scholarly journals Primary structure of the aspartic proteinase A from Saccharomyces cerevisiae

1986 ◽  
Vol 51 (1) ◽  
pp. 27-41 ◽  
Author(s):  
Thomas Dreyer ◽  
Barbara Halkier ◽  
Ib Svendsen ◽  
Martin Ottesen
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Primary Structure ◽  
Aspartic Proteinase ◽  
Proteinase A

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.

scholarly journals The primary structure of Aspergillus niger acid proteinase A.

1991 ◽  
Vol 266 (29) ◽  
pp. 19480-19483 ◽  
Author(s):  
K. Takahashi ◽  
H. Inoue ◽  
K. Sakai ◽  
T. Kohama ◽  
S. Kitahara ◽  
...  
Keyword(s):  
Aspergillus Niger ◽  
Primary Structure ◽  
Acid Proteinase ◽  
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.

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
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