Biosynthesis of sulphur amino acids in Saccharomyces cerevisiae: regulatory roles of methionine and S-adenosylmethionine reassessed.
cys4-1, a mutation in the reverse trans-sulphuration pathway, relieves the sulphate assimilation pathway and homocysteine synthase from methionine-mediated repression. Since the mutation blocks the synthesis of cysteine from methionine downstream from homocysteine, this indicates that neither methionine nor S-adenosylmethionine serve as low-molecular-mass effectors in this regulatory system, contradicting earlier hypotheses.
Paszewski
A
A
Institute of Biochemistry and Biophysics, Polish Academy of Sciences, Warszawa.
Ono
B I
BI
D000603:Amino Acids, Sulfur / Q000096:biosynthesis*; D019757:Carbon-Oxygen Lyases; D003547:Cysteine Synthase; D004794:Enzyme Repression; D015966:Gene Expression Regulation, Fungal; D008190:Lyases / Q000378:metabolism; D008715:Methionine / Q000378:metabolism; D009097:Multienzyme Complexes; D012436:S-Adenosylmethionine / Q000378:metabolism; D012441:Saccharomyces cerevisiae / Q000235:genetics / Q000378:metabolism*; D029701:Saccharomyces cerevisiae Proteins
D000603:Amino Acids, Sulfur; D009097:Multienzyme Complexes; D029701:Saccharomyces cerevisiae Proteins; D012436:S-Adenosylmethionine; D008715:Methionine; D003547:Cysteine Synthase; C103381:MET17 protein, S cerevisiae; C018725:O-acetylhomoserine (thiol)-lyase; D008190:Lyases; D019757:Carbon-Oxygen Lyases