Plant Physiology Preview
Published on November 7, 2002; 10.1104/pp.012484
Received August 2, 2002
Returned for revision August 11, 2002
Accepted August 22, 2002
The sac Mutants of Chlamydomonas reinhardtii Reveal Transcriptional and Posttranscriptional Control of Cysteine Biosynthesis
Cristina G. Ravina , Chwenn-In Chang , George P. Tsakraklides , Jeffery P. McDermott , Jose M. Vega , Thomas Leustek , Cecilia Gotor , and John P. Davies *
Instituto de Bioquímica Vegetal y Fotosíntesis, Consejo Superior de Investigaciones Cientificas (C.G.R., C.G.) and Departamento de Bioquímica Vegetal y Biología Molecular, Facultad de Química (J.M.V.), Universidad de Sevilla, 41092 Sevilla, Spain; Biotechnology Center for Agriculture and the Environment and the Department of Plant Biology and Pathology, Rutgers University, New Brunswick, New Jersey 08901-8520 (C.-I.C., G.P.T., T.L.); and Department of Botany, Iowa State University, Ames, Iowa 50011 (J.P.M., J.P.D.)
* Corresponding author; email: jdavies{at}exelixis.com.
Algae and vascular plants are cysteine (Cys) prototrophs. They are able to import, reduce, and assimilate sulfate into Cys, methionine, and other organic sulfur-containing compounds. Characterization of genes encoding the enzymes required for Cys biosynthesis from the unicellular green alga Chlamydomonas reinhardtii reveals that transcriptional and posttranscriptional mechanisms regulate the pathway. The derived amino acid sequences of the C. reinhardtii genes encoding 5'-adenylylsulfate (APS) reductase and serine (Ser) acetyltransferase are orthologous to sequences from vascular plants. The Cys biosynthetic pathway of C. reinhardtii is regulated by sulfate availability. The steady-state level of transcripts and activity of ATP sulfurylase, APS reductase, Ser acetyltransferase, and O-acetyl-Ser (thiol) lyase increase when cells are deprived of sulfate. The sac1 mutation, which impairs C. reinhardtii ability to acclimate to sulfur-deficient conditions, prevents the increase in accumulation of the transcripts encoding these enzymes and also prevents the increase in activity of all the enzymes except APS reductase. The sac2 mutation, which does not affect accumulation of APS reductase transcripts, blocks the increase in APS reductase activity. These results suggest that APS reductase activity is regulated posttranscriptionally in a SAC2-dependent process.
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