CC-4938 rbcL-P104A/P151A mt+
$30.00
From Robert J. Spreitzer, University of Nebraska, November 2014
Using standard methods of directed mutagenesis and chloroplast transformation of rbcL∆-MX3312 mt+ (CC-4696) (Satagopan and Spreitzer 2004), two substitutions (P104A and P151A) were created together in the Rubisco large subunit. Because Pro-104 and Pro-151 are hydroxylated (Taylor et al. 2001), this mutant was created to investigate the role of the modified residues in Rubisco structure or function. The P104A/P151A substitutions cause decreases in Rubisco CO2/O2 specificity and carboxylation catalytic efficiency, but have only minor effect on the photosynthetic growth of the mutant cells (Spreitzer et al., unpublished). This strain has been maintained with acetate medium in darkness to prevent selection for secondary mutations that may improve Rubisco function.
Satagopan S, Spreitzer RJ (2004) Substitutions at the Asp-473 latch residue of Chlamydomonas ribulosebisphosphate carboxylase/oxygenase cause decreases in carboxylation efficiency and CO2/O2 specificity. J Biol Chem 279:14240-14244
Taylor TC, Backlund A, Bjorhall K, Spreitzer RJ, Andersson I (2001) First crystal structure of Rubisco from a green alga, Chlamydomonas reinhardtii. J Biol Chem 276:48159-48164