Thiomonas bhubaneswarensis sp. nov., an obligately mixotrophic, moderately thermophilic, thiosulfate-oxidizing bacterium

Panda, Suchismita; Jyoti, V.; Bhadra, Bhaskar; Nayak, Kinshuk Chandra; Shivaji, Sisinthy; Rainey, Fred A.; Das, Subrata K.

doi:10.1099/ijs.0.007120-0

Cited by 46 publications

(24 citation statements)

References 29 publications

(24 reference statements)

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“…S5 in the supplemental material). With respect to utilization of RISCs, members of the genera Acidithiobacillus, Acidiphilium, Thiomonas, Hydrogenobaculum, and Burkholderia are able to oxidize thiosulfate (10,28,(45)(46)(47). Although L. ferrodiazotrophum is an acidophilic iron oxidizer, sulfur oxidation for energy generation has been suggested by the results of genomic analysis (48).…”

Section: Resultsmentioning

confidence: 99%

Tetrathionate-Forming Thiosulfate Dehydrogenase from the Acidophilic, Chemolithoautotrophic Bacterium Acidithiobacillus ferrooxidans

Kikumoto

Nogami

Kanao

et al. 2013

Appl Environ Microbiol

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bThiosulfate dehydrogenase is known to play a significant role in thiosulfate oxidation in the acidophilic, obligately chemolithoautotroph, Acidithiobacillus ferrooxidans. Enzyme activity measured using ferricyanide as the electron acceptor was detected in cell extracts of A. ferrooxidans ATCC 23270 grown on tetrathionate or sulfur, but no activity was detected in ferrous iron-grown cells. The enzyme was enriched 63-fold from cell extracts of tetrathionate-grown cells. Maximum enzyme activity (13.8 U mg ؊1 ) was observed at pH 2.5 and 70°C. The end product of the enzyme reaction was tetrathionate. The enzyme reduced neither ubiquinone nor horse heart cytochrome c, which serves as an electron acceptor. A major protein with a molecular mass of ϳ25 kDa was detected in the partially purified preparation. Heme was not detected in the preparation, according to the results of spectroscopic analysis and heme staining. The open reading frame of AFE_0042 was identified by BLAST by using the N-terminal amino acid sequence of the protein. The gene was found within a region that was previously noted for sulfur metabolismrelated gene clustering. The recombinant protein produced in Escherichia coli had a molecular mass of ϳ25 kDa and showed thiosulfate dehydrogenase activity, with maximum enzyme activity (6.5 U mg ؊1 ) observed at pH 2.5 and 50°C.

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Section: Resultsmentioning

confidence: 99%

Tetrathionate-Forming Thiosulfate Dehydrogenase from the Acidophilic, Chemolithoautotrophic Bacterium Acidithiobacillus ferrooxidans

Kikumoto

Nogami

Kanao

et al. 2013

Appl Environ Microbiol

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“…The jar was incubated at 37 u C and examined after 7 days. All other routine biochemical tests and procedures were performed as described by Panda et al (2009). Phenotypic properties of strain HT4…”

Section: Colonies Of Strain Ht4mentioning

confidence: 99%

“…Extraction of genomic DNA and PCR amplification of the 16S rRNA gene were carried out as described by Das et al (1996). The gel-purified 16S rRNA gene was sequenced by using a CEQ Dye terminator cycle sequencing kit in a model CEQ 8000 automated DNA sequencer (Panda et al, 2009). The 16S rRNA gene sequence of strain HT4…”

Section: Panday and S K Dasmentioning

confidence: 99%

Chelatococcus sambhunathii sp. nov., a moderately thermophilic alphaproteobacterium isolated from hot spring sediment

Panday

Das

2010

International Journal of Systematic and Evolutionary Microbiology

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A moderately thermophilic bacterial strain (HT4 T ) isolated from a hot spring sediment was characterized phenotypically and phylogenetically. Cells were Gram-negative, aerobic, non-sporulating, rod-shaped and motile by means of a single polar flagellum. Both oxidase and catalase activities were positive. Heterotrophic growth was observed at pH 6.0-8.5 and at 20-50 6C; optimum growth occurred at pH 7.5-8.0 and 37-42 6C. The major cellular fatty acids were C 14 : 0 3-OH, C 18 : 0 3-OH, Exploration of bacterial species in hot springs is of importance owing to the intriguing biogeochemistry and extreme conditions of these environments. The vast majority of bacterial species belonging to the most recent lines of descent, such as the Proteobacteria, are mesophilic, although slightly thermophilic, moderately thermophilic and even extremely thermophilic species have been described from these bacterial lineages. The Alphaproteobacteria includes many mesophilic species, but also a few slightly thermophilic or moderately thermophilic species, namely Rubritepida flocculans , 1975), but the micro-organisms present in these environments have been little studied (but see Ghosh et al., 2003). This paper describes a bacterial strain (HT4 T ) isolated from a hot spring located at Athamallik, Orissa, India. Based on the results of the present polyphasic taxonomic study, strain HT4T is considered to represent a novel species of the genus Chelatococcus.The hot spring at Athamallik is situated at 80 m above sea level. It has a series of outlets within a radius of 70 m. The water temperature at the main outlet was 56 u C and in the surrounding areas ranged from 43 to 50 u C. The pH of sediment samples taken for analysis was 7.4. Sediment samples were transported to the laboratory without temperature control and subsequently transferred into 250-ml conical flasks containing 50 ml nutrient broth (Difco) and incubated on a shaker (ISF-1-V; Adolf Kuhner AG) at 200 r.p.m. and 45 u C. After 2 days incubation, the contents of the flasks were serially diluted and plated onto nutrient agar medium (Difco) and incubated at 37 u C for 4 days. Several colonies that developed at 37 u C were picked and purified by repeated streaking on the same medium. A colony with a mucoid cream colour was selected for further analysis; this was designated strain HT4 T . Colonies of strain HT4T grown on nutrient agar were circular, 1.5-2.5 mm in diameter, mucoid and smooth.The GenBank/EMBL/DDBJ accession number for the 16S rRNA gene sequence of strain HT4T is DQ322070.A supplementary table detailing the fatty acid composition of strain HT4T and other members of the genus Chelatococcus is available with the online version of this paper.

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“…bhubaneswarensis , Ac. thiooxydans , Ga. acididurans , Sulfuriferula sp., and those of the AMD metagenome [45–49]. This phylogenetic tree also reveals that PilY1 and PilC are homologues; all the analyzed sequences comprise the Neisseria -PilC beta-propeller domain.…”

Section: Resultsmentioning

confidence: 92%

Sequence analysis and confirmation of type IV pili-associated proteins PilY1, PilW and PilV in Acidithiobacillus thiooxidans

García‐Meza

Alfaro-Saldaña

Hernández-Sánchez

et al. 2018

Preprint

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24 Acidithiobacillus thiooxidans is an acidophilic chemolithoautotrophic bacterium 25 widely used in the mining industry due to its metabolic sulfur-oxidizing capability. The 26 biooxidation of sulfide minerals is enhanced through the attachment of A. thiooxidans 27 cells to the mineral surface. The Type IV pili (TfP) of At. thiooxidans may play an 28 important role in the bacteria attachment, since among other functions, TfP play a 29 key adhesive role in the attachment to and colonization of different surfaces. In this 30 work, we reported for the first time the confirmed mRNA sequences of three TfP 31 proteins from At. thiooxidans, the protein PilY1 and the TfP pilins PilW and PilV. The 32 nucleotide sequences of these TfP proteins show changes of some nucleotide 33 positions with respect to the corresponding annotated sequences. The bioinformatic 34 analyses and 3D-modeling of protein structures sustain their classification as TfP 35 proteins, as structural homologs of the corresponding proteins of P. aeruginosa, 36 results that sustain the role of PilY1, PilW and PilV in pili assembly. Also, that PilY1 37 comprises the conserved Neisseria-PilC (superfamily) domain of the tip-associated 38 adhesin, while PilW of the superfamily of putative TfP assembly proteins and PilV 39 belongs to the superfamily of TfP assembly protein. Also, the analyses suggested 40 the presence of specific functional domains involved in adhesion, energy 41 transduction and signaling functions. The phylogenetic analysis indicated that the 42 PilY1 of Acidithiobacillus genus forms a cohesive group linked with iron-and/or 43 sulfur-oxidizing microorganisms from acid mine drainage or mine tailings. This work 3 44 enriches knowledge regarding colonization, adhesion and biooxidation of inorganic 45 sulfurs by A. thiooxidans. 46 4 47 Introduction 48 Acidithiobacillus thiooxidans is an acidophilic chemolithoautotroph that uses reduced 49 sulfurs as a source of electrons and reducing power, including elemental sulfur (S 0 ), 50 polysulfides (S n 2-) and sulfide minerals, such as pyrite (FeS 2 ), chalcopyrite (CuFeS 2 ) 51 or sphalerite (ZnS). 52 Bacterial attachment to mineral surfaces influences the rate of dissolution of the 53 mineral because of surficial phenomena: Mixed potential decreases, changes in 54 kinetics and mass-transport processes [1]. Accordingly, bacterial attachment is due 55 to self-organization by a bioelectrochemical evolution on the interface. Interfacial 56 studies on charge and mass transfer demonstrate that S 0 biooxidation by At. 57 thiooxidans begins in the early stages of interaction (1 to 24 h) when the biofilm is 58 not constituted, and it is primarily controlled by surficial characteristics that pivoted 59 the bacterial attachment to the hydrophobic S 0 ; such attachment is an energy-60 dependent process in which At. thiooxidans essentially activates or modifies the 61 reactive properties of S 0 [2, 3]. The hydrophobic character of the interface 62 "determines the free energy of the adhesion process" [4]. The Typ...

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Thiomonas bhubaneswarensis sp. nov., an obligately mixotrophic, moderately thermophilic, thiosulfate-oxidizing bacterium

Cited by 46 publications

References 29 publications

Tetrathionate-Forming Thiosulfate Dehydrogenase from the Acidophilic, Chemolithoautotrophic Bacterium Acidithiobacillus ferrooxidans

Tetrathionate-Forming Thiosulfate Dehydrogenase from the Acidophilic, Chemolithoautotrophic Bacterium Acidithiobacillus ferrooxidans

Chelatococcus sambhunathii sp. nov., a moderately thermophilic alphaproteobacterium isolated from hot spring sediment

Sequence analysis and confirmation of type IV pili-associated proteins PilY1, PilW and PilV in Acidithiobacillus thiooxidans

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