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  • 1
    Electronic Resource
    Electronic Resource
    The protein patterns of intracytoplasmic membranes and reaction center particles isolated fromRhodopseudomonas capsulata (1974)
    Springer
    Archives of microbiology 96 (1974), S. 161-174 
    Details
    ISSN: 1432-072X
    Keywords: Membrane Proteins ; Reaction Center ; Intracytoplasmic Membrane ; Rhodopseudomonas capsulata
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Intracytoplasmic membranes of wild type strain 37 b 4 and mutant strains A1a car-bchl-, A1a car-bchl+ ofRhodopseudomonas capsulata were isolated. The membrane proteins were solubilized and separated by polyacrylamide gel electrophoresis (methods of Takayamaet al., 1964; Weber and Osborn, 1969). The band patterns were compared with each other. From the strain A1a car-bchl+ reaction center particles were isolated by treatment of membrane with Triton X-100 followed by sucrose density gradient centrifugation. The reaction center particles were found to be enriched in reaction center bacteriochlorophyll. This pigment shows a reversible bleaching at 855 nm and a blue shift at 798 nm. The light harvesting bacteriochlorophyll portion of this fraction was 14–22% of the total bacteriochlorophyll content. The three main proteins of the reaction center particles amount to about 80% of the total protein of the particles. The molecular weights of the main proteins were estimated to be 32000, 27500 and 22500 daltons.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00590173
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  • 2
    Electronic Resource
    Electronic Resource
    Formation of reaction centers and light-harvesting bacteriochlorophyll-protein complexes in Rhodopseudomonas capsulata (1975)
    Springer
    Archives of microbiology 104 (1975), S. 77-82 
    Details
    ISSN: 1432-072X
    Keywords: Membrane Differentiation ; Reaction Center ; Bacteriochlorophyll ; Antenna-Pigment Complex ; Bacteriochlorophyll-Protein Association ; Photosynthetic Bacteria
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Formation of the photosynthetic apparatus was induced in aerobically grown dark cultures of Rhodopseudomonas capsulata by lowering of the oxygen tension. Besides the wild type strain the carotenoid-less mutant strain A1a+ was investigated. Both strains exhibited initially a decrease of the molar ratio of total bacteriochlorophyll (Bchl) to reaction center (RC) Bchl, followed by an increase. Synthesis of RC-Bchl preceded the synthesis of light-harvesting (LH) Bchl. Activities of photophosphorylation in membrane preparations, isolated from cultures after different periods of incubation at low aeration, decreased on the basis of total Bchl from about 9 to 2 μmole ATP/μmole total Bchl·min, whereas the rate on the basis of RC-Bchl remained constant (about 500 μmole ATP/μmole RC-Bchl·min). Under the same conditions the membrane proteins were labelled with U−14C-protein hydrolysate. Corresponding to RC-Bchl the synthesis of RC-proteins dominated during the first 30 min of incubation at pO2 below 3 mmHg. After 45–60 min of membrane formation at low aeration the synthesis of LH-complex proteins exceeded the synthesis of RC proteins. The correlations between protein and Bchl synthesis in the sequential formation of RC- and LH-complexes are discussed.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00447303
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  • 3
    Electronic Resource
    Electronic Resource
    Oxygen tension regulated expression of the hemA gene of Rhodobacter capsulatus (1991)
    Springer
    Archives of microbiology 156 (1991), S. 129-134 
    Details
    ISSN: 1432-072X
    Keywords: δ-Aminolevulinic acid synthase ; Bacteriochlorophyll ; Promoter activity ; Oxygen regulation ; Rhodobacter capsulatus
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The promoter of the Rhodobacter capsulatus hemA gene, coding for the enzyme δ-aminolevulinic acid synthase (ALAS), was identified by trans-complementation of a δ-aminolevulinic acid (ALA)-dependent mutant and found to be located within a 170 bp region proximal to the hemA gene. The activity of the hemA promoter was demonstrated by lacZ fusion and in vitro transcription-translation. An open reading frame (ORFX) was found downstream of hemA. The activity of the hemA promoter, but not that of the ORFX promoter, increased when oxygen tension was lowered in the culture. Deletions upstream of the hemA promoter region did not affect ALAS activity and formation of pigment-protein complexes in R. capsulatus.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00290985
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  • 4
    Electronic Resource
    Electronic Resource
    Cloning and sequencing of the hemA gene of Rhodobacter capsulatus and isolation of a δ-aminolevulinic acid-dependent mutant strain (1990)
    Springer
    Molecular genetics and genomics 221 (1990), S. 371-378 
    Details
    ISSN: 1617-4623
    Keywords: hemA ; δ-Aminolevulinic acid synthase ; Tetrapyrrole biosynthesis ; Phototrophic bacteria ; Rhodobacter capsulatus
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary The Rhodobacter capsulatus hemA gene, coding for the enzyme δ-aminolevulinic acid synthase (ALAS), was isolated from a genome bank by hybridization with a hemT probe from Rhodobacter sphaeroides. Subcloning of the initial 3.9 kb HindIII fragment allowed the isolation of a 2.5 kb HindIII-BglII fragment which was able to complement the δ-aminolevulinic acid-requiring (ALA-requiring) Escherichia coli mutant SHSP19. DNA sequencing revealed an open reading frame coding for a protein with 401 amino acids which displayed similarity to the amino acid sequences of other known ALASs. However, no resemblance was seen to the HemA protein of E. coli K12. Based on the sequence data, an ALA-requiring mutant strain of R. capsulatus was constructed by site-directed insertion mutagenesis. Introduction of a plasmid, containing the hemA gene of R. capsulatus on the 3.9 kb HindIII fragment, restored ALA-independent growth of the mutant indicating that there is only one gene for ALA biosynthesis in R. capsulatus. Transfer of the R′ factor pRPS404 and hybridization analysis revealed that the ALAS gene is not located within the major photosynthetic gene cluster.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00259402
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    Paper (German National Licenses)
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