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Physiological regulation of ribulose 1,5 bisphosphate carboxylase/oxygenase in Rhodospirillum rubrum

Thesis/Dissertation ·
OSTI ID:6438976
Rhodospirillum rubrum employs several mechanisms for regulating the activity of ribulose 1,5 bisphosphate carboxylase/oxygenase (RuBPC/O). The activity of RuBPC/O is modulated at the level of synthesis of the enzyme and also post-transcriptionally by inactivation of the preformed enzyme. The synthesis of RuBPC/O in R. rubrum is greatly influenced by the conditions of culture. Under conditions of carbon dioxide limitation, R. rubrum derepresses the synthesis of RuBPC/O. When growing autotrophically under low CO/sub 2/ (1.5-2%) concentrations, the synthesis of the enzyme is derepressed such that RuBPC/O represents up to 50% of the soluble protein in the cell. These phenomenal levels of enzyme activity are not observed when the culture is supplied with higher levels of CO/sub 2/ (5-6%). The increase in enzyme activity observed in derepressed cultures is not paralleled by an increase in vivo CO/sub 2/ fixation rate. Rhodospirillum rubrum grown in the presence of /sup 32/P-orthophosphate, has radiolabel associated with several proteins. One of these proteins co-migrates with RuBPC/O in a SDS-polyacrylamide gel. The phosphoprotein can be separated from RuBPC/O using the technique of two-dimensional gel electrophoresis. A Western blot does not show any immunological cross-reactivity between the two proteins.
Research Organization:
Texas Univ., Austin (USA)
OSTI ID:
6438976
Country of Publication:
United States
Language:
English