Identification of Ste4 as a potential regulator of Byr2 in the sexual response pathway of Schizosaccharomyces pombe

Barr, M. M., Tu, H., Van Aelst, L., Wigler, M. H. (October 1996) Identification of Ste4 as a potential regulator of Byr2 in the sexual response pathway of Schizosaccharomyces pombe. Mol Cell Biol, 16 (10). pp. 5597-603. ISSN 0270-7306 (Print)

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URL: https://www.ncbi.nlm.nih.gov/pubmed/8816472
DOI: 10.1128/MCB.16.10.5597

Abstract

A conserved MAP kinase cascade is central to signal transduction in both simple and complex eukaryotes. In the yeast Schizosaccharomyces pombe, Byr2, a homolog of mammalian MAPK/ERK kinase kinase and Saccharomyces cerevisiae STE11, is required for pheromone-induced sexual differentiation. A screen for S. pombe proteins that interact with Byr2 in a two-hybrid system led to the isolation of Ste4, a protein that is known to be required for sexual function. Ste4 binds to the regulatory region of Byr2. This binding site is separable from the binding site for Ras1. Both Ste4 and Ras1 act upstream of Byr2 and act at least partially independently. Ste4 contains a leucine zipper and is capable of homotypic interaction. Ste4 has regions of homology with STE50, an S. cerevisiae protein required for sexual differentiation that we show can bind to STE11.

Item Type: Paper
Uncontrolled Keywords: Binding Sites Ca(2+) Calmodulin Dependent Protein Kinase metabolism Crosses, Genetic DNA Primers Fungal Proteins metabolism GTP Binding Protein beta Subunits GTP Binding Proteins metabolism Genotype Heterotrimeric GTP-Binding Proteins Leucine Zippers MAP Kinase Kinase Kinases Mitogen Activated Protein Kinase Kinases Mutagenesis Site-Directed Pheromones physiology Polymerase Chain Reaction Protein Kinases metabolism Recombinant Fusion Proteins metabolism Recombination, Genetic Saccharomyces cerevisiae Proteins Schizosaccharomyces physiology Schizosaccharomyces pombe Proteins Signal Transduction Spores Fungal Transcription Factors metabolism ras Proteins metabolism
Subjects: organism description > yeast > Saccharomyces
bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein types > DNA binding protein
bioinformatics > genomics and proteomics > genetics & nucleic acid processing > DNA, RNA structure, function, modification > genes, structure and function > gene expression
bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein characterization
CSHL Authors:
Communities: CSHL labs > Van Aelst lab
CSHL labs > Wigler lab
Depositing User: CSHL Librarian
Date: October 1996
Date Deposited: 19 Apr 2012 16:41
Last Modified: 04 Nov 2016 20:17
PMCID: PMC231559
Related URLs:
URI: http://repository.cshl.edu/id/eprint/26155

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