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  • 1
    Electronic Resource
    Electronic Resource
    SOMETHING FROM ALMOST NOTHING: Carbon Dioxide Fixation in Chemoautotrophs (1998)
    Palo Alto, Calif. : Annual Reviews
    Annual Review of Microbiology 52 (1998), S. 191-230 
    Details
    ISSN: 0066-4227
    Source: Annual Reviews Electronic Back Volume Collection 1932-2001ff
    Topics: Biology
    Notes: Abstract The last decade has seen significant advances in our understanding of the physiology, ecology, and molecular biology of chemoautotrophic bacteria. Many ecosystems are dependent on CO2 fixation by either free-living or symbiotic chemoautotrophs. CO2 fixation in the chemoautotroph occurs via the Calvin-Benson-Bassham cycle. The cycle is characterized by three unique enzymatic activities: ribulose bisphosphate carboxylase/oxygenase, phosphoribulokinase, and sedoheptulose bisphosphatase. Ribulose bisphosphate carboxylase/oxygenase is commonly found in the cytoplasm, but a number of bacteria package much of the enzyme into polyhedral organelles, the carboxysomes. The carboxysome genes are located adjacent to cbb genes, which are often, but not always, clustered in large operons. The availability of carbon and reduced substrates control the expression of cbb genes in concert with the LysR-type transcriptional regulator, CbbR. Additional regulatory proteins may also be involved. All of these, as well as related topics, are discussed in detail in this review.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1146/annurev.micro.52.1.191
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  • 2
    Electronic Resource
    Electronic Resource
    Isolation and characterization of a carboxysome shell gene from Thiobacillus neapolitanus (1994)
    Oxford, UK : Blackwell Publishing Ltd
    Molecular microbiology 12 (1994), S. 0 
    Details
    ISSN: 1365-2958
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology , Medicine
    Notes: The gene coding for the major carboxysome shell peptide (csoS1) from Thiobacillus neapolitanus has been isolated and sequenced. Oligonucleotide primers for polymerase chain reaction (PCR) amplification of the 5’end of the gene were made possible by amino acid sequencing of the N-terminal residues of the shell peptide. A 41 bp PCR product was used as a probe to isolate the gene. The deduced amino acid composition of the 216 bp gene shows a high degree of hydrophobicity. The gene is located within a series of three repeated regions of DNA and appears to have arisen via gene duplication. The transcript of csoS1 is approximately 400 bases in length. The shell peptide shares significant homology with Synechococcus open reading frames implicated in carboxysome structure/assembly. These open reading frames and csoS1 are related and are probably members of a carboxysome gene family.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-2958.1994.tb01052.x
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  • 3
    Electronic Resource
    Electronic Resource
    Two forms of ribulose-1,5-bisphosphate carboxylase/oxygenase from Thiobacillus denitrificans (1992)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 94 (1992), S. 0 
    Details
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Abstract The autotrophic, sulfur-oxidizing bacterium Thiobacillus denitrificans possesses two forms of the Calvin cycle enzyme ribulose-1,5-bisphosphate carboxylase / oxygenase (RuBisCO). The form I and form II genes were isolated from a cosmid library using heterologous DNA probes. Restriction enzyme analysis indicated that the genes are within 17 kbp of each other. Other Calvin cycle enzyme genes are not present. Analysis of T. denitrificans RNA indicated that the form I genes for the large and small subunits are co-transcribed with a length of 2800 nucleotides. The transcript for the form II gene is 1900 nucleotides in length.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1574-6968.1992.tb05299.x
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  • 4
    Electronic Resource
    Electronic Resource
    Calvin cycle genes in Nitrobacter vulgaris T3 (1994)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 120 (1994), S. 0 
    Details
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Abstract The genes encoding the Calvin cycle enzymes of Nitrobacter vulgaris T3 are found as two separate clusters on the chromosome. One cluster contains the genes for the large and small subunits of ribulose-1,5-biphosphate carboxylase/oxygenase (RuBisCO), glyceraldehyde-3-phosphate dehydrogenase, and one encoding a regulatory protein of the LysR family. The other cluster contains the genes for fructose-1,6-/sedoheptulose-1,7-bisphosphatase, phosphoribulokinase, and fructose-1,6-/sedoheptulose-1,7-biphosphate aldolase. With the exception of the LysR-like gene, the genes in each cluster are apparently transcribed in the same direction. The deduced amino acid sequence of both the large and small subunits of RuBisCO are most similar (84–86%) to those of Thiobacillus ferrooxidans and Chromatium vinosum. The deduced sequences of phosphoribulokinase and fructose/sedoheptulose bisphosphatase are 67–73 aand 44–46% similar to those reported for other autotrophic bacteria, respectively.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1574-6968.1994.tb07005.x
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  • 5
    Electronic Resource
    Electronic Resource
    Nucleotide sequences ofCyanophora paradoxa cellular and cyanelle-associated 5S ribosomal RNAs: The cyanelle as a potential intermediate in plastid evolution (1986)
    Springer
    Journal of molecular evolution 23 (1986), S. 300-304 
    Details
    ISSN: 1432-1432
    Keywords: 5S rRNA ; Sequence ; Secondary structure ; Cyanophora paradoxa ; Cyanelle ; Chloroplast evolution
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary The 5S ribosomal RNAs from the cell cytoplasm and cyanelle (photosynthetic organelle) ofCyanophora paradoxa have been isolated and sequenced. The cellular and cyanelle 5S rRNAs were 119 and 118 nucleotides in length, respectively. Both RNAs exhibited typical 5S secondary structure, but the primary sequence of the cellular species was clearly eukaryotic in nature, while that of the organellar species was prokaryotelike. The primary sequence of the cyanellar 5S rRNA was most homologous to cyanobacterial 5S sequences, yet possessed secondary-structural features characteristic of higher-plant chloroplast 5S rRNAs. Both sequence comparison and structural analysis indicated an evolutionary position for cyanelle 5S rRNA intermediate between blue-green alga and chloroplast 5S rRNAs.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02100638
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  • 6
    Electronic Resource
    Electronic Resource
    Depression of the synthesis of the intermediate and large forms of ribulose-1,5-bisphosphate carboxylase/oxygenase in Rhodopseudomonas capsulata (1984)
    Springer
    Archives of microbiology 138 (1984), S. 233-236 
    Details
    ISSN: 1432-072X
    Keywords: Ribulose bisphosphate carboxylase ; Rhodopseudomonas capsulata ; Enzyme regulation
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: 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.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00402127
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  • 7
    Electronic Resource
    Electronic Resource
    Expression of the cbbLcbbS and cbbM genes and distinct organization of the cbb Calvin cycle structural genes of Rhodobacter capsulatus (1995)
    Springer
    Archives of microbiology 164 (1995), S. 396-405 
    Details
    ISSN: 1432-072X
    Keywords: Key wordsccb genes ; RubisCO ; Form I ; Form II ; Rhodobacter capsulatus ; Calvin cycle
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Rhodobacter capsulatus fixes CO2 via the Calvin reductive pentose phosphate pathway and, like some other nonsulfur purple bacteria, is known to synthesize two distinct structural forms of ribulose 1,5-bisphosphate carboxylase/oxygenase (RubisCO). Cosmid clones that hybridized to form I (cbbLcbbS) and form II (cbbM) RubisCO gene probes were isolated from a genomic library of R. capsulatus strain SB1003. Southern blotting and hybridization analysis with gene-specific probes derived from Rhodobacter sphaeroides revealed that R. capsulatus cbbM is clustered with genes encoding other enzymes of the Calvin cycle, including fructose 1,6/sedoheptulose 1,7-bisphosphatase (cbbF), phosphoribulokinase (cbbP), transketolase (cbbT), glyceraldehyde-3-phosphate dehydrogenase (cbbG), and fructose 1,6-bisphosphate aldolase (cbbA), as well as a gene (cbbR) encoding a divergently transcribed LysR-type regulatory protein. Surprisingly, a cosmid clone containing the R. capsulatus form I RubisCO genes (cbbL and cbbS) failed to hybridize to the other cbb structural gene probes, unlike the situation with the closely related organism R. sphaeroides. The form I and form II RubisCO genes were cloned into pUC-derived vectors and were expressed in Escherichia coli to yield active recombinant enzyme in each case. Complementation of a RubisCO-deletion strain of R. sphaeroides to photosynthetic growth by R. capsulatus cbbLcbbS or cbbM was achieved using the broad host-range vector, pRK415, and R. sphaeroides expression vector pRPS-1.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s002030050281
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  • 8
    Electronic Resource
    Electronic Resource
    The interpretation of the mass spectrum of an ornithine-containing lipid from Thiobacillus thiooxidans (1978)
    Chichester : Wiley-Blackwell
    Biological Mass Spectrometry 5 (1978), S. 64-71 
    Details
    ISSN: 0306-042X
    Keywords: Chemistry ; Analytical Chemistry and Spectroscopy
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: The electron impact mass spectrum of a previously identified ornithine-containing lipid from Thiobacillus thiooxidans has been interpreted using exact mass measurements, low and high energy ionization, and defocused metastable studies. The spectrum, which did not contain a molecular ion for the intact lipid, was consistent with cyclization of the ornithine zwitterionic moiety with elimination of water to give 3[3′-(11,12-methylene-2-hydroxyoctadecanoxy)hexadecanylamine]-2-iperidone. Production of this sufficiently volatile species for mass spectral analysis was accomplished by gentle pyrolysis in the mass spectrometer source. The spectrum can be understood to arise by three primary decompositions which serve to separate the two fatty acid constitutents. The remainder of the spectrum is consistent with the expected fragmentations of these constituents.
    Additional Material: 2 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bms.1200050112
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