TY - JOUR
T1 - Molecular cloning and expression of Thiobacillus ferrooxidans chromosomal ribulose bisphosphate carboxylase genes in Escherichia coli
AU - Kusano, Tomonobu
AU - Sugawara, Kazuyuki
AU - Inoue, Chihiro
AU - Suzuki, Nobuhiro
PY - 1991/1
Y1 - 1991/1
N2 - The genes coding for d-ribulose-1,5-bisphosphate carboxylase (RuBPCase) from an iron-oxidizing bacterium, Thiobacillus ferrooxidans, were cloned into an Escherichia coli plasmid, pUC18. The recombinant plasmid, termed pTR11, contained a 4.0-kb PstI fragment including the entire coding regions for both large and small subunits of RuBPCase. Escherichia coli carrying pTR11 did not show any CO2-fixing activity. However, a derivative plasmid with an appropriate deletion, which was placed under the control of a tac promoter, conferred ribulose bisphosphate-dependent CO2-fixing activity on the host cell. Analysis of gel-filtration chromatography of the RuBPCase synthesized in E. coli revealed that it had a hexadecameric form like the native enzyme of T. ferrooxidans.
AB - The genes coding for d-ribulose-1,5-bisphosphate carboxylase (RuBPCase) from an iron-oxidizing bacterium, Thiobacillus ferrooxidans, were cloned into an Escherichia coli plasmid, pUC18. The recombinant plasmid, termed pTR11, contained a 4.0-kb PstI fragment including the entire coding regions for both large and small subunits of RuBPCase. Escherichia coli carrying pTR11 did not show any CO2-fixing activity. However, a derivative plasmid with an appropriate deletion, which was placed under the control of a tac promoter, conferred ribulose bisphosphate-dependent CO2-fixing activity on the host cell. Analysis of gel-filtration chromatography of the RuBPCase synthesized in E. coli revealed that it had a hexadecameric form like the native enzyme of T. ferrooxidans.
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U2 - 10.1007/BF02106210
DO - 10.1007/BF02106210
M3 - Article
AN - SCOPUS:0025972919
SN - 0343-8651
VL - 22
SP - 35
EP - 41
JO - Current Microbiology
JF - Current Microbiology
IS - 1
ER -