Strains
From Lai-Wa Tam, Lefebvre lab, University of Minnesota, July 2014
Phenotype: mostly flagella-less
CC-4780 lf2-2 lf3-2 [381-F9]
$30.00
$30.00
From Lai-Wa Tam, Lefebvre lab, University of Minnesota, July 2014
Phenotype: mostly flagella-less
CC-4781 lf5-2 lf4-9 [2D]
$30.00
$30.00
From Lai-Wa Tam, Lefebvre lab, University of Minnesota, July 2014
Phenotype: long flagella
From Robert J. Spreitzer, University of Nebraska, July 2014
Phenotype: requires acetate, sensitive to light
Following 5-fluorodeoxyuridine treatment and ethyl-methanesulfonate mutagenesis of wild-type 2137 mt+ cells, colonies were screened for light-sensitive, acetate-requiring phenotypes (Spreitzer and Mets 1981). Mutant 10-6C was found to arise from a G171D substitution (GGT-GAT) in the chloroplast-encoded large subunit of Rubisco (Dron et al. 1983), which causes a decrease in Rubisco activities and alters the large-subunit isoelectric point (Spreitzer and Mets 1980; Spreitzer et al. 1982). Selection for photosynthesis-competent revertants yielded only true revertants (Spreitzer et al. 1982, 1985). This strain was recovered from a cross between 10-6C mt+ (CC-1815) and pf2 mt-, and has been maintained with acetate medium in darkness since 1980.
Dron M, Rahire M, Rochaix JD, Mets L (1983) First DNA sequence of a chloroplast mutation: A missense alteration in the ribulosebisphosphate carboxylase large subunit gene. Plasmid 9:321-324
Spreitzer RJ, Jordan DB, Ogren WL (1982) Biochemical and genetic analysis of an RuBP carboxylase/oxygenase mutant and revertants of Chlamydomonas reinhardtii. FEBS Lett 148:117-121
Spreitzer RJ, Rahire M, Rochaix JD (1985) True reversion of a mutation in the chloroplast gene encoding the large subunit of ribulosebisphosphate carboxylase/oxygenase in Chlamydomonas. Curr Genet 9:229-231
Spreitzer RJ, Mets L (1980) Non-mendelian mutation affecting ribulose-1,5-bisphosphate carboxylase structure and activity. Nature 285:114-115
Spreitzer RJ, Mets L (1981) Photosynthesis-deficient mutants of Chlamydomonas with associated light-sensitive phenotypes. Plant Physiol 67:565-569
From Robert J. Spreitzer, University of Nebraska, July 2014
Phenotype: requires acetate, sensitive to light
Following 5-fluorodeoxyuridine treatment and ethyl-methanesulfonate mutagenesis of wild-type 2137 mt+ cells, colonies were screened for light-sensitive, acetate-requiring phenotypes (Spreitzer and Mets 1981). Mutant 10-6C was found to arise from a G171D substitution (GGT-GAT) in the chloroplast-encoded large subunit of Rubisco (Dron et al. 1983), which causes a decrease in Rubisco activities and alters the large-subunit isoelectric point (Spreitzer and Mets 1980; Spreitzer et al. 1982). Selection for photosynthesis-competent revertants yielded only true revertants (Spreitzer et al. 1982, 1985). This strain was recovered from a cross between 10-6C mt+ (CC-1815) and pf2 mt-, and has been maintained with acetate medium in darkness since 1980.
Dron M, Rahire M, Rochaix JD, Mets L (1983) First DNA sequence of a chloroplast mutation: A missense alteration in the ribulosebisphosphate carboxylase large subunit gene. Plasmid 9:321-324
Spreitzer RJ, Jordan DB, Ogren WL (1982) Biochemical and genetic analysis of an RuBP carboxylase/oxygenase mutant and revertants of Chlamydomonas reinhardtii. FEBS Lett 148:117-121
Spreitzer RJ, Rahire M, Rochaix JD (1985) True reversion of a mutation in the chloroplast gene encoding the large subunit of ribulosebisphosphate carboxylase/oxygenase in Chlamydomonas. Curr Genet 9:229-231
Spreitzer RJ, Mets L (1980) Non-mendelian mutation affecting ribulose-1,5-bisphosphate carboxylase structure and activity. Nature 285:114-115
Spreitzer RJ, Mets L (1981) Photosynthesis-deficient mutants of Chlamydomonas with associated light-sensitive phenotypes. Plant Physiol 67:565-569
From Robert J. Spreitzer, University of Nebraska, July 2014
Phenotype: requires acetate, sensitive to light
The 18-5B chloroplast mutant was recovered by screening a collection of acetate-requiring mutants for lack of complementation with a known Rubisco rbcL mutant (Spreitzer and Ogren 1983). It results from an rbcL nonsense mutation that changes the codon for Trp-451 (TGG) to opal (TGA) (Spreitzer et al. 1985). Selection for photosynthesis-competent revertants yielded heteroplasmic strains that result from chloroplast informational (tRNA) suppression (Spreitzer et al. 1984; Spreitzer and Chastain 1987; Zhang and Spreitzer 1990). This strain was recovered from a cross between the original 18-5B mt+ and pf2 mt-, and has been maintained with acetate medium in darkness since its isolation.
Spreitzer RJ, Chastain CJ (1987) Heteroplasmic suppression of an amber mutation in the Chlamydomonas chloroplast gene that encodes the large subunit of ribulosebisphosphate carboxylase/oxygenase. Curr Genet 11:611-616
Spreitzer RJ, Chastain CJ, Ogren WL (1984) Chloroplast gene suppression of defective ribulosebisphosphate carboxylase/oxygenase in Chlamydomonas reinhardtii: Evidence for stable heteroplasmic genes. Curr Genet 9:83-89
Spreitzer RJ, Goldschmidt-Clermont M, Rahire M, Rochaix JD (1985) Nonsense mutations in the Chlamydomonas chloroplast gene that codes for the large subunit of ribulosebisphosphate carboxylase/oxygenase. Proc Natl Acad Sci USA 82:5460-5464
Spreitzer RJ, Ogren WL (1983) Rapid recovery of chloroplast mutations affecting ribulosebisphosphate carboxylase/oxygenase in Chlamydomonas reinhardtii. Proc Natl Acad Sci USA 80:6293-6297
Zhang D, Spreitzer RJ (1990) Evidence for informational suppression within the chloroplast of Chlamydomonas reinhardtii. Curr Genet 17:49-53
From Robert J. Spreitzer, University of Nebraska, July 2014
Phenotype: requires acetate, sensitive to light
The 18-7G chloroplast mutant was recovered by screening a collection of acetate-requiring mutants for lack of complementation with a known Rubisco rbcL mutant (Spreitzer and Ogren 1983). It results from an rbcL nonsense mutation that changes the codon for Trp-66 (TGG) to amber (TAG) (Spreitzer et al. 1985). Selection for photosynthesis-competent revertants yielded heteroplasmic strains that result from chloroplast informational (tRNA) suppression (Spreitzer and Chastain 1987; Yu and Spreitzer 1992). This strain was recovered from a cross between the original 18-7G mt+ (CC-2653) and pf2 mt-, and has been used as a host for chloroplast rbcL transformation. It has been maintained with acetate medium in darkness since its isolation.
Spreitzer RJ, Chastain CJ (1987) Heteroplasmic suppression of an amber mutation in the Chlamydomonas chloroplast gene that encodes the large subunit of ribulosebisphosphate carboxylase/oxygenase. Curr Genet 11:611-616
Spreitzer RJ, Goldschmidt-Clermont M, Rahire M, Rochaix JD (1985) Nonsense mutations in the Chlamydomonas chloroplast gene that codes for the large subunit of ribulosebisphosphate carboxylase/oxygenase. Proc Natl Acad Sci USA 82:5460-5464
Spreitzer RJ, Ogren WL (1983) Rapid recovery of chloroplast mutations affecting ribulosebisphosphate carboxylase/oxygenase in Chlamydomonas reinhardtii. Proc Natl Acad Sci USA 80:6293-6297
Yu W, Spreitzer RJ (1992) Chloroplast heteroplasmicity is stabilized by an amber-suppressor tryptophan tRNA(CUA). Proc Natl Acad Sci USA 89:3904-3907
From Robert J. Spreitzer, University of Nebraska, July 2014
Phenotype: requires acetate, sensitive to light
The 18-7G chloroplast mutant was recovered by screening a collection of acetate-requiring mutants for lack of complementation with a known Rubisco rbcL mutant (Spreitzer and Ogren 1983). It results from an rbcL nonsense mutation that changes the codon for Trp-66 (TGG) to amber (TAG) (Spreitzer et al. 1985). Selection for photosynthesis-competent revertants yielded heteroplasmic strains that result from chloroplast informational (tRNA) suppression (Spreitzer and Chastain 1987; Yu and Spreitzer 1992). This strain was recovered from a cross between the original 18-7G mt+ (CC-2653) and pf2 mt-, and has been maintained with acetate medium in darkness since its isolation.
Spreitzer RJ, Chastain CJ (1987) Heteroplasmic suppression of an amber mutation in the Chlamydomonas chloroplast gene that encodes the large subunit of ribulosebisphosphate carboxylase/oxygenase. Curr Genet 11:611-616
Spreitzer RJ, Goldschmidt-Clermont M, Rahire M, Rochaix JD (1985) Nonsense mutations in the Chlamydomonas chloroplast gene that codes for the large subunit of ribulosebisphosphate carboxylase/oxygenase. Proc Natl Acad Sci USA 82:5460-5464
Spreitzer RJ, Ogren WL (1983) Rapid recovery of chloroplast mutations affecting ribulosebisphosphate carboxylase/oxygenase in Chlamydomonas reinhardtii. Proc Natl Acad Sci USA 80:6293-6297
Yu W, Spreitzer RJ (1992) Chloroplast heteroplasmicity is stabilized by an amber-suppressor tryptophan tRNA(CUA). Proc Natl Acad Sci USA 89:3904-3907
From Robert J. Spreitzer, University of Nebraska, July 2014
Phenotype: requires acetate, sensitive to light
The 28-7J chloroplast mutant was recovered by screening a collection of acetate-requiring mutants for lack of complementation with a known Rubisco rbcL mutant. The mutant was crossed with pf2 mt- to confirm uniparental inheritance, and this mt+ progeny clone was analyzed. Mutant 28-7J results from an R217S substitution (CGT-AGT) in the chloroplast-encoded large subunit of Rubisco, which blocks Rubisco holoenzyme assembly (Thow et al. 1994). Selection for photosynthesis-competent revertants yielded true revertants, intragenic suppressors (see R14-A), and heteroplasmic suppressors (Thow et al. 1994) that likely arise from heteroplasmic informational (tRNA) suppression (Yu and Spreitzer 1992). This strain has been maintained with acetate medium in darkness since its isolation.
Thow G, Zhu G, Spreitzer RJ (1994) Complementing substitutions within loop regions 2 and 3 of the alpha/beta-barrel active site influence the CO2/O2 specificity of chloroplast ribulose-1,5-bisphosphate carboxylase/oxygenase. Biochemistry 33:5109-5114
Yu W, Spreitzer RJ (1992) Chloroplast heteroplasmicity is stabilized by an amber-suppressor tryptophan tRNA(CUA). Proc Natl Acad Sci USA 89:3904-3907
From Robert J. Spreitzer, University of Nebraska, July 2014
Phenotype: requires acetate at 35 °C, temperature-conditional
R14-A was recovered as a photosynthesis-competent revertant of rbcL-R217S mt+ (28-7J). It results from an intragenic-suppressor mutation that causes an A242V substitution (GCT-GTT) in the Rubisco large subunit, and the double-mutant enzyme has decreases in Rubisco CO2/O2 specificity, holoenzyme stability, and large-subunit isoelectric point (Thow et al. 1994). The mutant can grow on minimal medium at 25 °C, but dies on minimal medium at 35 °C. This strain has been maintained with acetate medium in darkness since its isolation.
Thow G, Zhu G, Spreitzer RJ (1994) Complementing substitutions within loop regions 2 and 3 of the alpha/beta-barrel active site influence the CO2/O2 specificity of chloroplast ribulose-1,5-bisphosphate carboxylase/oxygenase. Biochemistry 33:5109-5114
From Robert J. Spreitzer, University of Nebraska, July 2014
Phenotype: requires acetate at 35 °C, temperature-conditional
R14-A was recovered as a photosynthesis-competent revertant of rbcL-R217S mt+ (28-7J). It results from an intragenic-suppressor mutation that causes an A242V substitution (GCT-GTT) in the Rubisco large subunit, and the double-mutant enzyme has decreases in Rubisco CO2/O2 specificity, holoenzyme stability, and large-subunit isoelectric point (Thow et al. 1994). The mutant can grow on minimal medium at 25 °C, but dies on minimal medium at 35 °C. This strain was recovered from a cross between rbcL-R217S/A242V mt+ and pf2 mt-. It has been maintained with acetate medium in darkness since its isolation.
Thow G, Zhu G, Spreitzer RJ (1994) Complementing substitutions within loop regions 2 and 3 of the alpha/beta-barrel active site influence the CO2/O2 specificity of chloroplast ribulose-1,5-bisphosphate carboxylase/oxygenase. Biochemistry 33:5109-5114
From Robert J. Spreitzer, University of Nebraska, July 2014
Using standard methods of directed mutagenesis and chloroplast-gene transformation of rbcL∆-25B1 mt+ (CC-4700) (Zhu and Spreitzer 1996), Genhai Zhu in Spreitzer’s group created an A242V substitution (GCT-GTT) in the Rubisco large subunit. This is the intragenic-suppressor substitution that complements the R217S substitution in photosynthesis-competent revertant R14-A (rbcL-R217S/A242V) (Thow et al. 1994). Preliminary analysis indicated that the A242V substitution has little or no effect on Rubisco catalysis or holoenzyme stability (Zhu and Spreitzer, unpublished). This strain has been maintained with acetate medium in darkness to prevent selection for secondary mutations that may improve Rubisco function or stability.
Thow G, Zhu G, Spreitzer RJ (1994) Complementing substitutions within loop regions 2 and 3 of the alpha/beta-barrel active site influence the CO2/O2 specificity of chloroplast ribulose-1,5-bisphosphate carboxylase/oxygenase. Biochemistry 33:5109-5114
Zhu G, Spreitzer RJ (1996) Directed mutagenesis of chloroplast ribulose-1,5-bisphosphate carboxylase/oxygenase: Loop-6 substitutions complement for structural stability but decrease catalytic efficiency. J Biol Chem 271:18494-18498
From Robert J. Spreitzer, University of Nebraska, July 2014
Phenotype: requires acetate, sensitive to light
The 31-4E chloroplast mutant was recovered by screening a collection of acetate-requiring mutants (generated with 5-fluorodeoxyuridine and methyl methanesulfonate) for lack of complementation with a known Rubisco rbcL mutant by standard methods (Spreitzer and Ogren 1983; Spreitzer et al. 1988). The mutant was crossed with pf2 mt- to confirm uniparental inheritance, and this mt+ progeny clone was analyzed. Mutant 31-4E results from a G54D substitution (GGT-GAT) in the chloroplast-encoded large subunit of Rubisco, which blocks Rubisco holoenzyme assembly (Spreitzer 1993). Selection for photosynthesis-competent revertants yielded true revertants and pseudorevertants (see R95-1C and R95-10A) (Spreitzer et al. 1995). This strain has been maintained with acetate medium in darkness since its isolation.
Spreitzer RJ (1993) Genetic dissection of Rubisco structure and function. Annu Rev Plant Physiol Plant Mol Biol 44:411-434
Spreitzer RJ, Al-Abed SR, Huether MJ (1988) Temperature-sensitive, photosynthesis-deficient mutants of Chlamydomonas reinhardtii. Plant Physiol 86:773-777
Spreitzer RJ, Ogren WL (1983) Rapid recovery of chloroplast mutations affecting ribulosebisphosphate carboxylase/oxygenase in Chlamydomonas reinhardtii. Proc Natl Acad Sci USA 80:6293-6297
Spreitzer RJ, Thow G, Zhu G (1995) Pseudoreversion substitution at large-subunit residue 54 influences the CO2/O2 specificity of chloroplast ribulosebisphosphate carboxylase/oxygenase. Plant Physiol 109:681-686
From Robert J. Spreitzer, University of Nebraska, July 2014
Phenotype: requires acetate, sensitive to light
The 31-4E chloroplast mutant was recovered by screening a collection of acetate-requiring mutants (generated with 5-fluorodeoxyuridine and methyl methanesulfonate) for lack of complementation with a known Rubisco rbcL mutant by standard methods (Spreitzer and Ogren 1983; Spreitzer et al. 1988). The mutant was crossed with pf2 mt- to confirm uniparental inheritance, and this pf2 mt- progeny clone was retained for future genetic analysis. Mutant 31-4E results from a G54D substitution (GGT-GAT) in the chloroplast-encoded large subunit of Rubisco, which blocks Rubisco holoenzyme assembly (Spreitzer 1993). Selection for photosynthesis-competent revertants yielded true revertants and pseudorevertants (see R95-1C and R95-10A) (Spreitzer et al. 1995). This strain has been maintained with acetate medium in darkness since its isolation.
Spreitzer RJ (1993) Genetic dissection of Rubisco structure and function. Annu Rev Plant Physiol Plant Mol Biol 44:411-434
Spreitzer RJ, Al-Abed SR, Huether MJ (1988) Temperature-sensitive, photosynthesis-deficient mutants of Chlamydomonas reinhardtii. Plant Physiol 86:773-777
Spreitzer RJ, Ogren WL (1983) Rapid recovery of chloroplast mutations affecting ribulosebisphosphate carboxylase/oxygenase in Chlamydomonas reinhardtii. Proc Natl Acad Sci USA 80:6293-6297
Spreitzer RJ, Thow G, Zhu G (1995) Pseudoreversion substitution at large-subunit residue 54 influences the CO2/O2 specificity of chloroplast ribulosebisphosphate carboxylase/oxygenase. Plant Physiol 109:681-686
From Robert J. Spreitzer, University of Nebraska, July 2014
R95-1C was recovered as a photosynthesis-competent revertant of rbcL-G54D mt+ (31-4E). It results from a pseudoreversion mutation that causes an D54V substitution (GAT-GTT), which results in a G54V substitution (GGT-GTT) in the Rubisco large subunit (Spreitzer et al. 1995). The G54V substitution causes a decrease in Rubisco CO2/O2 specificity and holoenzyme stability. This strain has been maintained with acetate medium in darkness since its isolation.
Spreitzer RJ, Thow G, Zhu G (1995) Pseudoreversion substitution at large-subunit residue 54 influences the CO2/O2 specificity of chloroplast ribulosebisphosphate carboxylase/oxygenase. Plant Physiol 109:681-686
From Robert J. Spreitzer, University of Nebraska, July 2014
R95-10A was recovered as a photosynthesis-competent revertant of rbcL-G54D mt+ (31-4E). It results from a pseudoreversion mutation that causes an D54A substitution (GAT-GCT), which results in a G54A substitution (GGT-GCT) in the Rubisco large subunit (Spreitzer et al. 1995). The G54A substitution causes a decrease in Rubisco holoenzyme stability. This strain has been maintained with acetate medium in darkness since its isolation.
Spreitzer RJ, Thow G, Zhu G (1995) Pseudoreversion substitution at large-subunit residue 54 influences the CO2/O2 specificity of chloroplast ribulosebisphosphate carboxylase/oxygenase. Plant Physiol 109:681-686
CC-4795 rbcL-M42V mt+
$30.00
$30.00
From Robert J. Spreitzer, University of Nebraska, July 2014
Directed mutagenesis and chloroplast transformation of rbcL-W66Amber mt+ (Spreitzer et al. 1985) were used to create an M42V substitution (ATG-GTA) in the Rubisco large subunit, which causes a small decrease in Rubisco carboxylase activity (Du et al. 2003). This is the original mutant strain. It was created to investigate phylogenetic differences near large-subunit residue Gly-54 (see rbcL-G54D) (Spreitzer et al. 1995). The strain 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, Goldschmidt-Clermont M, Rahire M, Rochaix JD (1985) Nonsense mutations in the Chlamydomonas chloroplast gene that codes for the large subunit of ribulosebisphosphate carboxylase/oxygenase. Proc Natl Acad Sci USA 82:5460-5464
Spreitzer RJ, Thow G, Zhu G (1995) Pseudoreversion substitution at large-subunit residue 54 influences the CO2/O2 specificity of chloroplast ribulosebisphosphate carboxylase/oxygenase. Plant Physiol 109:681-686
CC-4796 rbcL-C53A mt+
$30.00
$30.00
From Robert J. Spreitzer, University of Nebraska, July 2014
Directed mutagenesis and chloroplast transformation of rbcL-W66Amber mt+ (Spreitzer et al. 1985) were used to create a C53A substitution (TGT-GCT) in the Rubisco large subunit (Du et al. 2003). This is the original mutant strain. It was created to investigate phylogenetic differences near large-subunit residue Gly-54 (see rbcL-G54D) (Spreitzer et al. 1995). The strain 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, Goldschmidt-Clermont M, Rahire M, Rochaix JD (1985) Nonsense mutations in the Chlamydomonas chloroplast gene that codes for the large subunit of ribulosebisphosphate carboxylase/oxygenase. Proc Natl Acad Sci USA 82:5460-5464
Spreitzer RJ, Thow G, Zhu G (1995) Pseudoreversion substitution at large-subunit residue 54 influences the CO2/O2 specificity of chloroplast ribulosebisphosphate carboxylase/oxygenase. Plant Physiol 109:681-686
CC-4797 rbcL-M42V/C53A mt+
$30.00
$30.00
From Robert J. Spreitzer, University of Nebraska, July 2014
Directed mutagenesis and chloroplast transformation of rbcL-W66Amber mt+ (Spreitzer et al. 1985) were used to create M42V (ATG-GTA) and C53A (TGT-GCT) substitutions in the Rubisco large subunit, which cause a decrease in Rubisco CO2/O2 specificity (Du et al. 2003). This is the original double-mutant strain. It was created to investigate phylogenetic differences near large-subunit residue Gly-54 (see rbcL-G54D) (Spreitzer et al. 1995). The strain 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, Goldschmidt-Clermont M, Rahire M, Rochaix JD (1985) Nonsense mutations in the Chlamydomonas chloroplast gene that codes for the large subunit of ribulosebisphosphate carboxylase/oxygenase. Proc Natl Acad Sci USA 82:5460-5464
Spreitzer RJ, Thow G, Zhu G (1995) Pseudoreversion substitution at large-subunit residue 54 influences the CO2/O2 specificity of chloroplast ribulosebisphosphate carboxylase/oxygenase. Plant Physiol 109:681-686
CC-4798 rbcL-A99C mt+
$30.00
$30.00
From Robert J. Spreitzer, University of Nebraska, July 2014
Directed mutagenesis and chloroplast transformation of rbcL∆-25B1 mt+ (CC-4700) were used to create an A99C substitution in the Rubisco large subunit. This mutant was created to investigate phylogenetic differences near large-subunit residue Gly-54 (see rbcL-G54D) (Spreitzer et al. 1995; Du et al. 2003). The strain has been maintained with acetate medium in darkness to prevent selection for secondary mutations that may improve Rubisco function.
William Zerges reported CC-4798 should have A99C but it is wild type, at least in the 5 portions where he sequenced, including that position. (personal communication, 12/8/20)
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, Thow G, Zhu G (1995) Pseudoreversion substitution at large-subunit residue 54 influences the CO2/O2 specificity of chloroplast ribulosebisphosphate carboxylase/oxygenase. Plant Physiol 109:681-686
CC-4799 rbcL-C53A/A99C mt+
$30.00
$30.00
From Robert J. Spreitzer, University of Nebraska, July 2014
Directed mutagenesis and chloroplast transformation of rbcL∆-25B1 mt+ (CC-4700) were used to create C53A and A99C substitutions in the Rubisco large subunit. This double mutant was created to investigate phylogenetic differences near large-subunit residue Gly-54 (see rbcL-G54D) (Spreitzer et al. 1995; Du et al. 2003). The strain 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, Thow G, Zhu G (1995) Pseudoreversion substitution at large-subunit residue 54 influences the CO2/O2 specificity of chloroplast ribulosebisphosphate carboxylase/oxygenase. Plant Physiol 109:681-686
From Robert J. Spreitzer, University of Nebraska, July 2014
Phenotype: requires acetate, sensitive to light
The 45-3B chloroplast mutant was recovered by screening a collection of acetate-requiring mutants for lack of complementation with a known Rubisco rbcL mutant (Spreitzer and Ogren 1983; Spreitzer et al. 1988). The mutant was crossed with pf2 mt- to confirm uniparental inheritance, and this mt+ progeny clone was analyzed. Mutant 45-3B results from a V331A substitution (GTT-GCT) in the chloroplast-encoded large subunit of Rubisco, which causes decreases in Rubisco CO2/O2 specificity and carboxylation catalytic efficiency (Chen and Spreitzer 1989). The V331A mutant-enzyme x-ray crystal structure has been solved (Karkehabadi et al. 2007). Selection for photosynthesis-competent revertants yielded true revertants and intragenic suppressors (see R40-9D and R61-2J) (Chen and Spreitzer 1989; Chen et al. 1991). Other types of revertants have been recovered (see R236-2A, R255-9A, and R258-3B) (Satagopan and Spreitzer, unpublished). This strain has been maintained with acetate medium in darkness since its isolation.
Chen Z, Spreitzer RJ (1989) Chloroplast intragenic suppression enhances the low CO2/O2 specificity of mutant ribulosebisphosphate carboxylase/oxygenase. J Biol Chem 264:3051-3053
Chen Z, Yu W, Lee JH, Diao R, Spreitzer RJ (1991) Complementing amino-acid substitutions within loop 6 of the alpha/beta-barrel active site influence the CO2/O2 specificity of chloroplast ribulose-1,5-bisphosphate carboxylase/oxygenase. Biochemistry 30:8846-8850
Karkehabadi S, Satagopan S, Taylor TC, Spreitzer RJ, Andersson I (2007) Structural analysis of altered large-subunit loop-6/carboxy-terminus interactions that influence catalytic efficiency and CO2/O2 specificity of ribulose-1,5-bisphosphate carboxylase/oxygenase. Biochemistry 46:11080-11089
Spreitzer RJ, Al-Abed SR, Huether MJ (1988) Temperature-sensitive, photosynthesis-deficient mutants of Chlamydomonas reinhardtii. Plant Physiol 86:773-777
Spreitzer RJ, Ogren WL (1983) Rapid recovery of chloroplast mutations affecting ribulosebisphosphate carboxylase/oxygenase in Chlamydomonas reinhardtii. Proc Natl Acad Sci USA 80:6293-6297
From Robert J. Spreitzer, University of Nebraska, July 2014
R40-9D was recovered as a photosynthesis-competent revertant of rbcL-V331A mt+ (45-3B) (Chen and Spreitzer 1989). It results from an intragenic-suppressor mutation that causes a T342I substitution (ACT-ATT) in the Rubisco large subunit, and the double-mutant enzyme has decreases in Rubisco CO2/O2 specificity and holoenzyme stability (Chen and Spreitzer 1989; Chen et al. 1991). The V331A/T342I mutant-enzyme x-ray crystal structure has been solved (Karkehabadi et al. 2007). The strain has been maintained with acetate medium in darkness to prevent selection for secondary mutations that may improve Rubisco function.
Chen Z, Spreitzer RJ (1989) Chloroplast intragenic suppression enhances the low CO2/O2 specificity of mutant ribulosebisphosphate carboxylase/oxygenase. J Biol Chem 264:3051-3053
Chen Z, Yu W, Lee JH, Diao R, Spreitzer RJ (1991) Complementing amino-acid substitutions within loop 6 of the alpha/beta-barrel active site influence the CO2/O2 specificity of chloroplast ribulose-1,5-bisphosphate carboxylase/oxygenase. Biochemistry 30:8846-8850
Karkehabadi S, Satagopan S, Taylor TC, Spreitzer RJ, Andersson I (2007) Structural analysis of altered large-subunit loop-6/carboxy-terminus interactions that influence catalytic efficiency and CO2/O2 specificity of ribulose-1,5-bisphosphate carboxylase/oxygenase. Biochemistry 46:11080-11089
From Robert J. Spreitzer, University of Nebraska, July 2014
R61-2J was recovered as a photosynthesis-competent revertant of rbcL-V331A mt+ (45-3B). It results from an intragenic-suppressor mutation that causes a G344S substitution (GGT-AGT) in the Rubisco large subunit, and the double-mutant enzyme has decreased Rubisco CO2/O2 specificity (Chen et al. 1991). The V331A/G344S mutant-enzyme x-ray crystal structure has been solved (Karkehabadi et al. 2007). The strain has been maintained with acetate medium in darkness to prevent selection for secondary mutations that may improve Rubisco function.
Chen Z, Spreitzer RJ (1989) Chloroplast intragenic suppression enhances the low CO2/O2 specificity of mutant ribulosebisphosphate carboxylase/oxygenase. J Biol Chem 264:3051-3053
Chen Z, Yu W, Lee JH, Diao R, Spreitzer RJ (1991) Complementing amino-acid substitutions within loop 6 of the alpha/beta-barrel active site influence the CO2/O2 specificity of chloroplast ribulose-1,5-bisphosphate carboxylase/oxygenase. Biochemistry 30:8846-8850
Karkehabadi S, Satagopan S, Taylor TC, Spreitzer RJ, Andersson I (2007) Structural analysis of altered large-subunit loop-6/carboxy-terminus interactions that influence catalytic efficiency and CO2/O2 specificity of ribulose-1,5-bisphosphate carboxylase/oxygenase. Biochemistry 46:11080-11089
CC-4803 rbcL-V331A/G344S mt+ (R61-2J revertant of 45-3B) (non-pf2 progeny used for genetic analysis)
$30.00
$30.00
From Robert J. Spreitzer, University of Nebraska, July 2014
R61-2J was recovered as a photosynthesis-competent revertant of rbcL-V331A mt+ (45-3B). It results from an intragenic-suppressor mutation that causes a G344S substitution (GGT-AGT) in the Rubisco large subunit, and the double-mutant enzyme has decreased Rubisco CO2/O2 specificity (Chen et al. 1991). The V331A/G344S mutant-enzyme x-ray crystal structure has been solved (Karkehabadi et al. 2007). This strain was recovered from a cross between rbcL-V331A/G344S mt + and pf2 mt-, and has been maintained with acetate medium in darkness to prevent selection for secondary mutations that may improve Rubisco function.
Chen Z, Spreitzer RJ (1989) Chloroplast intragenic suppression enhances the low CO2/O2 specificity of mutant ribulosebisphosphate carboxylase/oxygenase. J Biol Chem 264:3051-3053
Chen Z, Yu W, Lee JH, Diao R, Spreitzer RJ (1991) Complementing amino-acid substitutions within loop 6 of the alpha/beta-barrel active site influence the CO2/O2 specificity of chloroplast ribulose-1,5-bisphosphate carboxylase/oxygenase. Biochemistry 30:8846-8850
Karkehabadi S, Satagopan S, Taylor TC, Spreitzer RJ, Andersson I (2007) Structural analysis of altered large-subunit loop-6/carboxy-terminus interactions that influence catalytic efficiency and CO2/O2 specificity of ribulose-1,5-bisphosphate carboxylase/oxygenase. Biochemistry 46:11080-11089
CC-4804 rbcL-V331A/G344S mt- (R61-2J revertant of 45-3B) (non-pf2 progeny used for genetic analysis)
$30.00
$30.00
From Robert J. Spreitzer, University of Nebraska, July 2014
R61-2J was recovered as a photosynthesis-competent revertant of rbcL-V331A mt+ (45-3B). It results from an intragenic-suppressor mutation that causes a G344S substitution (GGT-AGT) in the Rubisco large subunit, and the double-mutant enzyme has decreased Rubisco CO2/O2 specificity (Chen et al. 1991). The V331A/G344S mutant-enzyme x-ray crystal structure has been solved (Karkehabadi et al. 2007). This strain was recovered from a cross between rbcL-V331A/G344S mt + and pf2 mt-, and has been maintained with acetate medium in darkness to prevent selection for secondary mutations that may improve Rubisco function.
Chen Z, Spreitzer RJ (1989) Chloroplast intragenic suppression enhances the low CO2/O2 specificity of mutant ribulosebisphosphate carboxylase/oxygenase. J Biol Chem 264:3051-3053
Chen Z, Yu W, Lee JH, Diao R, Spreitzer RJ (1991) Complementing amino-acid substitutions within loop 6 of the alpha/beta-barrel active site influence the CO2/O2 specificity of chloroplast ribulose-1,5-bisphosphate carboxylase/oxygenase. Biochemistry 30:8846-8850
Karkehabadi S, Satagopan S, Taylor TC, Spreitzer RJ, Andersson I (2007) Structural analysis of altered large-subunit loop-6/carboxy-terminus interactions that influence catalytic efficiency and CO2/O2 specificity of ribulose-1,5-bisphosphate carboxylase/oxygenase. Biochemistry 46:11080-11089
From Robert J. Spreitzer, University of Nebraska, July 2014
Using standard methods of directed mutagenesis and chloroplast-gene transformation of rbcL∆-MX3312 mt+ (CC-4696), a T342I substitution (ACT-ATT) was created in the Rubisco large subunit (Karkehabadi et al. 2007). This is the intragenic-suppressor substitution that complements the V331A substitution in photosynthesis-competent revertant R40-9D (rbcL-V331A/T342I) (Chen and Spreitzer 1989; Chen et al. 1991). The T342I substitution alone decreases the CO2/O2 specificity of Rubisco, and the x-ray crystal structure of the T342I mutant Rubisco has been solved (Karkehabadi et al. 2007). This strain has been maintained with acetate medium in darkness to prevent selection for secondary mutations that may improve Rubisco function.
Chen Z, Spreitzer RJ (1989) Chloroplast intragenic suppression enhances the low CO2/O2 specificity of mutant ribulosebisphosphate carboxylase/oxygenase. J Biol Chem 264:3051-3053
Chen Z, Yu W, Lee JH, Diao R, Spreitzer RJ (1991) Complementing amino-acid substitutions within loop 6 of the alpha/beta-barrel active site influence the CO2/O2 specificity of chloroplast ribulose-1,5-bisphosphate carboxylase/oxygenase. Biochemistry 30:8846-8850
Karkehabadi S, Satagopan S, Taylor TC, Spreitzer RJ, Andersson I (2007) Structural analysis of altered large-subunit loop-6/carboxy-terminus interactions that influence catalytic efficiency and CO2/O2 specificity of ribulose-1,5-bisphosphate carboxylase/oxygenase. Biochemistry 46:11080-11089
From Robert J. Spreitzer, University of Nebraska, July 2014
Using standard methods of directed mutagenesis and chloroplast-gene transformation of rbcL∆-MX3312 mt+ (CC-4696), a G344S substitution (GGT-TCT) was created in the Rubisco large subunit (Karkehabadi et al. 2007). This is the intragenic-suppressor substitution that complements the V331A substitution in photosynthesis-competent revertant R61-2J (rbcL-V331A/G344S) (Chen et al. 1991). The G344S substitution alone causes a small decrease in the CO2/O2 specificity of Rubisco (Karkehabadi et al. 2007). This strain has been maintained with acetate medium in darkness to prevent selection for secondary mutations that may improve Rubisco function.
Chen Z, Yu W, Lee JH, Diao R, Spreitzer RJ (1991) Complementing amino-acid substitutions within loop 6 of the alpha/beta-barrel active site influence the CO2/O2 specificity of chloroplast ribulose-1,5-bisphosphate carboxylase/oxygenase. Biochemistry 30:8846-8850
Karkehabadi S, Satagopan S, Taylor TC, Spreitzer RJ, Andersson I (2007) Structural analysis of altered large-subunit loop-6/carboxy-terminus interactions that influence catalytic efficiency and CO2/O2 specificity of ribulose-1,5-bisphosphate carboxylase/oxygenase. Biochemistry 46:11080-11089
From Robert J. Spreitzer, University of Nebraska, July 2014
R236-2A was recovered as a photosynthesis-competent revertant after MMS mutagenesis of rbcL-V331A mt+ (45-3B) (Chen and Spreitzer 1989; Chen et al. 1991). It results from pseudoreversion that causes an A331T substitution in the Rubisco large subunit, which decreases Rubisco CO2/O2 specificity (Satagopan and Spreitzer, unpublished). The strain has been maintained with acetate medium in darkness to prevent selection for secondary mutations that may improve Rubisco function.
Chen Z, Spreitzer RJ (1989) Chloroplast intragenic suppression enhances the low CO2/O2 specificity of mutant ribulosebisphosphate carboxylase/oxygenase. J Biol Chem 264:3051-3053
Chen Z, Yu W, Lee JH, Diao R, Spreitzer RJ (1991) Complementing amino-acid substitutions within loop 6 of the alpha/beta-barrel active site influence the CO2/O2 specificity of chloroplast ribulose-1,5-bisphosphate carboxylase/oxygenase. Biochemistry 30:8846-8850
From Robert J. Spreitzer, University of Nebraska, July 2014
R255-9A was recovered as a photosynthesis-competent revertant of rbcL-V331A mt+ (45-3B) (Chen and Spreitzer 1989; Chen et al. 1991). It results from pseudoreversion that causes an A331S substitution in the Rubisco large subunit, which decreases Rubisco CO2/O2 specificity (Satagopan and Spreitzer, unpublished). The strain has been maintained with acetate medium in darkness to prevent selection for secondary mutations that may improve Rubisco function.
Chen Z, Spreitzer RJ (1989) Chloroplast intragenic suppression enhances the low CO2/O2 specificity of mutant ribulosebisphosphate carboxylase/oxygenase. J Biol Chem 264:3051-3053
Chen Z, Yu W, Lee JH, Diao R, Spreitzer RJ (1991) Complementing amino-acid substitutions within loop 6 of the alpha/beta-barrel active site influence the CO2/O2 specificity of chloroplast ribulose-1,5-bisphosphate carboxylase/oxygenase. Biochemistry 30:8846-8850
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