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

• Published in: Journal of fermentation and bioengineering 1998-01, Vol.85 (2), p.150-155
• Main Authors: Hayashi, Nobuhiro R., Oguni, Asako, Yaguchi, Toshiaki, Chung, Seong-Yong, Nishihara, Hirofumi, Kodama, Tohru, Igarashi, Yasuo
• Format: Article
• Language: English
• Subjects: Biological and medical sciences; BIOLOGICAL PROPERTIES; Biology of microorganisms of confirmed or potential industrial interest; Biotechnology; Fundamental and applied biological sciences. Psychology; GENE; GENES; Hydrogenovibrio; Hydrogenovibrio marinus; Miscellaneous; Mission oriented research; PROPIEDADES BIOLOGICAS; PROPRIETE BIOLOGIQUE; RUBISCO; VIBRIO
• ISSN: 0922-338X
• DOI: 10.1016/S0922-338X(97)86759-1

Hydrogenovibrio marinus 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 (L 8S 8) 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 (τ values) were measured. The τ 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.