Isolation and characterization of Schizosaccharomyces pombe mutants lacking aminopeptidase activity.
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-beta-naphthylamide 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.
Arbesu
M J
MJ
Dpto Biolgogía Funcional, Facultad de Medicina, Universidad de Oveido, Spain.
Gascon
S
S
Suarez-Rendueles
P
P
D000483:Alleles; D000626:Aminopeptidases / Q000235:genetics*; D002851:Chromatography, High Pressure Liquid; D004591:Electrophoresis, Polyacrylamide Gel; D005800:Genes, Fungal; D016296:Mutagenesis; D009154:Mutation; D029701:Saccharomyces cerevisiae Proteins; D012568:Schizosaccharomyces / Q000201:enzymology* / Q000235:genetics / Q000502:physiology; D013172:Spores, Fungal
D029701:Saccharomyces cerevisiae Proteins; D000626:Aminopeptidases; C019689:APE1 protein, S cerevisiae