The yeast α-factor receptor: structural properties deduced from the sequence of theSTE2gene
- 1 January 1985
- journal article
- Published by Oxford University Press (OUP) in Nucleic Acids Research
- Vol. 13 (23) , 8463-8475
- https://doi.org/10.1093/nar/13.23.8463
Abstract
The STE2 gene of the yeast Saccharomyces cerevisiae encodes a component of the receptor for the oligopeptide pheromone alpha-factor. We have cloned and determined the nucleotide sequence of the STE2 gene. A sequence involved in the control of cell-type expression of the STE2 gene was found 5' of an open reading frame that could encode a protein of 431 amino acids. The predicted STE2 protein contains seven hydrophobic segments, suggesting that the alpha-factor receptor is an integral membrane protein. No extensive homology at the primary sequence level was detected between the predicted STE2 protein and other available protein sequences.Keywords
This publication has 35 references indexed in Scilit:
- Human insulin receptor and its relationship to the tyrosine kinase family of oncogenesNature, 1985
- Sensory and energy transduction: Light-activated retinal proteinsNature, 1984
- The human LDL receptor: A cysteine-rich protein with multiple Alu sequences in its mRNACell, 1984
- Human epidermal growth factor receptor cDNA sequence and aberrant expression of the amplified gene in A431 epidermoid carcinoma cellsNature, 1984
- Isolation, sequence analysis, and intron-exon arrangement of the gene encoding bovine rhodopsinCell, 1983
- Rhodopsin and bacteriorhodopsin: structure—function relationshipsFEBS Letters, 1982
- A simple method for displaying the hydropathic character of a proteinJournal of Molecular Biology, 1982
- Nucleotide sequence comparisons and functional analysis of yeast centromere DNAsCell, 1982
- Construction and characterization of three yeast-Escherichia coli shuttle vectors designed for rapid subcloning of yeast genes on small DNA fragmentsGene, 1981
- Mutants of Saccharomyces cerevisiae unresponsive to cell division control by polypeptide mating hormone.The Journal of cell biology, 1980