Abstract
We examined how the activity of O-acetylserine and O-acetylhomoserine sulphydrylase (OAS/OAH) SHLase of Saccharomyces cerevisiae is affected by sulphur source added to the growth medium and genetic background of the strain. In a wild-type strain, the activity was repressed if methionine, cysteine or glutathione was added to the growth medium. However, in a strain deficient of cystathionine γ-lyase, cysteine and glutathione were repressive, but methionine was not. In strains deficient of serine O-acetyltransferase (SATase), OAS/OAH SHLase activity was low regardless of sulphur source and was further lowered by cysteine and glutathione, but not by methionine. From these observations, we concluded that S-adenosylmethionine should be excluded from being the effector for regulation of OAS/OAH SHLase. Instead, we suspected that S. cerevisiae would have the same regulatory system as Escherichia coli for sulphate assimilation; i.e. cysteine inhibits SATase to lower the cellular concentration of OAS which is required for induction of the sulphate assimilation enzymes including OAS/OAH SHLase. Subsequently, we obtained data supporting this speculation.
Original language | English |
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Pages (from-to) | 1153-1162 |
Number of pages | 10 |
Journal | Yeast |
Volume | 12 |
Issue number | 11 |
DOIs | |
Publication status | Published - Sept 15 1996 |
Externally published | Yes |
Keywords
- Cysteine regulon
- O-acetylserine
- Saccharomyces cerevisiae
- Serine O-acetyltransferase
- Sulphate assimilation
ASJC Scopus subject areas
- Biotechnology
- Bioengineering
- Biochemistry
- Applied Microbiology and Biotechnology
- Genetics