Skip to main content
PMC home page
Journal of Bacteriology logoLink to Journal of Bacteriology
. 1977 Dec;132(3):818–823. doi: 10.1128/jb.132.3.818-823.1977

Isolation and preliminary characterization of two forms of ribulose 1,5-bisphosphate carboxylase from Rhodopseudomonas capsulata.

J L Gibson, F R Tabita
PMCID: PMC235583  PMID: 21872

Abstract

The presence of two distinct forms of ribulose 1,5-bisphosphate carboxylase has been demonstrated in extracts of Rhodopseudomonas capsulata, similar to the form I (peak I) and form II (peak II) carboxylases previously described from R. sphaeroides (J. Gibson and F. R. Tabita, J. Biol. Chem 252:943-949, 1977). The two activities, separated by diethylaminoethyl-cellulose chromatography, were shown to be of different molecular size after assay on polyacrylamide gels. The higher-molecular-weight carboxylase from R. capsulata was designated form I-C, whereas the smaller enzyme was designated form II-C. Catalytic studies revealed significant differences between the two enzymes in response to pH and the effector 6-phosphogluconate. Immunological studies with antisera directed against the carboxylases from R. sphaeroides demonstrated antigenic differences between the two R. capsulata enzymes; cross-reactivity was observed only between R. sphaeroides anti-form II serum and the corresponding R. capsulata enzyme, form II-C.

Full text

PDF
818

Images in this article

821Image
on p.821

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Bowien B., Mayer F., Codd G. A., Schlegel H. G. Purification, some properties and quaternary structure of the D-ribulose 1,5-diphosphate carboxylase of Alcaligenes eutrophus. Arch Microbiol. 1976 Nov 2;110(23):157–166. doi: 10.1007/BF00690223. [DOI] [PubMed] [Google Scholar]
  2. Chu D. K., Bassham J. A. Activation and inhibition of ribulose 1,5-diphosphate carboxylase by 6-phosphogluconate. Plant Physiol. 1973 Oct;52(4):373–379. doi: 10.1104/pp.52.4.373. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Chu D. K., Bassham J. A. Inhibition of ribulose 1,5-diphosphate carboxylase by 6-phosphogluconate. Plant Physiol. 1972 Aug;50(2):224–227. doi: 10.1104/pp.50.2.224. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Gibson J. L., Tabita F. R. Characterization of antiserum directed against form II ribulose 1,5-bisphosphate carboxylase from Rhodopseudomonas sphaeroides. J Bacteriol. 1977 Sep;131(3):1020–1022. doi: 10.1128/jb.131.3.1020-1022.1977. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Gibson J. L., Tabita F. R. Different molecular forms of D-ribulose-1,5-bisphosphate carboxylase from Rhodopseudomonas sphaeroides. J Biol Chem. 1977 Feb 10;252(3):943–949. [PubMed] [Google Scholar]
  6. LOWRY O. H., ROSEBROUGH N. J., FARR A. L., RANDALL R. J. Protein measurement with the Folin phenol reagent. J Biol Chem. 1951 Nov;193(1):265–275. [PubMed] [Google Scholar]
  7. Marrs B. Genetic recombination in Rhodopseudomonas capsulata. Proc Natl Acad Sci U S A. 1974 Mar;71(3):971–973. doi: 10.1073/pnas.71.3.971. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. McFadden B. A. Autotrophic CO2 assimilation and the evolution of ribulose diphosphate carboxylase. Bacteriol Rev. 1973 Sep;37(3):289–319. doi: 10.1128/br.37.3.289-319.1973. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. McFadden B. A., Denend A. R. Ribulose diphosphate carboxylase from autotrophic microorganisms. J Bacteriol. 1972 May;110(2):633–642. doi: 10.1128/jb.110.2.633-642.1972. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. McFadden B. A., Tabita F. R. D-ribulose-1, 5-diphosphate carboxylase and the evolution of autotrophy. Biosystems. 1974 Oct;6(2):93–112. doi: 10.1016/0303-2647(74)90002-1. [DOI] [PubMed] [Google Scholar]
  11. McFadden B. A., Tabita F. R., Kuehn G. D. Ribulose-diphosphate carboxylase from the hydrogen bacteria and Rhodospirillum rubrum. Methods Enzymol. 1975;42:461–472. doi: 10.1016/0076-6879(75)42152-8. [DOI] [PubMed] [Google Scholar]
  12. ORMEROD J. G., ORMEROD K. S., GEST H. Light-dependent utilization of organic compounds and photoproduction of molecular hydrogen by photosynthetic bacteria; relationships with nitrogen metabolism. Arch Biochem Biophys. 1961 Sep;94:449–463. doi: 10.1016/0003-9861(61)90073-x. [DOI] [PubMed] [Google Scholar]
  13. Orr M. D., Blakley R. L., Panagou D. Discontinuous buffer systems for analytical and preparative electrophoresis of enzymes on polyacrylamide gel. Anal Biochem. 1972 Jan;45(1):68–85. doi: 10.1016/0003-2697(72)90008-5. [DOI] [PubMed] [Google Scholar]
  14. Purohit K., McFadden B. A., Cohen A. L. Purification, quaternary structure, composition, and properties of D-ribulose-1,5-bisphosphate carboxylase from Thiobacillus intermedius. J Bacteriol. 1976 Jul;127(1):505–515. doi: 10.1128/jb.127.1.505-515.1976. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. Purohit K., McFadden B. A. Quaternary structure and oxygenase activity of D-ribulose-1,5-bisphosphate carboxylase from Hydrogenomonas eutropha. J Bacteriol. 1977 Jan;129(1):415–421. doi: 10.1128/jb.129.1.415-421.1977. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. Spomer G. G. Molecular diversity of the ribulose-1,5-diphosphate carboxylase from photosynthetic microorganisms. Science. 1968 Aug 2;161(3840):482–485. [PubMed] [Google Scholar]
  17. Tabita F. R., McFadden B. A. D-ribulose 1,5-diphosphate carboxylase from Rhodospirillum rubrum. I. Levels, purification, and effects of metallic ions. J Biol Chem. 1974 Jun 10;249(11):3453–3458. [PubMed] [Google Scholar]
  18. Tabita F. R., McFadden B. A. D-ribulose 1,5-diphosphate carboxylase from Rhodospirillum rubrum. II. Quaternary structure, composition, catalytic, and immunological properties. J Biol Chem. 1974 Jun 10;249(11):3459–3464. [PubMed] [Google Scholar]
  19. Tabita F. R., McFadden B. A. Molecular and catalytic properties of ribulose 1,5-bisphosphate carboxylase from the photosynthetic extreme halophile Ectothiorhodospira halophila. J Bacteriol. 1976 Jun;126(3):1271–1277. doi: 10.1128/jb.126.3.1271-1277.1976. [DOI] [PMC free article] [PubMed] [Google Scholar]
  20. Tabita F. R., McFadden B. A., Pfennig N. D-ribulose-1,5-bisphosphate carboxylase in Chlorobium thiosulfatophilum Tassajara. Biochim Biophys Acta. 1974 Mar 21;341(1):187–194. doi: 10.1016/0005-2744(74)90079-5. [DOI] [PubMed] [Google Scholar]
  21. Tabita F. R., McFadden B. A. Regulation of ribulose-1,5-diphosphate carboxylase by 6-phospho-D-gluconate. Biochem Biophys Res Commun. 1972 Sep 5;48(5):1153–1159. doi: 10.1016/0006-291x(72)90831-5. [DOI] [PubMed] [Google Scholar]
  22. Tabita F. R., Stevens S. E., Jr, Gibson J. L. Carbon dioxide assimilation in blue-green algae: initial studies on the structure of ribulose 1,5-bisphosphate carboxylase. J Bacteriol. 1976 Feb;125(2):531–539. doi: 10.1128/jb.125.2.531-539.1976. [DOI] [PMC free article] [PubMed] [Google Scholar]
  23. Tabita R. F., Stevens S. E., Jr, Quijano R. D-ribulose 1, 5-diphosphate carboxylase from blue-green algae. Biochem Biophys Res Commun. 1974 Nov 6;61(1):45–52. doi: 10.1016/0006-291x(74)90531-2. [DOI] [PubMed] [Google Scholar]
  24. Takabe T., Akazawa T. Catalytic role of subunit A in ribulose-1,5-diphosphate carboxylase from Chromatium strain D. Arch Biochem Biophys. 1973 Jul;157(1):303–308. doi: 10.1016/0003-9861(73)90415-3. [DOI] [PubMed] [Google Scholar]
  25. Takabe T., Nishimura M., Akazawa T. Presence of two subunit types in ribulose-1,5-bisphosphate carboxylase from blue-green algae. Biochem Biophys Res Commun. 1976 Jan 26;68(2):537–544. doi: 10.1016/0006-291x(76)91179-7. [DOI] [PubMed] [Google Scholar]
  26. Wall J. D., Weaver P. F., Gest H. Genetic transfer of nitrogenase-hydrogenase activity in Rhodopseudomonas capsulata. Nature. 1975 Dec 18;258(5536):630–631. doi: 10.1038/258630a0. [DOI] [PubMed] [Google Scholar]
  27. Whitman W., Tabita F. R. Inhibition of D-ribulose 1,5-bisphosphate carboxylase by pyridoxal 5'-phosphate. Biochem Biophys Res Commun. 1976 Aug 23;71(4):1034–1039. doi: 10.1016/0006-291x(76)90758-0. [DOI] [PubMed] [Google Scholar]

Articles from Journal of Bacteriology are provided here courtesy of American Society for Microbiology (ASM)

RESOURCES