| Title: | "Biological activity of the Asn-5,Arg-7 tridecapeptide encoded by MF alpha 2 of Saccharomyces cerevisiae" |
| Author(s): | Raths S; Shenbagamurthi P; Naider F; Becker JM; |
| DOI: | 10.1128/jb.168.3.1468-1471.1986 |
| ISSN/ISBN: | 0021-9193 (Print) 1098-5530 (Electronic) 0021-9193 (Linking) |
| Abstract: | "The precursor predicted by the nucleotide sequence of the MF alpha 2 gene of Saccharomyces cerevisiae contains one copy of the tridecapeptide alpha-factor previously characterized (H2N-Trp-His-Trp-Leu-Gln-Leu-Lys-Pro-Gly-Gln-Pro-Met-Tyr-COOH) and one copy of a peptide that contains two conservative amino acid substitutions (H2N-Trp-His-Trp-Leu-Asn-Leu-Arg-Pro-Gly-Gln-Pro-Met-Tyr-COOH). To determine whether the novel molecule possesses biological activity, the Asn-5,Arg-7 tridecapeptide was prepared chemically by solid-phase peptide synthesis. Growth arrest and morphogenesis assays gave identical activity profiles for the Asn-5,Arg-7 peptide and the other gene product, the Gln-5,Lys-7 peptide. The activities of the two peptides were additive and indistinguishable for S. cerevisiae X2180-1A. When present in fourfold molar excess, the biologically inactive desTrp-1,Ala-3 dodecapeptide reversed activity of the Asn-5,Arg-7 and Gln-5,Lys-7 tridecapeptides. Furthermore, neither peptide caused growth arrest of a MATa ste2(Ts) mutant when assayed at the restrictive temperature. These studies suggest that both pheromones interact with the alpha-factor receptor in a similar manner" |
| Keywords: | "Amino Acid Sequence Base Sequence Cell Cycle Genes *Genes, Fungal Mating Factor Peptides/chemical synthesis/genetics/*physiology Saccharomyces cerevisiae/genetics/*physiology;" |
| Notes: | "MedlineRaths, S Shenbagamurthi, P Naider, F Becker, J M eng GM 22086/GM/NIGMS NIH HHS/ GM 22087/GM/NIGMS NIH HHS/ T32-AI-07123/AI/NIAID NIH HHS/ Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S. 1986/12/01 J Bacteriol. 1986 Dec; 168(3):1468-71. doi: 10.1128/jb.168.3.1468-1471.1986" |
