Regulation of the O-acetyl-L-serine(thiol)lyase activity in Monoraphidium braunii

J Physiol Biochem. 1998 Sep;54(3):141-8.

Abstract

Total level of O-acetyl-L-serine(thiol)lyase (OASTL) activity observed in Monoraphidium braunii fed-repleted cells decreases up to 40% after 24 h the carbon source was removed from the culture; however, no significant change in the activity is observed in N-starved cells. On the other hand, sulfur starvation induces OASTL activity in M. braunii, which may increase 2.5-fold after 36 h. Normal intracellular level of the activity is restored when a sulfur source, such as sulfate, sulfite, L-cysteine, L-methionine or glutathione is added to the culture. The induction of the OASTL activity requires de novo synthesis of protein, and thus the presence in the culture of adequate carbon and nitrogen sources. The OASTL isoenzymes from M. braunii cells are differently affected by S-starvation.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Carbon / metabolism
  • Cell Division
  • Chlorophyta / drug effects
  • Chlorophyta / enzymology*
  • Chlorophyta / growth & development*
  • Cycloheximide / pharmacology
  • Cysteine / metabolism
  • Cysteine Synthase / drug effects
  • Cysteine Synthase / isolation & purification
  • Cysteine Synthase / metabolism*
  • Glutathione / metabolism
  • Light
  • Methionine / metabolism
  • Nitrogen / metabolism
  • Protein Synthesis Inhibitors / pharmacology
  • Sulfonic Acids / metabolism
  • Sulfur / metabolism
  • Thiosulfates / metabolism
  • Time Factors

Substances

  • Protein Synthesis Inhibitors
  • Sulfonic Acids
  • Thiosulfates
  • Sulfur
  • Carbon
  • Cycloheximide
  • sulfamic acid
  • Methionine
  • Cysteine Synthase
  • Glutathione
  • Cysteine
  • Nitrogen