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Role of extracellular charged amino acids in the yeast alpha-factor receptor.

Authors :
Bajaj A
Connelly SM
Gehret AU
Naider F
Dumont ME
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.

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