BAR1/YIL015W Summary Help

BAR1 BASIC INFORMATION

Standard Name BAR1 1
Systematic Name YIL015W
Alias SST1 1 , 2
Feature Type ORF, Verified
Description Aspartyl protease secreted into the periplasmic space of mating type a cells, helps cells find mating partners, cleaves and inactivates alpha factor allowing cells to recover from alpha-factor-induced cell cycle arrest (2, 3, 4 and see Summary Paragraph)
Name Description BARrier to the alpha factor response 1, 5
GO Annotations All BAR1 GO evidence and references
    View Computational GO annotations for BAR1
Molecular Function
Manually curated
Biological Process
Manually curated
Cellular Component
Manually curated
Mutant Phenotype All BAR1 Phenotype details and references
Classical genetics
null
Large-scale survey
null
Interactions BAR1 All interactions details and references
3 total interaction(s) for 3 unique genes/features.
Physical Interactions
  • Affinity Capture-MS: 1

Genetic Interactions
  • Dosage Rescue: 1
  • Synthetic Rescue: 1

Sequence Information
ChrIX:322340 to 324103 | ORF Map | GBrowse
Gbrowse
Genetic position: -12 cM
Last Update Coordinates: 1994-12-10 | Sequence: 1994-12-10
Subfeature details
Relative
Coordinates
Chromosomal
Coordinates
Most Recent Updates
Coordinates Sequence
CDS 1..1764 322340..324103 1994-12-10 1994-12-10
External Links All Associated Seq | E.C. | Entrez Gene | Entrez RefSeq Protein | MIPS | UniProtKB
Primary SGDIDS000001277

BAR1 RESOURCES

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SGD ORF map
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  • Functional Analysis

Click on histogram for expression summary
Expression Summary histogram

SUMMARY PARAGRAPH for BAR1

Bar1p is a protease secreted into the periplasmic space of Mata cells that cleaves and inactivates alpha factor (2, 6). Mata cells that lack Bar1p are supersensitive to alpha factor-induced G1 arrest (2, 7). Transcription of BAR1 in alpha haploids and a/alpha diploids is repressed by the alpha2 protein and cofactors, and BAR1 transcription in Mata cells is stimulated by the presence of alpha factor (8, 9, 10). Bar1p is an aspartyl protease with similarity to pepsin, Pep4p, and Yap3p (11, 12, 6).

Last updated: 1999-12-31

REFERENCES CITED ON THIS PAGE [View Complete Literature Guide for BAR1]

1) Sprague GF Jr and Herskowitz I  (1981) Control of yeast cell type by the mating type locus. I. Identification and control of expression of the a-specific gene BAR1. J Mol Biol 153(2):305-21
2) Chan RK and Otte CA  (1982) Physiological characterization of Saccharomyces cerevisiae mutants supersensitive to G1 arrest by a factor and alpha factor pheromones. Mol Cell Biol 2(1):21-9
3) Ciejek E and Thorner J  (1979) Recovery of S. cerevisiae a cells from G1 arrest by alpha factor pheromone requires endopeptidase action. Cell 18(3):623-35
4) Barkai N, et al.  (1998) Protease helps yeast find mating partners. Nature 396(6710):422-3
5) Hicks JB and Herskowitz I  (1976) Evidence for a new diffusible element of mating pheromones in yeast. Nature 260(5548):246-8
6) Ballensiefen W and Schmitt HD  (1997) Periplasmic Bar1 protease of Saccharomyces cerevisiae is active before reaching its extracellular destination. Eur J Biochem 247(1):142-7
7) Chan RK and Otte CA  (1982) Isolation and genetic analysis of Saccharomyces cerevisiae mutants supersensitive to G1 arrest by a factor and alpha factor pheromones. Mol Cell Biol 2(1):11-20
8) Kronstad JW, et al.  (1987) A yeast operator overlaps an upstream activation site. Cell 50(3):369-77
9) Manney TR  (1983) Expression of the BAR1 gene in Saccharomyces cerevisiae: induction by the alpha mating pheromone of an activity associated with a secreted protein. J Bacteriol 155(1):291-301
10) Hagen DC, et al.  (1991) Pheromone response elements are necessary and sufficient for basal and pheromone-induced transcription of the FUS1 gene of Saccharomyces cerevisiae. Mol Cell Biol 11(6):2952-61
11) MacKay VL, et al.  (1988) The Saccharomyces cerevisiae BAR1 gene encodes an exported protein with homology to pepsin. Proc Natl Acad Sci U S A 85(1):55-9
12) Egel-Mitani M, et al.  (1990) A novel aspartyl protease allowing KEX2-independent MF alpha propheromone processing in yeast. Yeast 6(2):127-37