Open AccessAnalysis of Proteinase A Function in Yeast
Author(s) -
MECHLER Bernd,
WOLF Dieter H.
Publication year - 1981
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1981.tb06427.x
Subject(s) - mutant , biology , proteinase k , yeast , mutation , biochemistry , gene , catabolite repression , saccharomyces cerevisiae , microbiology and biotechnology , enzyme , genetics
Yeast mutants lacking proteinase A were isolated. One of these mutants (Hb I) is characterized in detail. The mutation called pral segregates 2:2 in meiotic tetrads indicating a single gene mutation. No anti‐(proteinase A) cross‐reacting material can be detected. Diploids heterozygous for pral show gene dosage. Thus, it appears that PRAI might be the structural gene for proteinase A. Results obtained with this mutant show that proteinase A is not a vital component of the vegetative cell cycle. The mutant exhibits normal mitotic growth under rich and poor growth conditions and shows normal mating. Enzymes subject to carbon catabolite inactivation and inactivation of NADP‐dependent glutamate dehydrogenase, processes which were proposed to be of proteolytic nature, are not affected by the absence of proteinase A. However, protein degradation under sporulation conditions is about 30;(reduced in proteinasc A mutant cells. The differentiation process of spordation is also disturbed leading to a 40 reduced sporulation frequency in mutant cells.