Proteinase B is, indeed, not required for chitin synthetase 1 function in Saccharomyces cerevisiae.
Previous genetic evidence led to the conclusion that proteinase B of yeast was not involved in the function of chitin synthetase 1 (Chs1), based on the demonstration of normal septum formation, cell division and chitin deposition in mutants devoid of the proteinase (Zubenko, G.S., Mitchell, A.P., and Jones, E.W. (1979) Proc. Natl. Acad. Sci. USA 76, 2395-2399). Later, however, it was found that the essential enzyme for septum formation is chitin synthetase 2, whereas Chs1 acts as an auxiliary enzyme, whose absence results in daughter cell lysis under acidic conditions (Cabib, E., Sburlati, A., Bowers, B. and Silverman, S.J. (1989) J. Cell Biol. 108, 1665-1672). By using the lytic behavior as a criterion, we have now found that prb1 strains are not defective in Chs1 function. Certain strains contain a recessive suppressor of lysis which could mask the Chs1 defect. However, appropriate crosses and transformation experiments showed that the prb1 mutants do not harbor the suppressor. It may now be concluded with confidence that proteinase B is not required for chitin synthetase 1 function.
Silverman
S J
SJ
Laboratory of Biochemistry and Metabolism National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892.
Shaw
J A
JA
Cabib
E
E
D001483:Base Sequence; D002687:Chitin Synthase / Q000235:genetics*; D005838:Genotype; D008969:Molecular Sequence Data; D009154:Mutation; D012441:Saccharomyces cerevisiae / Q000187:drug effects / Q000201:enzymology / Q000235:genetics*; D012697:Serine Endopeptidases / Q000494:pharmacology*; D014170:Transformation, Genetic; D014357:Trypsin; D029701:Saccharomyces cerevisiae Proteins
D002687:Chitin Synthase; D012697:Serine Endopeptidases; D014357:Trypsin; C023302:yeast proteinase B; D029701:Saccharomyces cerevisiae Proteins