Disease relevance of Alphaproteobacteria

• We have identified a circularly permuted version of the tmRNA gene in alpha-proteobacteria as well as in a lineage of cyanobacteria [1].
• Actinobacteria contributed 70% to glucose assimilation in freshwater, while Alphaproteobacteria assimilated 60% of this compound in saline water [2].
• Wolbachia spp. are intracellular alpha proteobacteria closely related to Rickettsia [3].
• We provide experimental evidence for RNase III-dependent processing in helix 9 of the 23S rRNA as a general feature of many species in the alpha subclass of Proteobacteria (alpha-Proteobacteria) [4].
• Fifty-two percent of the pcaH clones could be assigned to the roseobacter group, a marine lineage of the class alpha-Proteobacteria abundant in coastal ecosystems [5].

High impact information on Alphaproteobacteria

• 5-Aminolevulinate synthase (ALAS) is the first and rate-limiting enzyme of heme biosynthesis in humans, animals, other non-plant eukaryotes, and alpha-proteobacteria [6].
• This hypothesis relates to the plethora of duplicated HSP60 sequences among the classical alpha-proteobacteria contrasted with no duplications of HSP60 among other clades of proteobacterial genomes [7].
• The flaF gene, which is conserved in several speices of flagellated alpha-proteobacteria, is required for motility and flagellin protein synthesis [8].
• The nodulation of legumes has for more than a century been considered an exclusive capacity of a group of microorganisms commonly known as rhizobia and belonging to the alpha-Proteobacteria [9].
• Single-strand conformational polymorphism analysis showed that plant species had no impact on the diversity of alpha-Proteobacteria tfdA-like genes, although an impact of 2,4-D application was recorded [10].

Chemical compound and disease context of Alphaproteobacteria

• The tfdAalpha genes were also detected in 2,4-D-degrading alpha-Proteobacteria previously isolated from pristine environments in Hawaii and in Saskatchewan, Canada (Y. Kamagata, R. R. Fulthorpe, K. Tamura, H. Takami, L. J. Forney, and J. M. Tiedje, Appl. Environ. Microbiol. 63:2266-2272, 1997) [11].
• These bacteria are able to use methyl halides as a sole source of carbon and energy, are all members of the alpha-Proteobacteria and were isolated from a variety of polluted and pristine terrestrial environments [12].
• Sulfitobacter mediterraneus sp. nov., a new sulfite-oxidizing member of the alpha-Proteobacteria [13].
• The most frequently obtained new isolates, mostly from 10(3)- and 10(4)-fold dilutions of the continental slope sediment, oxidized thiosulfate to sulfate and fell into a distinct phylogenetic cluster of marine alpha-Proteobacteria [14].
• Rather, we found that at least one function of BacA is to affect the distribution of LPS fatty acids, including a very-long-chain fatty acid thought to be unique to the alpha-proteobacteria, including B. abortus [15].

Biological context of Alphaproteobacteria

• During a molecular phylogenetic survey of extremely acidic (pH < 1), metal-rich acid mine drainage habitats in the Richmond Mine at Iron Mountain, Calif., we detected 16S rRNA gene sequences of a novel bacterial group belonging to the order Rickettsiales in the Alphaproteobacteria [16].
• All strains showed positive signals for tfdAalpha, and its phylogenetic tree was congruent with that of 16S rRNA genes in alpha-Proteobacteria, indicating evolution of tfdAalpha without horizontal gene transfer [17].
• This operon encodes a putative aldehyde dehydrogenase (ALD2; 357 amino acids) related to class III alcohol dehydrogenases and most similar to glutathione-dependent formaldehyde dehydrogenases from alpha-Proteobacteria and Anabeana azollae [18].
• Site-directed mutations that changed this consensus sequence abolished the DNA-damage-mediated expression of the R. palustris recA gene, confirming that this sequence is the SOS box of R. palustris and probably plays the same role in other alpha-Proteobacteria [19].
• Widespread occurrence of a separate small RNA derived from the 5'-end of 23S rRNA and of an intervening sequence (IVS) which separates this domain from the main segment of 23S rRNA in the alpha-proteobacteria implies that processing reactions which act to excise the IVS are also maintained in this group [20].

Gene context of Alphaproteobacteria

• Phylogenomic analysis supports lateral transfer of a eukaryotic-like HisRS into the alpha-proteobacteria followed by in situ adaptation of the bacterial tDNA(His) and identity rule divergence [21].
• The variable part of the dnaK gene as an alternative marker for phylogenetic studies of rhizobia and related alpha Proteobacteria [22].
• Strong recognition of U35 and U36 was confined to the pyrococcus-spirochete grouping within the archaeal branch of the class I LysRS phylogenetic tree, while U36 recognition was seen in other archaea and an example from the alpha-proteobacteria [23].
• All bacteria other than the low G+C small cocci and a few of the alpha-Proteobacteria accumulated PHB [24].
• Evolutionary relationship of phototrophic bacteria in the alpha-Proteobacteria based on farnesyl diphosphate synthase [25].

Analytical, diagnostic and therapeutic context of Alphaproteobacteria

• The genes responsible for the degradation of 2,4-dichlorophenoxyacetate (2,4-D) by alpha-Proteobacteria have previously been difficult to detect by using gene probes or polymerase chain reaction (PCR) primers [26].
• DESIGN: Amoeba-associated alpha Proteobacteria were isolated from water samples taken from ICU taps and general hospital reservoir tanks using an amoebal co-culture procedure [27].

References