CC-4825 rbcL-S379A mt+ (original isolate)
$30.00
From Robert J. Spreitzer, University of Nebraska, July 2014
Phenotype: requires acetate, sensitive to light
Directed mutagenesis and chloroplast co-transformation of wild-type 2137 mt+ (CC-3269) were used to create an S379A substitution (TCA-GCA) in the Rubisco large subunit, which causes a decrease in Rubisco CO2/O2 specificity but not holoenzyme stability (Zhu and Spreitzer 1994). This is the original mutant strain. It was created due to previous studies of Synechococcus and Rhodospirillum rubrum Rubisco (Harpel and Hartman 1992; Lee and McFadden 1992). The strain has been maintained with acetate medium in darkness since its creation.
Harpel MR, Hartman FC (1992) Enhanced CO2/O2 specificity of a site-directed mutant of ribulosebisphosphate carboxylase/oxygenase. J Biol Chem 267:6475-6478
Lee GJ, McFadden BA (1992) Serine-376 contributes to the binding of substrate by ribulose-bisphosphate carboxylase/oxygenase from Anacystis nidulans. Biochemistry 31:2304-2308
Zhu G, Spreitzer RJ (1994) Directed mutagenesis of chloroplast ribulose-bisphosphate carboxylase/oxygenase: Substitutions at large subunit asparagine 123 and serine 379 decrease CO2/O2 specificity. J Biol Chem 269:3952-3956