Molecular and General Genetics MGG

, Volume 126, Issue 4, pp 367–374 | Cite as

Deficiency in methionine adenosyltransferase resulting in limited repressibility of methionine biosynthetic enzymes in Aspergillus nidulans

  • Norman J. Pieniążek
  • Iwona M. Kowalska
  • Piotr P. Stępień


In Aspergillus nidulans methionine can be metabolized to cysteine. Mutants blocked in this pathway were selected and divided into three groups representing three separate loci: mecA, mecB and mecC. mecC13 mutant possesses a low level of methionine adenosyltransferase and shows a limited extent of methionine-caused repression of three enzymes of the methionine biosynthetic pathway: sulfate permease, sulfite reductase and 0-acetylhomoserine sulfhydrylase. Intracellular pools of methionine do not differ markedly in the mutant and in wild type, while the S-adenosylmethionine (SAM) pool is decreased in the mutant. Methionine adenosyltransferase was found to be inducible by methionine, SAM is postulated to be involved in regulation of methionine biosynthetic enzymes in A. nidulans. Differences in regulation of methionine biosynthesis in A. nidulans, Escherichia coli and Saccharomyces cerevisiae are discussed.


Enzyme Escherichia Coli Cysteine Methionine Aspergillus 
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Copyright information

© Springer-Verlag 1973

Authors and Affiliations

  • Norman J. Pieniążek
    • 1
  • Iwona M. Kowalska
    • 1
  • Piotr P. Stępień
    • 1
  1. 1.Department of GeneticsWarsaw UniversityWarsawPoland

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