title: A nucleolar protein that affects mating efficiency in Saccharomyces cerevisiae by altering the morphological response to pheromone.
abstract: SSF1 and SSF2 are redundant essential yeast genes that, when overexpressed, increase the mating efficiency of cells containing a defective Ste4p Gbeta subunit. To identify the precise function of these genes in mating, different responses to pheromone were assayed in cells that either lacked or overexpressed SSF gene products. Cells containing null alleles of both SSF1 and SSF2 displayed the normal transcriptional induction response to pheromone but were unable to form mating projections. Overexpression of SSF1 conferred the ability to form mating projections on cells containing a temperature-sensitive STE4 allele, but had only a small effect on transcriptional induction. SSF1 overexpression preferentially increased the mating efficiency of a strain containing a null allele of SPA2, a gene that functions specifically in cell morphology. To investigate whether Ssf1p plays a direct physical role in mating projection formation, its subcellular location was determined. An Ssf1p-GFP fusion was found to localize to the nucleolus, implying that the role of SSF gene products in projection formation is indirect. The region of Ssf1p-GFP localization in cells undergoing projection formation was larger and more diffuse, and was often present in a specific orientation with respect to the projection. Although the function of Ssf1p appears to originate in the nucleus, it is likely that it ultimately acts on one or more of the proteins that is directly involved in the morphological response to pheromone. Because many of the proteins required for projection formation during mating are also required for bud formation during vegetative growth, regulation of the activity or amount of one or more of these proteins by Ssf1p could explain its role in both mating and dividing cells.
authors.affiliation: Department of Cell Biology and Anatomy, Mount Sinai School of Medicine, New York, New York 10029, USA.
authors.forename: J
authors.initials: J
authors.lastname: Kim
authors.forename: J P
authors.initials: JP
authors.lastname: Hirsch
mesh_terms: D002466:Cell Nucleolus / Q000235:genetics* / Q000378:metabolism; D003598:Cytoskeletal Proteins; D005656:Fungal Proteins / Q000187:drug effects / Q000235:genetics* / Q000378:metabolism / Q000502:physiology; D044387:GTP-Binding Protein beta Subunits; D019204:GTP-Binding Proteins / Q000235:genetics / Q000378:metabolism; D017353:Gene Deletion; D020962:Heterotrimeric GTP-Binding Proteins; D008565:Membrane Proteins; D009687:Nuclear Proteins / Q000235:genetics* / Q000378:metabolism / Q000502:physiology; D020718:Ribonucleoproteins, Small Nucleolar; D012441:Saccharomyces cerevisiae / Q000235:genetics* / Q000254:growth & development*; D029701:Saccharomyces cerevisiae Proteins
chemical_list: D003598:Cytoskeletal Proteins; C490024:FUS1 protein, S cerevisiae; D005656:Fungal Proteins; D044387:GTP-Binding Protein beta Subunits; D008565:Membrane Proteins; C064793:NOP1 protein, S cerevisiae; D009687:Nuclear Proteins; D020718:Ribonucleoproteins, Small Nucleolar; C065889:SPA2 protein, S cerevisiae; C114037:SSF1 protein, S cerevisiae; C491918:SSF2 protein, S cerevisiae; D029701:Saccharomyces cerevisiae Proteins; C067576:Ste4 protein, S cerevisiae; D019204:GTP-Binding Proteins; D020962:Heterotrimeric GTP-Binding Proteins