title: Impact of sulfur starvation on cysteine biosynthesis in T-DNA mutants deficient for compartment-specific serine-acetyltransferase.
abstract: Sulfur plays a pivotal role in the cellular metabolism of many organisms. In plants, the uptake and assimilation of sulfate is strongly regulated at the transcriptional level. Regulatory factors are the demand of reduced sulfur in organic or non-organic form and the level of O-acetylserine (OAS), the carbon precursor for cysteine biosynthesis. In plants, cysteine is synthesized by action of the cysteine-synthase complex (CSC) containing serine acetyltransferase (SAT) and O-acetylserine-(thiol)-lyase (OASTL). Both enzymes are located in plastids, mitochondria and the cytosol. The function of the compartmentation of the CSC to regulate sulfate uptake and assimilation is still not clearly resolved. To address this question, we analyzed Arabidopsis thaliana mutants for the plastidic and cytosolic SAT isoenzymes under sulfur starvation conditions. In addition, subcellular metabolite analysis by non-aqueous fractionation revealed distinct changes in subcellular metabolite distribution upon short-term sulfur starvation. Metabolite and transcript analyses of SERAT1.1 and SERAT2.1 mutants [previously analyzed in Krueger et al. (Plant Cell Environ 32:349-367, 2009)] grown under sulfur starvation conditions indicate that both isoenzymes do not contribute directly to the transcriptional regulation of genes involved in sulfate uptake and assimilation. Here, we summarize the current knowledge about the regulation of cysteine biosynthesis and the contribution of the different compartments to this metabolic process. We relate hypotheses and views of the regulation of cysteine biosynthesis with our results of applying sulfur starvation to mutants impaired in compartment-specific cysteine biosynthetic enzymes.
authors.affiliation: Max Planck Institut für Molekulare Pflanzenphysiologie, Potsdam-Golm, Germany.
authors.forename: Stephan
authors.initials: S
authors.lastname: Krueger
authors.forename: Andrea
authors.initials: A
authors.lastname: Donath
authors.forename: M Carmen
authors.initials: MC
authors.lastname: Lopez-Martin
authors.forename: Rainer
authors.initials: R
authors.lastname: Hoefgen
authors.forename: Cecilia
authors.initials: C
authors.lastname: Gotor
authors.forename: Holger
authors.initials: H
authors.lastname: Hesse
mesh_terms: D027321:Anion Transport Proteins / Q000235:genetics / Q000378:metabolism; D017360:Arabidopsis / Q000201:enzymology / Q000235:genetics* / Q000378:metabolism*; D029681:Arabidopsis Proteins / Q000235:genetics / Q000378:metabolism; D001692:Biological Transport; D019757:Carbon-Oxygen Lyases / Q000378:metabolism; D002736:Chloroplasts / Q000378:metabolism; D003545:Cysteine / Q000096:biosynthesis*; D003547:Cysteine Synthase / Q000378:metabolism; D003600:Cytosol / Q000201:enzymology / Q000378:metabolism; D004269:DNA, Bacterial / Q000235:genetics; D018506:Gene Expression Regulation, Plant; D055786:Gene Knockout Techniques; D030821:Plants, Genetically Modified; D010957:Plasmids; D018087:Plastids / Q000378:metabolism; D016133:Polymerase Chain Reaction; D018749:RNA, Plant; D036226:Seedlings / Q000378:metabolism; D012694:Serine / Q000031:analogs & derivatives / Q000378:metabolism; D051050:Serine O-Acetyltransferase / Q000235:genetics / Q000378:metabolism*; D013431:Sulfates / Q000378:metabolism; D013438:Sulfhydryl Compounds / Q000378:metabolism; D013455:Sulfur / Q000378:metabolism*
chemical_list: D027321:Anion Transport Proteins; D029681:Arabidopsis Proteins; D004269:DNA, Bacterial; D018749:RNA, Plant; D013431:Sulfates; D013438:Sulfhydryl Compounds; C550543:Sultr4;1 protein, Arabidopsis; C036483:T-DNA; D012694:Serine; D013455:Sulfur; D051050:Serine O-Acetyltransferase; D003547:Cysteine Synthase; C018725:O-acetylhomoserine (thiol)-lyase; D019757:Carbon-Oxygen Lyases; C043943:O-acetylserine; D003545:Cysteine