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Isolation and characterization of Schizosaccharomyces pombe mutants lacking aminopeptidase activity

Author:
Arbesú, María José; Gascón Muñoz, SantiagoUniovi authority; Suárez Rendueles, María PazUniovi authority
Publication date:
1991
Editorial:

Wiley

Publisher version:
http://dx.doi.org/10.1002/yea.320070512
Citación:
Yeast, 7(5), p. 525–531 (1991); doi:10.1002/yea.320070512
Descripción física:
p. 525-531
Abstract:

A mutant strain of the fission yeast Schizosaccharomyces pombe defective in aminopeptidase I was isolated by screening for lack of activity against the chromogenic substrate lysine-β-naphthlamide in isolated colonies. Tetrad dissection of sporulated diploids heterozygous for the wild-type and mutant allele resulted in a 2:2 segregation of mutant and wild-type phenotype indicating a single chromosomal gene mutation. Gene dosage experiments indicated that the mutation might reside in the structural gene of aminopeptidase I. No vital consequences of aminopeptidase I deficiency on cell life and sporulation could be detected. However, the enzyme seems to be involved in protein degradation under conditions of nutrient deprivation

A mutant strain of the fission yeast Schizosaccharomyces pombe defective in aminopeptidase I was isolated by screening for lack of activity against the chromogenic substrate lysine-β-naphthlamide in isolated colonies. Tetrad dissection of sporulated diploids heterozygous for the wild-type and mutant allele resulted in a 2:2 segregation of mutant and wild-type phenotype indicating a single chromosomal gene mutation. Gene dosage experiments indicated that the mutation might reside in the structural gene of aminopeptidase I. No vital consequences of aminopeptidase I deficiency on cell life and sporulation could be detected. However, the enzyme seems to be involved in protein degradation under conditions of nutrient deprivation

URI:
http://hdl.handle.net/10651/28924
ISSN:
0749-503X; 1097-0061
DOI:
10.1002/yea.320070512
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