scholarly journals Phenotypic analysis of proteinase A mutants. Implications for autoactivation and the maturation pathway of the vacuolar hydrolases of Saccharomyces cerevisiae.

1993 ◽  
Vol 268 (12) ◽  
pp. 8990-8998
Author(s):  
C.A. Woolford ◽  
J.A. Noble ◽  
J.D. Garman ◽  
M.F. Tam ◽  
M.A. Innis ◽  
...  
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Phenotypic Analysis ◽  
Proteinase A

PEP4 gene of Saccharomyces cerevisiae encodes proteinase A, a vacuolar enzyme required for processing of vacuolar precursors

1986 ◽  
Vol 6 (7) ◽  
pp. 2490-2499
Author(s):  
G Ammerer ◽  
C P Hunter ◽  
J H Rothman ◽  
G C Saari ◽  
L A Valls ◽  
...  
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Amino Acid ◽  
Structural Gene ◽  
Yeast Cells ◽  
Linkage Data ◽  
Predicted Amino Acid Sequence ◽  
Multicopy Plasmid ◽  
Proteinase A ◽  
Pep4 Gene ◽  
Cloned Gene

The proteinase A structural gene of Saccharomyces cerevisiae was cloned by using an immunological screening procedure that allows detection of yeast cells which are aberrantly secreting vacuolar proteins (J. H. Rothman, C. P. Hunter, L. A. Valls, and T. H. Stevens, Proc. Natl. Acad. Sci. USA, 83:3248-3252, 1986). A second cloned gene was obtained on a multicopy plasmid by complementation of a pep4-3 mutation. The nucleotide sequences of these two genes were determined independently and were found to be identical. The predicted amino acid sequence of the cloned gene suggests that proteinase A is synthesized as a 405-amino-acid precursor which is proteolytically converted to the 329-amino-acid mature enzyme. Proteinase A shows substantial homology to mammalian aspartyl proteases, such as pepsin, renin, and cathepsin D. The similarities may reflect not only analogous functions but also similar processing and intracellular targeting mechanisms for the two proteins. The cloned proteinase A structural gene, even when it is carried on a single-copy plasmid, complements the deficiency in several vacuolar hydrolase activities that is observed in a pep4 mutant. A strain carrying a deletion in the genomic copy of the gene fails to complement a pep4 mutant of the opposite mating type. Genetic linkage data demonstrate that integrated copies of the cloned proteinase A structural gene map to the PEP4 locus. Thus, the PEP4 gene encodes a vacuolar aspartyl protease, proteinase A, that is required for the in vivo processing of a number of vacuolar zymogens.

scholarly journals The selectivity of action of the aspartic-proteinase inhibitor IA3 from yeast (Saccharomyces cerevisiae)

1985 ◽  
Vol 231 (3) ◽  
pp. 777-779 ◽  
Author(s):  
T Dreyer ◽  
M J Valler ◽  
J Kay ◽  
P Charlton ◽  
B M Dunn
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Proteinase Inhibitor ◽  
Aspartic Proteinase ◽  
Significant Extent ◽  
Aspartic Proteinases ◽  
Yeast Saccharomyces Cerevisiae ◽  
Naturally Occurring ◽  
Proteinase A

The ability of the aspartic-proteinase inhibitor IA3 from yeast (Saccharomyces cerevisiae) to affect the activities of a range of mammalian and microbial aspartic proteinases was examined. The inhibitor appeared to be completely selective in that only the aspartic proteinase A from yeast was inhibited to any significant extent. IA3 thus represents the first example of a totally specific, naturally occurring, aspartic-proteinase inhibitor.

Vacuolar and extracellular maturation of Saccharomyces cerevisiae proteinase A

Yeast ◽  
1996 ◽  
Vol 12 (9) ◽  
pp. 823-832 ◽  
Author(s):  
Anne Mette Wolff ◽  
Nanni Din ◽  
Jens G. Litske Petersen
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Proteinase A

Comprehensive phenotypic analysis of single-gene deletion and overexpression strains of Saccharomyces cerevisiae

Yeast ◽  
2011 ◽  
Vol 28 (5) ◽  
pp. 349-361 ◽  
Author(s):  
Katsunori Yoshikawa ◽  
Tadamasa Tanaka ◽  
Yoshihiro Ida ◽  
Chikara Furusawa ◽  
Takashi Hirasawa ◽  
...  
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Gene Deletion ◽  
Single Gene ◽  
Phenotypic Analysis ◽  
Single Gene Deletion

scholarly journals Transcriptomic and phenotypic analysis of the effects of T-2 toxin on Saccharomyces cerevisiae: evidence of mitochondrial involvement

2010 ◽  
Vol 11 (1) ◽  
pp. 133-150 ◽  
Author(s):  
Lyne Jossé ◽  
Xingmin Li ◽  
Raymond D. Coker ◽  
Campbell W. Gourlay ◽  
Ivor H. Evans
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Phenotypic Analysis

Characterization of proteinase A excretion from Saccharomyces cerevisiae in high sugar stress conditions

2015 ◽  
Vol 58 (2) ◽  
pp. 203-208 ◽  
Author(s):  
Liang Dong ◽  
Feng Li ◽  
Yongzhe Piao ◽  
Dong Sun ◽  
Rui Zhao ◽  
...  
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Stress Conditions ◽  
High Sugar ◽  
Proteinase A

scholarly journals Dissection of Filamentous Growth by Transposon Mutagenesis in Saccharomyces cerevisiae

Genetics ◽  
1997 ◽  
Vol 145 (3) ◽  
pp. 671-684 ◽  
Author(s):  
Hans-Ulrich Mösch ◽  
Gerald R Fink
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Signaling Pathway ◽  
Filamentous Growth ◽  
Invasive Growth ◽  
Cell Morphogenesis ◽  
Phenotypic Analysis ◽  
Cellular Processes ◽  
Evolutionarily Conserved ◽  
Mutant Strains ◽  
Bud Site

Diploid Saccharomyces cerevisiae strains starved for nitrogen undergo a developmental transition from growth as single yeast form (YF) cells to a multicellular form consisting of filaments of pseudohyphal (PH) cells. Filamentous growth is regulated by an evolutionarily conserved signaling pathway that includes the small GTP-binding proteins Ras2p and Cdc42p, the protein kinases Ste20p, Ste11p and Ste7p, and the transcription factor Ste12p. Here, we designed a genetic screen for mutant strains defective for filamentous growth (dfg) to identify novel targets of the filamentation signaling pathway, and we thereby identified 16 different genes, CDC39, STE12, TEC1, WH13, NAB1, DBR1, CDC55, SRV2, TPM1, SPA2, BNI1, DFG5, DFG9, DFG10, BUD8 and DFG16, mutations that block filamentous growth. Phenotypic analysis of dfg mutant strains genetically dissects filamentous growth into the cellular processes of signal transduction, bud site selection, cell morphogenesis and invasive growth. Epistasis tests between dfg mutant alleles and dominant activated alleles of the RAS2 and STE11 genes, RAS2Val19 and STE11-4, respectively, identify putative targets for the filamentation signaling pathway. Several of the genes described here have homologues in filamentous fungi, where they also regulate fungal development.

Effect of RP51 gene dosage alterations on ribosome synthesis in Saccharomyces cerevisiae

1985 ◽  
Vol 5 (12) ◽  
pp. 3429-3435
Author(s):  
N Abovich ◽  
L Gritz ◽  
L Tung ◽  
M Rosbash
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Growth Rate ◽  
Ribosomal Protein ◽  
Dosage Compensation ◽  
Ribosomal Proteins ◽  
Gene Dosage ◽  
Translational Efficiency ◽  
Phenotypic Analysis ◽  
Ribosomal Subunits ◽  
Single Deletion

The Saccharomyces cerevisiae ribosomal protein rp51 is encoded by two interchangeable genes, RP51A and RP51B. We altered the RP51 gene dose by creating deletions of the RP51A or RP51B genes or both. Deletions of both genes led to spore inviability, indicating that rp51 is an essential ribosomal protein. From single deletion studies in haploid cells, we concluded that there was no intergenic dosage compensation at the level of mRNA abundance or mRNA utilization (translational efficiency), although phenotypic analysis had previously indicated a small compensation effect on growth rate. Similarly, deletions in diploid strains indicated that no strong mechanisms exist for intragenic dosage compensation; in all cases, a decreased dose of RP51 genes was characterized by a slow growth phenotype. A decreased dose of RP51 genes also led to insufficient amounts of 40S ribosomal subunits, as evidenced by a dramatic accumulation of excess 60S ribosomal subunits. We conclude that inhibition of 40S synthesis had little or no effect on the synthesis of the 60S subunit components. Addition of extra copies of rp51 genes led to extra rp51 protein synthesis. The additional rp51 protein was rapidly degraded. We propose that rp51 and perhaps many ribosomal proteins are normally oversynthesized, but the unassembled excess is degraded, and that the apparent compensation seen in haploids, i.e., the fact that the growth rate of mutant strains is less depressed than the actual reduction in mRNA, is a consequence of this excess which is spared from proteolysis under this circumstance.

Mathematical Modeling of Proteinase A Overproduction by Saccharomyces cerevisiae

1996 ◽  
Vol 782 (1) ◽  
pp. 350-362 ◽  
Author(s):  
SUSANNE GRØN ◽  
KIRSTEN VAEVER JOCHUMSEN ◽  
KIRSTEN BIEDERMANN ◽  
CLAUS EMBORG
Keyword(s):  
Mathematical Modeling ◽  
Saccharomyces Cerevisiae ◽  
Proteinase A
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