Abstract
Ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco) and a 66-kD protein were co-purified from solubilized microsomal preparations of the green alga Botryococcus braunii by Green A agarose, sucrose density gradient, MonoQ, and gel filtration. The 66-kD protein remained intact after 6 M urea treatment and sodium dodecyl sulfate-polyacrylamide gel electrophoresis. It could be detected in the soluble fraction of the cell-free extract but appeared to be more abundant in the microsomal preparations. It cross-reacted with antibodies raised against Rubisco holoenzyme, large and small subunits, indicating that the 66-kD protein contains both the large and the small subunits of Rubisco. The N-terminal amino acid sequence of this protein and that of a proteolytic fragment showed high homology with the mature Rubisco small subunits, and the sequence of another proteolytic fragment showed high homology with that of the Rubisco large subunit. It is concluded that the 66-kD protein is produced by cross-linking of large and small sub-units of Rubisco in the cell.
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- Dennis M., Kolattukudy P. E. A cobalt-porphyrin enzyme converts a fatty aldehyde to a hydrocarbon and CO. Proc Natl Acad Sci U S A. 1992 Jun 15;89(12):5306–5310. doi: 10.1073/pnas.89.12.5306. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Hwang S. R., Tabita F. R. Cloning and expression of the chloroplast-encoded rbcL and rbcS genes from the marine diatom Cylindrotheca sp. strain N1. Plant Mol Biol. 1989 Jul;13(1):69–79. doi: 10.1007/BF00027336. [DOI] [PubMed] [Google Scholar]
- Hwang S. R., Tabita F. R. Cotranscription, deduced primary structure, and expression of the chloroplast-encoded rbcL and rbcS genes of the marine diatom Cylindrotheca sp. strain N1. J Biol Chem. 1991 Apr 5;266(10):6271–6279. [PubMed] [Google Scholar]
- Towbin H., Staehelin T., Gordon J. Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications. Proc Natl Acad Sci U S A. 1979 Sep;76(9):4350–4354. doi: 10.1073/pnas.76.9.4350. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Valentin K., Zetsche K. The genes of both subunits of ribulose-1,5-bisphosphate carboxylase constitute an operon on the plastome of a red alga. Curr Genet. 1989 Sep;16(3):203–209. doi: 10.1007/BF00391478. [DOI] [PubMed] [Google Scholar]
- 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]
- Wilson M. I., Ghosh S., Gerhardt K. E., Holland N., Babu T. S., Edelman M., Dumbroff E. B., Greenberg B. M. In Vivo Photomodification of Ribulose-1,5-Bisphosphate Carboxylase/Oxygenase Holoenzyme by Ultraviolet-B Radiation (Formation of a 66-Kilodalton Variant of the Large Subunit). Plant Physiol. 1995 Sep;109(1):221–229. doi: 10.1104/pp.109.1.221. [DOI] [PMC free article] [PubMed] [Google Scholar]