Disease relevance of Proteobacteria

• A considerable amount of evidence suggests that Proteobacteria (Purple bacteria) acquired quinol oxidase through a lateral gene transfer from Gram-positive bacteria [1].
• Glutathione metabolism is associated with oxygenic cyanobacteria and the oxygen-utilizing purple bacteria, but is absent in many other prokaryotes [2].
• Here we report the characterization of a well conserved glutamyl-tRNA synthetase (GluRS) paralog (YadB in Escherichia coli) that is present in the genomes of >40 species of proteobacteria, cyanobacteria, and actinobacteria [3].
• The reaction center of photo-system 2 (PS2) is related to the well-characterized reaction center of purple bacteria, while the reaction center of photosystem 1 (PS1) is related to the green sulfur bacteria, as is convincingly documented here [4].
• In the present work we report the expression of genes encoding the light-harvesting 2 (LH2) membrane-spanning proteins from a number of species of purple bacteria in mutants of Rhodobacter sphaeroides that lack the native LH2 antenna [5].

High impact information on Proteobacteria

• Nodulation of legumes by members of the beta-subclass of Proteobacteria [6].
• Unlike other eukaryotes, dinoflagellates containing peridinin use a form of RuBisCO (form II) previously found only in some species of proteobacteria [7].
• In bacteria in the phylum Proteobacteria that contain HPr kinase and XPr, the latter may be at the center of a complex regulatory network involving both CCR and the Ntr system [8].
• The results extend the structural analogies between the secondary quinone binding site in D1 and in subunit L of the photosynthetic reaction center in purple bacteria [9].
• Acyl-homoserine lactone (acyl-HSL) signaling is thought to mediate quorum sensing in many species of Proteobacteria [10].

Chemical compound and disease context of Proteobacteria

• Femtosecond dynamics of the forbidden carotenoid S1 state in light-harvesting complexes of purple bacteria observed after two-photon excitation [11].
• The Calvin-Benson-Bassham cycle constitutes the principal route of CO2 assimilation in aerobic chemoautotrophic and in anaerobic phototrophic purple bacteria [12].
• The proteins encoded by hscA and hscB, the chaperone HSP66 and the co-chaperone HSP20, have been shown to be required for the synthesis of 2Fe-2S clusters on ferredoxin in proteobacteria [13].
• The two best characterised obligately aerobic NTA-utilising genera (Chelatobacter and Chelatococcus) are members of the alpha-subgroup of Proteobacteria [14].
• The periplasmic nitrate reductase (Nap) is wide-spread in proteobacteria [15].

Biological context of Proteobacteria

• Temporally and spectrally resolved subpicosecond energy transfer within the peripheral antenna complex (LH2) and from LH2 to the core antenna complex in photosynthetic purple bacteria [16].
• We determined the nucleotide sequence of the puf operon of Rubrivivax gelatinosus (formerly called Rhodocyclus gelatinosus), a photosynthetic bacterium belonging to the beta subclass of purple bacteria (proteobacteria) [17].
• Pleiotropic effects of puf interposon mutagenesis on carotenoid biosynthesis in Rubrivivax gelatinosus. A new gene organization in purple bacteria [18].
• 16S rRNA gene analyses indicated that the rocks were dominated by sequences similar to sequences of Proteobacteria and that most organisms were related to nitrate reducers from a saline, alkaline, cold habitat; however, some phylotypes were either members of a novel lineage or closely related to uncultured clones [19].
• Evidence for autotrophic CO2 fixation via the reductive tricarboxylic acid cycle by members of the epsilon subdivision of proteobacteria [20].

Anatomical context of Proteobacteria

• Glutathione, the most abundant thiol in the eukaryotic cells, the cyanobacteria, and the alpha, beta, and gamma groups of the proteobacteria, has long been suspected to be involved in selenium metabolism [21].
• Two regimens of electrogenic cyclic redox chain operation in chromatophores of non-sulfur purple bacteria. A study using antimycin A [22].

Gene context of Proteobacteria

• Genes homologous to yadB are present only in bacteria, mostly in Proteobacteria [23].
• Myxococcus xanthus, a member of the Proteobacteria delta-class, has two independent recA genes, recA1 and recA2, but only recA2 is DNA damage-inducible [24].
• Oligonucleotides specific for B. henselae gltA were evaluated for the ability to prime PCR amplification within the alpha and gamma branches of the proteobacteria [25].
• Southern hybridization and nucleotide sequencing data have revealed apparent csrA homologs within several families of the alpha and gamma subdivisions of the proteobacteria (purple bacteria) and in the Gram-positive bacterium Bacillus subtilis [26].
• Only two exceptions had been reported-the Enterobacteriaceae and Myxococcus xanthus (members of the gamma and delta groups of the class Proteobacteria, respectively)-in which ornithine is produced from N-alpha-acetylornithine by a deacylase, acetylornithinase (AOase) (argE encoded) [27].

Analytical, diagnostic and therapeutic context of Proteobacteria

• Sequence analysis confirmed the genetic data and showed the presence of crtD and crtC genes downstream of the puf operon, a localization different from that known for other purple bacteria [18].
• Hydrogen ion equilibria of the reaction center protein from photosynthetic purple bacteria Rhodobacter sphaeroides and Rhodobacter capsulatus dissolved in micellular solution were studied by acid-base titration to estimate the water accessibility of protonatable residues of the protein determined from structural data [28].
• In situ hybridization results have indicated that Nitrosomonas-like ammonia oxidizing and Nitrospira-related nitrite oxidizing bacteria were intensively present in vigorous flocs in nitrification biofilter while carbonaceous bacteria belong to beta subclass of Proteobacteria were considerably dominant in oxidation ditch [29].

References