CC-4943 rbcL-C369V 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), a C369V substitution (TGT-GTT) was created in the Rubisco large subunit. Because Cys-369 is methylated in Chlamydomonas Rubisco (Taylor et al. 2001), but replaced by Val in plant Rubisco (Du et al. 2003), the mutant was created to investigate the role of the modified residue in Rubisco structure or function. The C369F substitution causes small increases in Rubisco CO2/O2 specificity and carboxylation catalytic efficiency (Spreitzer et al., unpublished). This strain has been maintained with acetate medium in darkness to prevent selection for secondary mutations that may alter Rubisco function.
Du YC, Peddi SR, Spreitzer RJ (2003) Assessment of structural and functional divergence far from the large subunit active site of ribulose-1,5-bisphosphate carboxylase/oxygenase. J Biol Chem 278:49401-49405
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