This Article Full Text Full Text (PDF) All Versions of this Article: 138/1/433    most recent pp.104.057521v1 Alert me when this article is cited Alert me if a correction is posted Services Email this article to a friend Similar articles in this journal Similar articles in Web of Science Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via CrossRef Citing Articles via Web of Science (20) Citing Articles via Google Scholar Google Scholar Articles by Hopkins, L. Articles by Hawkesford, M. J. Search for Related Content PubMed PubMed Citation Articles by Hopkins, L. Articles by Hawkesford, M. J. Agricola Articles by Hopkins, L. Articles by Hawkesford, M. J.

BIOCHEMICAL PROCESSES AND MACROMOLECULAR STRUCTURES

O-Acetylserine and the Regulation of Expression of Genes Encoding Components for Sulfate Uptake and Assimilation in Potato¹

Laura Hopkins, Saroj Parmar, Anna Baszczyk, Holger Hesse, Rainer Hoefgen and Malcolm J. Hawkesford^*

Crop Performance and Improvement Division, Rothamsted Research, Harpenden, Hertfordshire, AL5 2JQ, United Kingdom (L.H., S.P., M.J.H.); Institute of Biochemistry and Biophysics, Polish Academy of Sciences, 02–106 Warsaw, Poland (A.B.); and Max-Planck-Institute of Molecular Plant Physiology, Department of Molecular Physiology, 14476 Potsdam-Golm, Germany (H.H., R.H.)

cDNAs encoding a high-affinity sulfate transporter and an adenosine 5'-phosphosulfate reductase from potato (Solanum tuberosum L. cv Désirée) have been cloned and used to examine the hypothesis that sulfate uptake and assimilation is transcriptionally regulated and that this is mediated via intracellular O-acetylserine (OAS) pools. Gas chromotography coupled to mass spectrometry was used to quantify OAS and its derivative, N-acetylserine. Treatment with external OAS increased sulfate transporter and adenosine 5'-phosphosulfate reductase gene expression consistent with a model of transcriptional induction by OAS. To investigate this further, the Escherichia coli gene cysE (serine acetyltransferase EC 2.3.1.30), which synthesizes OAS, has been expressed in potato to modify internal metabolite pools. Transgenic lines, with increased cysteine and glutathione pools, particularly in the leaves, had increased sulfate transporter expression in the roots. However, the small increases in the OAS pools were not supportive of the hypothesis that this molecule is the signal of sulfur (S) nutritional status. In addition, although during S starvation the content of S-containing compounds decreased (consistent with derepression as a mechanism of regulation), OAS pools increased only following extended starvation, probably as a consequence of the S starvation. Taken together, expression of these genes may be induced by a demand-driven model, via a signal from the shoots, which is not OAS. Rather, the signal may be the depletion of intermediates of the sulfate assimilation pathway, such as sulfide, in the roots. Finally, sulfate transporter activity did not increase in parallel with transcript and protein abundance, indicating additional posttranslational regulatory mechanisms.

Article, publication date, and citation information can be found at www.plantphysiol.org/cgi/doi/10.1104/pp.104.057521.

^* Corresponding author; e-mail malcolm.hawkesford{at}bbsrc.ac.uk; fax 44–1582–763010.

Received December 1, 2004; returned for revision February 4, 2005; accepted February 13, 2005.

This article has been cited by other articles:

				U. Scheerer, R. Haensch, R. R. Mendel, S. Kopriva, H. Rennenberg, and C. Herschbach Sulphur flux through the sulphate assimilation pathway is differently controlled by adenosine 5'-phosphosulphate reductase under stress and in transgenic poplar plants overexpressing {gamma}-ECS, SO, or APR J. Exp. Bot., November 18, 2009; (2009) erp327v1. [Abstract] [Full Text] [PDF]

				H. Rouached, M. Wirtz, R. Alary, R. Hell, A. B. Arpat, J.-C. Davidian, P. Fourcroy, and P. Berthomieu Differential Regulation of the Expression of Two High-Affinity Sulfate Transporters, SULTR1.1 and SULTR1.2, in Arabidopsis Plant Physiology, June 1, 2008; 147(2): 897 - 911. [Abstract] [Full Text] [PDF]

				M. Wirtz and R. Hell Dominant-Negative Modification Reveals the Regulatory Function of the Multimeric Cysteine Synthase Protein Complex in Transgenic Tobacco PLANT CELL, February 1, 2007; 19(2): 625 - 639. [Abstract] [Full Text] [PDF]

				J. A. Francois, S. Kumaran, and J. M. Jez Structural Basis for Interaction of O-Acetylserine Sulfhydrylase and Serine Acetyltransferase in the Arabidopsis Cysteine Synthase Complex PLANT CELL, December 1, 2006; 18(12): 3647 - 3655. [Abstract] [Full Text] [PDF]

				A. Maruyama-Nakashita, Y. Nakamura, T. Tohge, K. Saito, and H. Takahashi Arabidopsis SLIM1 Is a Central Transcriptional Regulator of Plant Sulfur Response and Metabolism PLANT CELL, November 1, 2006; 18(11): 3235 - 3251. [Abstract] [Full Text] [PDF]

				F. F. Nocito, C. Lancilli, B. Crema, P. Fourcroy, J.-C. Davidian, and G. A. Sacchi Heavy Metal Stress and Sulfate Uptake in Maize Roots Plant Physiology, July 1, 2006; 141(3): 1138 - 1148. [Abstract] [Full Text] [PDF]

				S. KOPRIVA Regulation of Sulfate Assimilation in Arabidopsis and Beyond Ann. Bot., April 1, 2006; 97(4): 479 - 495. [Abstract] [Full Text] [PDF]