CC-4843 rbcL-C256F/I265V mt+
$30.00
From Robert J. Spreitzer, University of Nebraska, August 2014
Directed mutagenesis and chloroplast transformation of rbcL∆-25B1 mt+ (CC-4700) were used to create C256F (TGT-TTC) and I265V (ATT-GTA) substitutions in the Rubisco large subunit, which cause decreases in carboxylation catalytic efficiency and CO2/O2 specificity (Du et al. 2003). This is the original mutant strain. It was created to investigate phylogenetic differences near large-subunit residue Leu-290 (see rbcL-L290F) (Chen et al. 1988; Spreitzer et al. 2005). The strain has been maintained with acetate medium in darkness to prevent selection for secondary mutations that may improve Rubisco function.
Chen Z, Chastain CJ, Al-Abed SR, Chollet R, Spreitzer RJ (1988) Reduced CO2/O2 specificity of ribulose-1,5-bisphosphate carboxylase/oxygenase in a temperature-sensitive chloroplast mutant of Chlamydomonas reinhardtii. Proc Natl Acad Sci USA 85:4696-4699
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
Spreitzer RJ, Peddi SR, Satagopan S (2005) Phylogenetic engineering at an interface between large and small subunits imparts land-plant kinetic properties to algal Rubisco. Proc Natl Acad Sci USA 102:17225-17230