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Journal of Bacteriology, February 2001, p. 1069-1077, Vol. 183, No. 3
0021-9193/01/$04.00+0   DOI: 10.1128/JB.183.3.1069-1077.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.

Starchless Mutants of Chlamydomonas reinhardtii Lack the Small Subunit of a Heterotetrameric ADP-Glucose Pyrophosphorylase

Christophe Zabawinski,1 Nathalie Van Den Koornhuyse,1 Christophe D'Hulst,1 Ralf Schlichting,2 Christoph Giersch,2 Brigitte Delrue,1 Jean-Marie Lacroix,1 Jack Preiss,3 and Steven Ball1,*

Laboratoire de Chimie Biologique, Unité Mixte de Recherche du C.N.R.S. No. 8576, Université des Sciences et Technologies de Lille, 59655 Villeneuve d'Ascq Cedex, France1; Institut fuer Botanik, Technische Universität, D-64287 Darmstadt, Germany2; and Department of Biochemistry, Michigan State University, East Lansing, Michigan 488243

Received 30 June 2000/Accepted 26 October 2000

ADP-glucose synthesis through ADP-glucose pyrophosphorylase defines the major rate-controlling step of storage polysaccharide synthesis in both bacteria and plants. We have isolated mutant strains defective in the STA6 locus of the monocellular green alga Chlamydomonas reinhardtii that fail to accumulate starch and lack ADP-glucose pyrophosphorylase activity. We show that this locus encodes a 514-amino-acid polypeptide corresponding to a mature 50-kDa protein with homology to vascular plant ADP-glucose pyrophosphorylase small-subunit sequences. This gene segregates independently from the previously characterized STA1 locus that encodes the large 53-kDa subunit of the same heterotetramer enzyme. Because STA1 locus mutants have retained an AGPase but exhibit lower sensitivity to 3-phosphoglyceric acid activation, we suggest that the small and large subunits of the enzyme define, respectively, the catalytic and regulatory subunits of AGPase in unicellular green algae. We provide preliminary evidence that both the small-subunit mRNA abundance and enzyme activity, and therefore also starch metabolism, may be controlled by the circadian clock.

* Corresponding author. Mailing address: Laboratoire de Chimie Biologique, Unité Mixte de Recherche du C.N.R.S. No. 8576, Batiment C9, Université des Sciences et Technologies de Lille, 59655 Villeneuve d'Ascq Cedex, France. Phone: 33 3 20.43.65.43. Fax: 33 3 20.43.65.43. E-mail: Steven.Ball{at}univ-lille1.fr.

Journal of Bacteriology, February 2001, p. 1069-1077, Vol. 183, No. 3
0021-9193/01/$04.00+0   DOI: 10.1128/JB.183.3.1069-1077.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.


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