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  • 1
    Electronic Resource
    Electronic Resource
    Purification and characterization of an N-acylphosphatidylserine from Rhodopseudomonas sphaeroides (1982)
    s.l. : American Chemical Society
    Biochemistry 21 (1982), S. 2765-2773 
    Details
    ISSN: 1520-4995
    Source: ACS Legacy Archives
    Topics: Biology , Chemistry and Pharmacology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1021/bi00540a029
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    Pseudomonas aeruginosa RoxR, a response regulator related to Rhodobacter sphaeroides PrrA, activates expression of the cyanide-insensitive terminal oxidase (2002)
    Oxford, UK : Blackwell Science Ltd
    Molecular microbiology 45 (2002), S. 0 
    Details
    ISSN: 1365-2958
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology , Medicine
    Notes: The facultative anaerobe Pseudomonas aeruginosa has multiple aerobic electron transport pathways, one of which is terminated by a cyanide-insensitive oxidase (CIO). This study characterizes a P. aeruginosa two-component system that regulates CIO production. The response regulator of this system (RoxR) has significant amino acid sequence similarity to PrrA of Rhodobacter sphaeroides and related proteins in other α-proteobacteria. In heterologous complementation analysis, R. sphaeroides PrrA rescued the growth defect of a P. aeruginosa mutant lacking RoxR, and RoxR enabled photosynthetic growth of an R. sphaeroides PrrA mutant. Also, RoxR could substitute for PrrA in activating transcription in vitro, demonstrating that these proteins are functional homologues. P. aeruginosa strains lacking RoxR or the sensor kinase (RoxS) were more sensitive than wild type to the respiratory inhibitors cyanide and azide. The phenotypes of these mutant strains correlated with reduced cyanide-insensitive O2 utilization and less cyanide-dependent expression of the locus encoding the CIO (cioAB). The ability of purified RoxR to bind to the cioAB promoter region also suggests that this protein acts directly to regulate cioAB transcription. Therefore, RoxR appears to play a role in regulating the transcription of loci for P. aeruginosa energy-generating enzymes similar to that of its homologues in α-proteobacteria.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1046/j.1365-2958.2002.03046.x
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  • 3
    Electronic Resource
    Electronic Resource
    Phenotypic and genetic characterization of cytochrome c2-deficient mutants of Rhodobacter sphaeroides (1988)
    s.l. : American Chemical Society
    Biochemistry 27 (1988), S. 1918-1925 
    Details
    ISSN: 1520-4995
    Source: ACS Legacy Archives
    Topics: Biology , Chemistry and Pharmacology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1021/bi00406a018
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  • 4
    Electronic Resource
    Electronic Resource
    Activation of the cycA P2 promoter for the Rhodobacter sphaeroides cytochrome c2 gene by the photosynthesis response regulator (1999)
    Oxford BSL : Blackwell Science Ltd
    Molecular microbiology 34 (1999), S. 0 
    Details
    ISSN: 1365-2958
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology , Medicine
    Notes: The Rhodobacter sphaeroides photosynthesis response regulator, PrrA, positively regulates cycA P2 expression. Deletion analysis has identified sequences within 73 bp upstream of the transcription initiation site that are required for the activation of cycA P2 by PrrA. A mutant form of the Rhodobacter capsulatus PrrA homologue, whose activity is independent of phosphorylation (RegA*), protects an ≈ 26 bp region of cycA P2 that is centred at ≈ −50 from DNase digestion, and activates transcription of a mutant −14T promoter with increased activity when using either R. sphaeroides RNA polymerase or Escherichia coli Eσ70. A 4 bp target site mutation that eliminated DNA binding and transcription activation by RegA*in vitro also abolished PrrA activation of cycA P2 transcription in vivo, indicating that this region contains a PrrA binding site. By analysing the behaviour of the −14T mutant cycA P2 promoter in vivo, we also found that PrrA uses the same target site to activate expression in both the presence and the absence of O2. However, the extent of transcription activation by PrrA at cycA P2 in vivo is greater under anaerobic conditions.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1046/j.1365-2958.1999.01649.x
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  • 5
    Electronic Resource
    Electronic Resource
    Differences in two Pseudomonas aeruginosa cbb3 cytochrome oxidases (2004)
    Oxford, UK : Blackwell Science Ltd
    Molecular microbiology 51 (2004), S. 0 
    Details
    ISSN: 1365-2958
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology , Medicine
    Notes: Bacterial cytochrome cbb3 oxidases are members of the haeme-copper oxidase superfamily that are important for energy conservation by a variety of proteobacteria under oxygen-limiting conditions. The opportunistic pathogen Pseudomonas aeruginosa is unusual in possessing two operons that each potentially encode a cbb3 oxidase (cbb3-1 or cbb3-2). Our results demonstrate that, unlike typical enzymes of this class, the cbb3-1 oxidase has an important metabolic function at high oxygen tensions. In highly aerated cultures, cbb3-1 abundance and expression were greater than that of cbb3-2, and only loss of cbb3-1 influenced growth. Also, the activity of cbb3-1, not cbb3-2, inhibited expression of the alternative oxidase CioAB and thus influenced a signal transduction pathway much like that found in the α-proteobacterium Rhodobacter sphaeroides. Cbb3-2 appeared to play a more significant role under oxygen limitation by nature of its increased abundance and expression compared to highly aerated cultures, and the regulation of the cbb3-2 operon by the putative iron-sulphur protein Anr. These results indicate that each of the two P. aeruginosa cbb3 isoforms have assumed specialized energetic and regulatory roles.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1046/j.1365-2958.2003.03904.x
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  • 6
    Electronic Resource
    Electronic Resource
    Synthesis of Rhodobacter sphaeroides cytochrome c2 in Escherichia coli (1989)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 59 (1989), S. 0 
    Details
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Abstract The cytochrome c2 structural gene, cycA, from Rhodobacter sphaeroides was expressed in Escherichia coli. CycA-specific mRNA was detected in E. coli both under aerobic and anaerobic conditions with trimethylamine-N-oxide as electron acceptor. However mature holocytochrome c2 was only detected in anaerobically-grown cells. The mature form of cytochrome c2 (Mr= 12,500) was secreted into the periplasm of E. coli suggesting that the signal polypeptide was processed. The cytochrome c2 synthesized in E. coli exhibited absorbance maxima in the reduced from at 550 nm (α-band) and 521 nm (β-band) and contained covalently attached haem c. The results indicate that a foreign c-type cytochrome can be secreted and assembled in E. coli under anaerobic conditions.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1574-6968.1989.tb03120.x
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  • 7
    Electronic Resource
    Electronic Resource
    The puf operon region of Rhodobacter sphaeroides (1988)
    Springer
    Photosynthesis research 19 (1988), S. 39-61 
    Details
    ISSN: 1573-5079
    Keywords: Bacteriochlorophyll-protein complex ; gene expression ; light-harvesting complex ; reaction center ; Rhodospirillaceae ; transcriptional control ; translational control
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The puf operon of the purple nonsulfur photosynthetic bacterium, Rhodobacter sphaeroides, contains structural gene information for at least two functionally distinct bacteriochlorophyll-protein complexes (light harvesting and reaction center) which are present in a fixed ratio within the photosynthetic intracytoplasmic membrane. Two proximal genes (pufBA) specify subunits of a long wavelength absorbing (i.e., 875 nm) light harvesting complex which are present in the photosynthetic membrane in ≃15 fold excess relative to the reaction center subunits which are encoded by the pufLM genes. This review summarizes recent studies aimed at determining how expression of the R. sphaeroides puf operon region relates to the ratio of individual bacteriochlorophyll-protein complexes found within the photosynthetic membrane. These experiments indicate that puf operon expression may be regulated at the transcriptional, post-transcriptional, translation and post-translational levels. In addition, this review discusses the possible role(s) of newly identified loci upstream of pufB which may be involved in regulating either synthesis or assembly of individual bacteriochrlorophyll-protein complexes as well as the pufX gene, the most distal genetic element within the puf operon whose function is still unknown.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00114568
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  • 8
    Electronic Resource
    Electronic Resource
    Biosynthesis of the photosynthetic membranes of rhodopseudomonas sphaeroides (1983)
    New York, N.Y. : Wiley-Blackwell
    Journal of Cellular Biochemistry 22 (1983), S. 15-29 
    Details
    ISSN: 0730-2312
    Keywords: Rhodopseudomonas sphaeroides ; photosynthetic membrane synthesis ; cell cycle ; freeze fracture ; macromolecule distribution ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: The steady-state biosynthesis of the photosynthetic membrane (ICM) of Rhodopseudomonas sphaeroides has been reviewed. At moderate light intensities, 500 ft-c, preexisting ICM serves as the insertion matrix for newly synthesized membrane components. Whereas the bulk of the membrane protein, protein-pigment complexes, and pigments are inserted into preexisting ICM throughout the cell cycle, phospholipid is transferred from outside the ICM to the ICM only at the time of cell division. Because the site of cellular phospholipid synthesis is the cytoplasmic membrane, these results infer that despite the physical continuity of cytoplasmic membrane and ICM, there must exist between these membranous domains a “barrier” to the free diffusion of cellular phospholipid. The cyclical alternation in protein to phospholipid ratio of the ICM infers major structural and functional alternations, such as changes in the protein to lipid ratio of the membrane, specific density of the membrane, lipid structure within the membrane, and the rate of cyclic electron flow. When biochemical studies are correlated with detailed electron microscopic investigations we can further conclude that the number of photosynthetic units within the plane of the membrane can vary by nearly a factor of two over the course of the cell cycle. The average physical size of the photosynthetic units is constant for a given light intensity but inversely proportional to light intensity. The distribution of photosynthetic unit size classes within the membrane can be interpreted as suggesting that the “core” of the photosynthetic unit (reaction center plus fixed antenna complex) is inserted into the membrane coordinately as a structural entity. The variable antenna complex is, on the other hand, inserted independent of the “core” and randomly associates with both old and new core complexes. Finally, we conclude that there is substantial substructure to the distribution of photosynthetic units within the ICM, ie, they are highly ordered and exist in a defined spatial orientation to one another.
    Additional Material: 9 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/jcb.240220103
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  • 9
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    Toward a predictive understanding of Earth’s microbiomes to address 21st century challenges (2016)
    American Society for Microbiology
    Details
    Publication Date: 2022-05-25
    Description: © The Author(s), 2016. This article is distributed under the terms of the Creative Commons Attribution License. The definitive version was published in mBio 7 (2016): e00714-16, doi:10.1128/mBio.00714-16.
    Description: Microorganisms have shaped our planet and its inhabitants for over 3.5 billion years. Humankind has had a profound influence on the biosphere, manifested as global climate and land use changes, and extensive urbanization in response to a growing population. The challenges we face to supply food, energy, and clean water while maintaining and improving the health of our population and ecosystems are significant. Given the extensive influence of microorganisms across our biosphere, we propose that a coordinated, cross-disciplinary effort is required to understand, predict, and harness microbiome function. From the parallelization of gene function testing to precision manipulation of genes, communities, and model ecosystems and development of novel analytical and simulation approaches, we outline strategies to move microbiome research into an era of causality. These efforts will improve prediction of ecosystem response and enable the development of new, responsible, microbiome-based solutions to significant challenges of our time.
    Description: E.L.B. is supported by the Genomes-to-Watersheds Subsurface Biogeochemical Research Scientific Focus Area, and T.R.N. is supported by ENIGMA-Ecosystems and Networks Integrated with Genes and Molecular Assemblies (http://enigma.lbl.gov) Scientific Focus Area, funded by the U.S. Department of Energy (US DOE), Office of Science, Office of Biological and Environmental Research under contract no. DE-AC02- 05CH11231 to Lawrence Berkeley National Laboratory (LBNL). M.E.M. is also supported by the US DOE, Office of Science, Office of Biological and Environmental Research under contract no. DE-AC02-05CH11231. Z.G.C. is supported by National Science Foundation Integrative Organismal Systems grant #1355085, and by US DOE, Office of Biological and Environmental Research grant # DE-SC0008182 ER65389 from the Terrestrial Ecosystem Science Program. M.J.B. is supported by R01 DK 090989 from the NIH. T.J.D. is supported by the US DOE Office of Science’s Great Lakes Bioenergy Research Center, grant DE-FC02- 07ER64494. J.L.G. is supported by Alfred P. Sloan Foundation G 2-15-14023. R.K. is supported by grants from the NSF (DBI-1565057) and NIH (U01AI24316, U19AI113048, P01DK078669, 1U54DE023789, U01HG006537). K.S.P. is supported by grants from the NSF DMS- 1069303 and the Gordon & Betty Moore Foundation (#3300).
    Repository Name: Woods Hole Open Access Server
    Type: Article
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