CC-4854 rbcL-L290F/rbcS2-C65S mt+ (R88-5A revertant of 68-4PP)
$30.00
From Robert J. Spreitzer, University of Nebraska, August 2014
R88-5A was recovered as a spontaneous photosynthesis-competent revertant of rbcL-L290F mt+ (68-4PP) (Hong 1996; Hong and Spreitzer 1997). It results from a transversion mutation in rbcS2 that causes a C65S substitution (TGC-TCC) in the Rubisco small subunit, which increases the CO2/O2 specificity of the original mutant enzyme (Genkov et al. 2006). See also S88-5A. Gene-centromere mapping indicated that rbcS2 is 20 map units from its centromere (Du et al. 2000). This is the original revertant strain. It has been maintained with acetate medium in darkness to prevent selection for secondary mutations that may improve Rubisco function.
Du YC, Hong S, Spreitzer RJ (2000) RbcS suppressors enhance the CO2/O2 specificity and thermal stability of rbcL-mutant ribulose-1,5-bisphosphate carboxylase/oxygenase. Proc Natl Acad Sci USA 97:14206-14211
Genkov T, Du YC, Spreitzer RJ (2006) Small-subunit cysteine-65 substitutions can suppress or induce alterations in the large-subunit catalytic efficiency and holoenzyme thermal stability of ribulose-1,5-bisphosphate carboxylase/oxygenase. Arch Biochem Biophys 451:167-174
Hong S (1996) Nuclear mutations affect the catalysis, stability, and expression of chloroplast ribulose-1,5-bisphosphate carboxylase/oxygenase in Chlamydomonas reinhardtii. Ph. D. thesis, University of Nebraska
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