Redox control of the activity of phosphoglycerate kinase in synechocystis sp. PCC6803

Abstract

Phosphoglycerate kinase catalyzes the phosphorylation of 3-phosphoglycerate to 1,3-diphosphoglycerate using ATP within the Calvin-Benson cycle. Recent proteomic analysis of thioredoxin targets in Synechocystis sp. PCC6803 revealed this enzyme as one of the target candidates, and we present here further characterization of the interaction between these proteins. By using the His-tagged recombinant enzyme, we determined that Synechocystis phosphoglycerate kinase is inactivated by oxidation and that the oxidized enzyme is easily reduced and reactivated by thioredoxin, suggesting a role for thioredoxin in the control of the redox state of this enzyme. In addition, thorough analysis of redox-relevant cysteines revealed that a cysteine pair, Cys314 and Cys340, located on the C-terminal domain of the molecule, is critical for redox regulation. © 2013 The Author 2013. Published by Oxford University Press on behalf of Japanese Society of Plant Physiologists. All rights reserved. For permissions, please email: journals.permissions@oup.com.