Evidence for functional convergence of redox regulation in G6PDH isoforms of cyanobacteria and higher plants.

In a recent paper (Wenderoth et al., J Biol Chem 272: 26985-26990, 1997) we reported that the positions of the two redox regulatory cysteines identified in a plastidic G6PD isoform from potato (Solanum tuberosum L.) differ substantially from those conserved in cyanobacterial G6PDH sequences. To investigate the origin of redox regulation in G6PDH enzymes from photoautotrophic organisms, we isolated and characterized several G6PD cDNA sequences from higher plants and from a green and a red alga. Alignments of the deduced amino acid sequences showed that the cysteine residues cluster in the coenzyme-binding domain of the plastidic isoforms and are conserved at three out of six positions. Comparison of the mature proteins and the signal peptides revealed that two different plastidic G6PDH classes (P1 and P2) evolved from a common ancestral gene. The two algal sequences branch off prior to this class separation in higher plants, sharing about similar amino acid identity with either of the two plastidic G6PDH classes. The genes for cytosolic plant isoforms clearly share a common ancestor with animal and fungal G6PDH homologues, whereas the cyanobacterial isoforms branch within the eubacterial G6PDH sequences. The data suggest that cysteine-mediated redox regulation arose independently in G6PDH isoenzymes of eubacterial and eukaryotic lineages.