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Role of extracellular charged amino acids in the yeast alpha-factor receptor.
- Source :
-
Biochimica et biophysica acta [Biochim Biophys Acta] 2007 Jun; Vol. 1773 (6), pp. 707-17. Date of Electronic Publication: 2007 Feb 17. - Publication Year :
- 2007
-
Abstract
- The yeast pheromone receptor, Ste2p, is a G protein coupled receptor that initiates cellular responses to alpha-mating pheromone, a 13 residue peptide that carries a net positive charge at physiological pH. We have examined the role of extracellular charged groups on the receptor in response to the pheromone. Substitutions of Asn or Ala for one extracellular residue, Asp275, affected both pheromone binding and signaling, suggesting that this position interacts directly with ligand. The other seven extracellular acidic residues could be individually replaced by polar residues with no detectable effects on receptor function. However, substitution of Ala for each of these seven residues resulted in impairment of signaling without affecting pheromone binding, implying that the polar nature of these residues promotes receptor activation. In contrast, substitution of Ala for each of the six positively charged residues at the extracellular surface of Ste2p did not affect signaling.
- Subjects :
- Amino Acid Substitution
Amino Acids, Basic genetics
Aspartic Acid genetics
Mating Factor
Mutation, Missense
Peptides genetics
Peptides metabolism
Protein Binding physiology
Receptors, G-Protein-Coupled genetics
Receptors, Mating Factor genetics
Saccharomyces cerevisiae genetics
Saccharomyces cerevisiae Proteins genetics
Amino Acids, Basic metabolism
Aspartic Acid metabolism
Receptors, G-Protein-Coupled metabolism
Receptors, Mating Factor metabolism
Saccharomyces cerevisiae metabolism
Saccharomyces cerevisiae Proteins metabolism
Signal Transduction physiology
Subjects
Details
- Language :
- English
- ISSN :
- 0006-3002
- Volume :
- 1773
- Issue :
- 6
- Database :
- MEDLINE
- Journal :
- Biochimica et biophysica acta
- Publication Type :
- Academic Journal
- Accession number :
- 17433461
- Full Text :
- https://doi.org/10.1016/j.bbamcr.2007.02.002