ Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, Non-P.H.S. Research Support, U.S. Gov't, P.H.S. 1992/01/21 Biochemistry. 1992 Jan 21; 31(2):551-7. doi: 10.1021/bi00117a036" |
