CC-1227 a12-2B (ac214) mt+
$30.00
From Laurens Mets, 1981
Phenotype: requires acetate
This mutant was isolated by Spreitzer and Mets using 5-fluorodeoxyuridine plus ethyl methanesulfonate mutagenesis, and was originally described as isolate 12-2B, unable to fix CO2. Subsequent work by Salvucci and Ogren showed it was deficient in phosphoribulokinase activity, and Roesler et al. demonstrated that the mutation is a C to T transition that changes the conserved arginine at position 64 to cysteine in the structural gene for phosphoribulokinase. Avilan et al. (1997) made other site-directed changes at this position and assayed enzyme activity after expression of the mutated gene in E. coli.
Spreitzer and Mets reported relatively close linkage of the ac214 (12-2B) mutant to its centromere (ac/y1 14:14:3). Crosses at the Chlamydomonas Genetics Center assigned this locus to linkage group XII/XIII. Dutcher et al. confirmed its linkage to NIC15.
CC-1228 is the same mutation in mt-. CC-2259 is another isolate of the same strain, acquired more recently from Spreitzer.
Spreitzer RJ, Mets L (1981) Photosynthesis-deficient Mutants of Chlamydomonas reinhardii with Associated Light-sensitive Phenotypes. Plant Physiol 67:565-569
Salvucci ME, Ogren WL (1985) A Chlamydomonas reinhardii mutant with catalytically and structurally altered ribulose-5-phosphate kinase. Planta 165:340-347
Dutcher SK, Power J, Galloway RE, Porter ME (1991) Reappraisal of the genetic map of Chlamydomonas reinhardtii. J Hered 82:295-301
Roesler KR, Marcotte BL, Ogren WL (1992) Functional Importance of Arginine 64 in Chlamydomonas reinhardtii Phosphoribulokinase. Plant Physiol 98:1285-1289
Avilan L, Gontero B, Lebreton S, Ricard J (1997) Information transfer in multienzyme complexes--2. The role of Arg64 of Chlamydomonas reinhardtii phosphoribulokinase in the information transfer between glyceraldehyde-3-phosphate dehydrogenase and phosphoribulokinase. Eur J Biochem 250:296-302