Analysis of the Arabidopsis O-acetylserine(thiol)lyase gene family demonstrates compartment-specific differences in the regulation of cysteine synthesis

Plant Cell. 2008 Jan;20(1):168-85. doi: 10.1105/tpc.107.056747. Epub 2008 Jan 25.

Abstract

Cys synthesis in plants takes place in plastids, cytosol, and mitochondria. Why Cys synthesis is required in all compartments with autonomous protein biosynthesis and whether Cys is exchanged between them has remained enigmatic. This question was addressed using Arabidopsis thaliana T-DNA insertion lines deficient in the final step of Cys biosynthesis catalyzed by the enzyme O-acetylserine(thiol)lyase (OAS-TL). Null alleles of oastlA or oastlB alone showed that cytosolic OAS-TL A and plastid OAS-TL B were completely dispensable, although together they contributed 95% of total OAS-TL activity. An oastlAB double mutant, relying solely on mitochondrial OAS-TL C for Cys synthesis, showed 25% growth retardation. Although OAS-TL C alone was sufficient for full development, oastlC plants also showed retarded growth. Targeted affinity purification identified the major OAS-TL-like proteins. Two-dimensional gel electrophoresis and mass spectrometry showed no compensatory changes of OAS-TL isoforms in the four mutants. Steady state concentrations of Cys and glutathione and pulse-chase labeling with [35S]sulfate indicated strong perturbation of primary sulfur metabolism. These data demonstrate that Cys and also sulfide must be sufficiently exchangeable between cytosol and organelles. Despite partial redundancy, the mitochondria and not the plastids play the most important role for Cys synthesis in Arabidopsis.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Arabidopsis / enzymology*
  • Arabidopsis / genetics
  • Arabidopsis / growth & development
  • Arabidopsis Proteins / chemistry
  • Arabidopsis Proteins / isolation & purification
  • Catalysis
  • Catalytic Domain
  • Cell Compartmentation*
  • Cysteine / biosynthesis*
  • DNA, Bacterial
  • Escherichia coli / enzymology
  • Genome, Plant
  • Isoenzymes
  • Models, Biological
  • Molecular Sequence Data
  • Multigene Family*
  • Mutagenesis, Insertional
  • Phenotype
  • Protein Processing, Post-Translational
  • Serine O-Acetyltransferase / chemistry
  • Serine O-Acetyltransferase / genetics*
  • Serine O-Acetyltransferase / isolation & purification
  • Subcellular Fractions / enzymology
  • Sulfur / metabolism
  • Sulfur Radioisotopes

Substances

  • Arabidopsis Proteins
  • DNA, Bacterial
  • Isoenzymes
  • Sulfur Radioisotopes
  • T-DNA
  • Sulfur
  • Serine O-Acetyltransferase
  • Cysteine

Associated data

  • RefSeq/NM_125059