First published online November 7, 2002; 10.1104/pp.012484
Plant Physiol, December 2002, Vol. 130, pp. 2076-2084
The sac Mutants of Chlamydomonas
reinhardtii Reveal Transcriptional and Posttranscriptional
Control of Cysteine Biosynthesis1
Cristina G.
Ravina,
Chwenn-In
Chang,
George P.
Tsakraklides,
Jeffery P.
McDermott,
Jose M.
Vega,
Thomas
Leustek,
Cecilia
Gotor, and
John P.
Davies2*
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.)
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.
1
This work was funded in part by the United
States National Science Foundation (grant no. IBN-9817594 to T.L.), by
the U.S. Department of Agriculture (grant no. 9900622 to J.P.D.), and
by funds from the Iowa State University Office of Biotechnology.
2
Present address: Exelixis Plant Sciences, 16160 SW Upper
Boones Ferry Road, Portland, OR 97224.
*
Corresponding author; e-mail jdavies{at}exelixis.com; fax
503-670-7702.
© 2002 American Society of Plant Biologists
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