Different properties of gene products of three sets ribulose 1,5-bisphosphate carboxylase/oxygenase from a marine obligately autotrophic hydrogen-oxidizing bacterium, Hydrogenovibrio marinus strain MH-110

被引:23
作者
Hayashi, NR
Oguni, A
Yaguchi, T
Chung, SY
Nishihara, H
Kodama, T
Igarashi, Y
机构
[1] Suntory Ltd, Inst Fundamental Res, Shimamoto, Osaka 618, Japan
[2] Ibaraki Univ, Dept Appl Biol Resource Sci, Ami, Ibaraki 30003, Japan
[3] Shinshu Univ, Fac Text Sci & Technol, Ueda, Nagano 386, Japan
[4] Univ Tokyo, Dept Biotechnol, Bunkyo Ku, Tokyo 113, Japan
来源
JOURNAL OF FERMENTATION AND BIOENGINEERING | 1998年 / 85卷 / 02期
基金
日本学术振兴会;
关键词
RubisCO; Hydrogenovibrio;
D O I
10.1016/S0922-338X(97)86759-1
中图分类号
Q81 [生物工程学(生物技术)]; Q93 [微生物学];
学科分类号
071005 ; 0836 ; 090102 ; 100705 ;
摘要
Hydrogenovibrio marinas strain MH-110 is an obligately lithoautotrophic hydrogen-oxidizing bacterium, possessing three sets of the genes for ribulose 1,5-bisphosphate carboxylase/oxygenase (RubisCO); one form II type (L-x) and two form I type (L8S8) enzymes. The genes for the form I type enzymes are named cbbLS-1 and cbbLS-2, and that for the form II type enzyme is named cbbM. These three sets of genes were cloned in plasmid vectors, and the expression of the genes in E. coli cells were studied. The three RubisCOs were purified through the same steps, and their specificity factors (tau values) were measured. The tau values of CbbLS-1 and CbbLS-2 were higher than that of CbbM, but lower than those of other form I RubisCOs. The specific activity of CbbM was very low and CbbM was inactivated easily during the process of purification. Immunochemical analyses revealed that the antibody against form I type reacted only with CbbL-1 and CbbL-2, and the antibody against form II type reacted only with CbbM. The antibody to neither form of RubisCO demonstrated cross-reactivity for the other form.
引用
收藏
页码:150 / 155
页数:6
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