Abstract
At the C-terminal end of Rubisco's large subunit major differences in sequence length and in charges of the amino acid residues occur in unicellular organisms and in plants. This C-terminal segment of the large subunit participates in large movements during the catalytic cycle. It participates in the closing mechanism of the binding niche for the substrate RuBP, changing from an ordered structure in the “open” enzyme conformation to a position, stretched over the protein surface, in a “closed” conformation. We analyzed the sequence variability in the C terminus in rbcL to investigate whether this structurally important entity evolved in an ordered process. Cyanobacteria and chlorophytes show similar C-terminal sequences (DXX), whereby D-473 is the last strictly conserved amino acid residue for all rbcLs. Contrary to the gymnosperms (D + 2 residues), the C termini of the angiosperms show variable lengths from D + 2 to D + 17 residues. The plant orders of Asterales, Batales, Capparales, Caryophyllales, Fabales, Gentianales, Lamiales, Rubiales, Myrtales, Scrophulariales, and Solanales contain species with particularly elongated C termini. Recent studies regarding enzyme kinetics demonstrated that molecules with longer C termini are better adapted for a wider temperature range. We speculate that longer C termini confer properties to the enzyme that modulate the success of different species in different environments. This is supported by the fact that “modern” (e.g., phylogenetically young taxa in an actual radiation process) generally display a long C terminus, while conservative taxa have a relatively short C terminus.
Key words
Rubisco -
rbcL
- evolution - phylogenetic analysis - C terminus
