Gh. Zhu et al., DEPENDENCE OF CATALYSIS AND CO2 O-2 SPECIFICITY OF RUBISCO ON THE CARBOXY-TERMINUS OF THE LARGE SUBUNIT AT DIFFERENT TEMPERATURES/, Photosynthesis research, 57(1), 1998, pp. 71-79
Variations in length and charge of the C-terminus of the Rubisco large
subunit (L) can be seen in L from different phylogenetic lineages. We
examined the catalytic parameters of Rubisco from higher plants and f
rom engineered Synechococcus rbcL in relation to differences in the C-
terminus. Among three selected higher plants, spinach, wheat, and Flav
eria pringlei, spinach Rubisco with the shortest C-tail extension (D-4
73 + 2) showed the lowest temperature response. The response of Rubisc
o from wheat (D-473 + 4) was intermediate, and the enzyme from F. prin
glei (D-473 + 12) displayed the highest temperature response in terms
of V-max for the carboxylase reaction. This observation was further in
vestigated in a model system: the temperature-response for carboxylati
on was enhanced after lengthening the C-terminus of the Synechococcus
large subunit protein by two amino acid residues (DK). The results poi
nt towards the length of the C-terminus as an additional factor for co
ntrolling Rubisco activity, especially as an adaptation that widens th
e temperature range in which the enzyme can function. Longer C-termini
, we suggest, could establish additional interactions with the protein
surface.