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  • 1
    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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  • 2
    Electronic Resource
    Electronic Resource
    Redox-controlled, in vivo and in vitro phosphorylation of the α subunit of the light-harvesting complex I in Rhodobacter capsulatus (1992)
    Springer
    Archives of microbiology 158 (1992), S. 315-319 
    Details
    ISSN: 1432-072X
    Keywords: Protein phosphorylation ; Antenna protein ; Rhodobacter capsulatus
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Labelling of Rhodobacter capsulatus cells with (32P)Pi in a phototrophic culture results in phosphorylation of a membrane-bound polypeptide identified as the α subunit of the LHI antenna complex of the photosynthetic apparatus. Phosphorylation of the same polypeptide was also observed by incubation of chromatophores with (32P)ATP or under conditions of photophosphorylation with ADP and (32P)Pi. The identity of the phosphorylated LHI-α subunit was demonstrated by N-terminal protein sequencing of the phosphorylated polypeptide and by failure of labelling in LHI-defective mutants. Pre-aeration of the samples or addition of the oxidant potassium ferrcyanide stimulated the kinase activity whereas the presence of soluble cytoplasmic proteins impaired phosphorylation in an in vitro assay. No effect resulted from addition of reductants to the assay medium. The results indicate the presence of a membrane-bound protein kinase in R. capsulatus that phosphorylates the α subunit of the LHI antenna complex under redox control.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00245359
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  • 3
    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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