Abstract
The mRNA levels specific for ribulose-1,5-bisphosphate carboxylase, light-harvesting I polypeptides alpha and beta, and reaction center polypeptides L and M were assayed by use of a series of DNA probes specific for each cognate mRNA. Both the steady-state amounts and sizes of the specific mRNAs were measured as a function of the light intensity incident to the culture, the presence or absence of oxygen, and the type of substrate present in the growth medium. Northern hybridization revealed at least two and possibly three transcripts for ribulose-1,5-bisphosphate carboxylase. The cellular level of mRNA specific for ribulose-1,5-bisphosphate carboxylase increased in consort with enzyme activity as a function of both light intensity and reducing state of the substrate. Neither mRNA nor enzyme activity was detectable in aerobically grown cells. For the light-harvesting I and reaction center polypeptides there exist two transcripts, the larger of which appears to be a polycistronic mRNA possessing information for all four polypeptides and a smaller transcript specific for only the alpha and beta polypeptides of the light-harvesting I complex. The regulation of each of these mRNAs was affected by light and oxygen, but was not significantly affected by the oxidation-reduction state of the substrate.
MeSH Terms
Bacterial Proteins/analysis,genetics
Bacteriochlorophylls/analysis
Light
Light-Harvesting Protein Complexes
Nucleic Acid Hybridization
Oxygen/pharmacology
Photosynthetic Reaction Center Complex Proteins
RNA, Bacterial/analysis
RNA, Messenger/analysis
Rhodobacter sphaeroides/genetics
Ribulose-Bisphosphate Carboxylase/analysis,genetics
Chemicals
Bacterial Proteins
Bacteriochlorophylls
Light-Harvesting Protein Complexes
Photosynthetic Reaction Center Complex Proteins
RNA, Bacterial
RNA, Messenger
Ribulose-Bisphosphate Carboxylase
Oxygen
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Zhu Y S
Kaplan S
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