Abstract
Rhodopseudomonas capsulata produces both an intermediate (I) and a large (L) form of ribulose-1,5-bisphosphate carboxylase/oxygenase. Both forms are derepressed under CO2-limiting conditions. The L-form of the enzyme is completely repressed when the culture is grown either photoautotrophically or photoheterotrophically with malate as the electron donor. The L-form is derepressed in the late logarithmic phase of growth when cells are grown photoheterotrophically with butyrate as the electron donor and the NaHCO3 supplement is 0.01%. The level of the I-form is increased about fivefold under latter growth conditions when compared to malate-grown cells. Analytical ultracentrifugation revealed the molecular masses of the I-and L-forms to be 300,000 and 542,000, respectively. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis showed the I-form to be composed of only one type subunit with a molecular weight of 64,000. The L-form possessed both large and small subunits with molecular weights of 58,000 and 10,000.
Similar content being viewed by others
References
Anderson LE, Price GB, Fuller RC (1968) Molecular diversity of the ribulose-1,5-diphosphate carboxylase from photosynthetic microorganisms. Science 161:482–484
Berhow MA, Saluja, McFadden BA (1982) Rapid purification of D-ribulose-1,5-bisphosphate carboxylase by vertical sedimentation in a reoriented gradient. Plauf Sci Lett 27:51–57
Beudeker RF, Cannon GC, Kuenen JG, Shively JM (1980) Relations between D-ribulose-1,5-bisphosphate carboxylase, carboxysomes and CO2 fixing capacity in the obligate chemolithotroph Thiobacillus neapolitanus grown under different limitations in the chemostat. Arch Microbiol 124:185–189
Dijkuizen L, Harder W (1979) Regulation of autotrophic and heterotrophic metabolism in Pseudomonas oxalaticus oxl: growth on mixtures of oxalate and formate in continuous culture. Arch Microbiol 123:55–63
Friedrich CG (1982) Derepression of hydrogenase during limitation of electron donors and derepression of ribulose bisphosphate carboxylase during carbon limitation of Alkaligenes eutrophus. J Bacteriol 149:203–210
Gibson JL, Tabita FR (1977a) Different molecular forms of D-ribulose-1,5-bisphosphate carboxylase from Rhodopseudomonas sphaeroides. J Biol Chem 252:943–949
Gibson JL, Tabita FR (1977b) Isolation and preliminary characterization of two forms of ribulose-1,5-bisphosphate carboxylase from Rhodopseudomonas capsulata. J Bacteriol 132:818–823
Jordan DB, Orgren WL (1981) Species variation in the specificity of ribulose bisphosphate carboxylase/oxygenase. Nature (London) 291:513–515
Karagouni AD, Slater JH (1979) Enzymes of the Calvin cycle and intermediary metabolism in the cyanobacterium Anacystis nidulans grown in chemostat culture. J Gen Microbiol 115:369–376
Laemmli UK (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature (London) 227:680–685
Lee JC, Timasheff SN (1979) The calculation of partial specific volume of proteins in 6 M guanidine hydrochloride. In: Hirs CHW, Timasheff SN (eds) Enzyme structure, part H. Methods Enzymol 61:49–57
Lowry DH, Rosebrough NJ, Farr AL, Randall RJ (1951) Protein measurement with the Folin phenol reagent. J Biol Chem 193:265–275
Marrs B (1981) Mobilization of the genes for photosynthesis from Rhodopseudomonas capsulata by a promiscuous plasmid. J Bacteriol 146:1003–1012
McFadden BA (1980) A perspective of ribulose bisphosphate carboxylase/oxygenase, the key catalyst in photosynthesis and photorespiration. Acc Chem Res 13:394–399
Sarles LS, Tabita FR (1983) Derepression on the synthesis of D-ribulose-1,5-bisphosphate carboxylase/oxygenase from Rhodospirillum rubrum. J Bacteriol 153:458–464
Shivley JM, Ball F, Brown DH, Saunders RE (1973) Functional organelles in prokaryotes: polyhedral inclusions (carboxysomes) of Thiobacillus neapolitanus. Science 182:584–586
Tabita FR, McFadden BA (1974) D-Ribulose-1,5-diphosphate carboxylase from Rhodospirillum rubrum. I. Levels, purification and effects of metallic ions. J Biol Chem 249:3453–3458
Weaver PF, Wall JD, Gest H (1975) Characterization of Rhodopseudomonas capsulata. Arch Microbiol 105:207–216
Author information
Authors and Affiliations
Rights and permissions
About this article
Cite this article
Shively, J.M., Davidson, E. & Marrs, B.L. Depression of the synthesis of the intermediate and large forms of ribulose-1,5-bisphosphate carboxylase/oxygenase in Rhodopseudomonas capsulata . Arch. Microbiol. 138, 233–236 (1984). https://doi.org/10.1007/BF00402127
Received:
Accepted:
Issue Date:
DOI: https://doi.org/10.1007/BF00402127