CC-4835 rbcL-L290F/A222T mt+ (R96-8E revertant of 68-4PP)
$30.00
From Robert J. Spreitzer, University of Nebraska, August 2014
R96-8E was recovered as a photosynthesis-competent revertant after methyl-methanesulfonate mutagenesis of rbcL-L290F mt+ (68-4PP) (Hong and Spreitzer 1997). It results from an intragenic-suppressor mutation that causes an A222T substitution (GCT-ACT) in the Rubisco large subunit, which increases the CO2/O2 specificity of the original mutant enzyme (Hong and Spreitzer 1997; Du and Spreitzer 2000). The L290F/A222T mutant-enzyme x-ray crystal structure has been solved (Karkehabadi et al. 2005). The strain has been maintained with acetate medium in darkness to prevent selection for secondary mutations that may improve Rubisco function.
Du YC, Spreitzer RJ (2000) Suppressor mutations in the chloroplast-encoded large subunit improve the thermal stability of wild-type ribulose-1,5-bisphosphate carboxylase/oxygenase. J Biol Chem 275:19844-19847
Hong S, Spreitzer RJ (1997) Complementing substitutions at the bottom of the barrel influence catalysis and stability of ribulose-bisphosphate carboxylase/oxygenase. J Biol Chem 272:11114-11117
Karkehabadi S, Taylor TC, Spreitzer RJ, Andersson I (2005) Altered intersubunit interactions in crystal structures of catalytically-compromised ribulose-1,5-bisphosphate carboxylase/oxygenase. Biochemistry 44:113-120