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Significance Rubisco activase (Rca) regulates the activation state of Rubisco, the carboxylating enzyme of photosynthesis. Regulation of Rca by redox status of cysteine residues in species such asArabidopsis is well recognized, but the role of recently identified phosphorylation of Rca at threonine-78 was uncertain. We now show a regulatory role ofArabidopsis Rca phosphorylation. Surprisingly, we also observed that the conservative substitution of serine for threonine-78 results in impaired functionality of Rca in vivo that is associated with retention of phosphorylation well into the light period and with reduced plant growth. This likely reflects in part the specificity of the requisite protein kinase(s) for serine versus threonine and may explain the absence of serine at this position in terrestrial plants.

In vivo evidence for a regulatory role of phosphorylation of Arabidopsis Rubisco activase at the Thr78 site