CC-4810 rbcL-L326I mt+
$30.00
From Robert J. Spreitzer, University of Nebraska, July 2014
Directed mutagenesis and chloroplast transformation of rbcL∆-25B1 mt+ (CC-4700) were used to create an L326I substitution (CTT-ATT) in the Rubisco large subunit, which causes a decrease in Rubisco holoenzyme stability (Zhu and Spreitzer 1996). This is the original mutant strain. It was created to investigate phylogenetic differences near large-subunit residue Val-331 (see rbcL-V331A) (Chen and Spreitzer 1989; Chen et al. 1991). The strain has been maintained with acetate medium in darkness to prevent selection for secondary mutations that may improve Rubisco function.
Chen Z, Spreitzer RJ (1989) Chloroplast intragenic suppression enhances the low CO2/O2 specificity of mutant ribulosebisphosphate carboxylase/oxygenase. J Biol Chem 264:3051-3053
Chen Z, Yu W, Lee JH, Diao R, Spreitzer RJ (1991) Complementing amino-acid substitutions within loop 6 of the alpha/beta-barrel active site influence the CO2/O2 specificity of chloroplast ribulose-1,5-bisphosphate carboxylase/oxygenase. Biochemistry 30:8846-8850
Zhu G, Spreitzer RJ (1996) Directed mutagenesis of chloroplast ribulose-1,5-bisphosphate carboxylase/oxygenase: Loop-6 substitutions complement for structural stability but decrease catalytic efficiency. J Biol Chem 271:18494-18498