Rubisco surprises in dinoflagellates.

Rubisco surprises in dinoflagellates.

Continued evolutionary surprises among dinoflagellates.

I t is well established that chloroplasts in green and red algae are derived from a primary endosymbiotic event between a cyanobacterium and a eukaryotic organism 1 billion years ago (Fig. 1; refs. 1 and 2). Although these two groups account for many of the world’s photosynthetic species, most other major taxonomic groups of photosynthetic organisms (stramenopiles—including diatoms, phaeophytes...

Rubisco in marine symbiotic dinoflagellates: form II enzymes in eukaryotic oxygenic phototrophs encoded by a nuclear multigene family.

Genes encoding ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco) were cloned from dinoflagellate symbionts (Symbiodinium spp) of the giant clam Tridacna gigas and characterized. Strikingly, Symbiodinium Rubisco is completely different from other eukaryotic (form I) Rubiscos: it is a form II enzyme that is approximately 65% identical to Rubisco from Rhodospirillum rubrum (Rubisco forms I...

Rubisco, Rubisco activase, and global climate change.

Global warming and the rise in atmospheric CO(2) will increase the operating temperature of leaves in coming decades, often well above the thermal optimum for photosynthesis. Presently, there is controversy over the limiting processes controlling photosynthesis at elevated temperature. Leading models propose that the reduction in photosynthesis at elevated temperature is a function of either de...

Rubisco in complex with Rubisco large subunit methyltransferase.

SET domain protein lysine methyltransferases (PKMT) are a structurally unique class of enzymes that catalyze the specific methylation of lysine residues in a number of different substrates. Especially histone-specific SET domain PKMTs have received widespread attention because of their roles in the regulation of epigenetic gene expression and the development of some cancers. Rubisco large subun...