CC-5033 rbcL-V149Q/V221C/C256F/K258R/I265V/I282H/rbcS1-ABSO mt+ (AG256)
$30.00
From Robert J. Spreitzer, University of Nebraska, November 2014
Using standard methods of directed mutagenesis and chloroplast transformation of rbcL∆/rbcS1-ABSO mt+ (Spreitzer et al. 2005), Boon Hoe Lim in Spreitzer’s group created six substitutions (V149Q, V221C, C256F, K258R, I265V, and I282H) together in the Rubisco large subunit. This mutant (also named AG256) represents one of 15 “associated groups” of amino acids that differ between Chlamydomonas and land plants (Du et al. 2003). It was created to investigate phylogenetic differences that influence Rubisco catalysis (Spreitzer et al. 2005). The mutant strain has a small decrease in Rubisco holoenzyme when grown at 35 °C (Lim and Spreitzer, unpublished). It has been maintained with acetate medium in darkness to prevent selection for secondary mutations that may improve Rubisco function.
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