| Literature DB >> 8896281 |
B Ono1, K Kijima, N Ishii, T Kawato, A Matsuda, A Paszewski, S Shinoda.
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 gamma-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.Entities:
Mesh:
Substances:
Year: 1996 PMID: 8896281 DOI: 10.1002/(SICI)1097-0061(19960915)12:11%3C1153::AID-YEA16%3E3.0.CO;2-2
Source DB: PubMed Journal: Yeast ISSN: 0749-503X Impact factor: 3.239