Disease relevance of Shewanella

• Flavocytochrome c(3) (Fcc(3)), the globular fumarate reductase from Shewanella frigidimarina, and the soluble subcomplex of the membrane-bound fumarate reductase of Escherichia coli (FrdAB) each contain an active site FAD that is redox-connected to the surface by a chain of hemes or Fe-S clusters, respectively [1].
• The translated ksdD gene product was found to be similar to the 3-ketosteroid-delta 1-dehydrogenase of Pseudomonas testosteroni and to the fumarate reductase of Shewanella putrefaciens [2].
• Reduction of Prussian Blue by the two iron-reducing microorganisms Geobacter metallireducens and Shewanella alga [3].
• We describe a case of bacteremia due to imipenem-susceptible Shewanella algae [4].
• Homogentisic acid is the primary precursor of melanin synthesis in Vibrio cholerae, a Hyphomonas strain, and Shewanella colwelliana [5].

High impact information on Shewanella

• Fe(III)-reducing microorganisms in the genus Shewanella have resolved this problem by releasing soluble quinones that can carry electrons from the cell surface to Fe(III) oxide that is at a distance from the cell [6].
• Force microscopy has been used to quantitatively measure the infinitesimal forces that characterize interactions between Shewanella oneidensis (a dissimilatory metal-reducing bacterium) and goethite (alpha-FeOOH), both commonly found in Earth near-surface environments [7].
• Experiments with dissimilatory Fe-reducing bacteria of the genus Shewanella algae grown on a ferrihydrite substrate indicate that the delta(56)Fe of ferrous Fe in solution is isotopically lighter than the ferrihydrite substrate by 1.3 per mil [8].
• Here, we identify two gene clusters in Shewanella oneidensis strain MR-1 that each contain homologs of genes required for metal reduction and genes that are predicted to encode dimethyl sulfoxide (DMSO) reductase subunits [9].
• Extracellular respiration of dimethyl sulfoxide by Shewanella oneidensis strain MR-1 [9].

Chemical compound and disease context of Shewanella

• The soluble fumarate reductase of Shewanella putrefaciens MR-1 is a periplasmic tetraheme flavocytochrome c. The crystal structures of the enzyme were solved to 2.9 A for the uncomplexed form and to 2.8 A and 2.5 A for the fumarate and the succinate-bound protein, respectively [10].
• We show that DMSO respiration is an extracellular respiratory process through the analysis of mutants defective in type II secretion, which is required for transporting proteins to the outer membrane in Shewanella [9].
• Here we show that a two-gene cluster (arrAB; arsenate respiratory reduction) in the bacterium Shewanella sp. strain ANA-3 specifically confers respiratory As(V) reductase activity [11].
• The dicarboxylate ligand in oxaloacetate-containing crystals appears to be the same as that reported for Shewanella flavocytochrome c treated with fumarate [12].
• Crystal structure of oxidized trimethylamine N-oxide reductase from Shewanella massilia at 2.5 A resolution [13].

Biological context of Shewanella

• The mtr operon, which is involved in iron reduction, was poorly conserved among other known metal-reducing Shewanella species [14].
• The periplasmic trimethylamine N-oxide (TMAO) reductase from the marine bacteria Shewanella massilia is involved in a respiratory chain, having trimethylamine N-oxide as terminal electron acceptor [13].
• Within the frame of the characterization of the structure and function of cytochromes c, an 81-amino acid cytochrome c was identified in the genome of Shewanella putrefaciens [15].
• The amino acid sequence of the Lly protein exhibits a high degree of homology with the sequences of the MelA protein responsible for melanin production in the freshwater bacterium Shewanella colwelliana and the 4-hydroxyphenylpyruvate dioxygenase of Pseudomonas spp [16].
• Involvement of cytochromes in the anaerobic biotransformation of tetrachloromethane by Shewanella putrefaciens 200 [17].

Anatomical context of Shewanella

• Vanadium(V) reduction by Shewanella oneidensis MR-1 requires menaquinone and cytochromes from the cytoplasmic and outer membranes [18].

Gene context of Shewanella

• Cloning and sequence of cymA, a gene encoding a tetraheme cytochrome c required for reduction of iron(III), fumarate, and nitrate by Shewanella putrefaciens MR-1 [19].
• OBJECTIVES: To determine the beta-lactamase gene content of beta-lactam-susceptible psychrophilic gram-negative bacilli, Shewanella frigidimarina and Shewanella livingstonensis, isolated from a marine environment [20].
• Sequence and genetic characterization of etrA, an fnr analog that regulates anaerobic respiration in Shewanella putrefaciens MR-1 [21].
• Six monoclonal antibodies were produced to whole cells of Shewanella colwelliana (Aco1 to Aco6) and two (Aco22 to Aco23) to purified exopolysaccharide (EPS) [22].
• Genetic complementation of an outer membrane cytochrome omcB mutant of Shewanella putrefaciens MR-1 requires omcB plus downstream DNA [23].

Analytical, diagnostic and therapeutic context of Shewanella

• Crystallization and preliminary X-ray analysis of flavocytochrome c(3), the fumarate reductase from Shewanella frigidimarina [24].
• Electron microscopy, sodium dodecyl sulfate-polyacrylamide gel electrophoresis with silver staining and (1)H, (13)C, and (31)P-nuclear magnetic resonance (NMR) were used to detect and characterize the lipopolysaccharides (LPSs) of several Shewanella species [25].
• PCR primers specific to individual ORFs from Shewanella oneidensis MR-1 and Deinococcus radiodurans R1 have been designed [26].
• An eicosapentaenoic acid-producing bacterium, previously described as Shewanella sp. strain SCRC-2738, was classified by phenotypic characterization, chemotaxonomic analysis, 16S rRNA gene sequence analysis and DNA-DNA hybridization [27].
• Changes in mRNA and protein expression profiles of Shewanella oneidenesis MR-1 during switch from aerobic to fumarate-, Fe(III)-, or nitrate-reducing conditions were examined using DNA microarrays and two-dimensional polyacrylamide gel electrophoresis (2-D PAGE) [28].

References