- Open Access
Complete genome sequence of Thioalkalivibrio sp. K90mix
© The Author(s) 2011
- Published: 31 December 2011
Thioalkalivibrio sp. K90mix is an obligately chemolithoautotrophic, natronophilic sulfur-oxidizing bacterium (SOxB) belonging to the family Ectothiorhodospiraceae within the Gammaproteobacteria. The strain was isolated from a mixture of sediment samples obtained from different soda lakes located in the Kulunda Steppe (Altai, Russia) based on its extreme potassium carbonate tolerance as an enrichment method. Here we report the complete genome sequence of strain K90mix and its annotation. The genome was sequenced within the Joint Genome Institute Community Sequencing Program, because of its relevance to the sustainable removal of sulfide from wastewater and gas streams.
- sulfur-oxidizing bacteria
- soda lakes
Thioalkalivibrio sp. K90mix is an obligately chemolithoautotrophic SOxB using CO2 as a carbon source and reduced inorganic sulfur compounds as an energy source. It belongs to the genus Thioalkalivibrio. This genus represents a dominant SOxB type in soda lakes — extremely alkaline and saline habitats - and is the first example of an obligate chemolithoautotroph capable of growing in saturated sodium carbonate brines. It forms a monophyletic group within the family Ectothiorhodospiraceae of the Gammaproteobacteria. The genus currently includes nine validly published species  and around 70, yet uncharacterized strains that are extremely salt-tolerant and genetically different from the characterized isolates recovered from hypersaline soda lakes [2–4]. The members are slow growing obligate autotrophs, well adapted to hypersaline (up to salt saturation) and alkaline (up to pH 10.5) conditions. Members of the genus Thioalkalivibrio have versatile metabolic capabilities, including oxidation of reduced sulfur compounds [1,2], denitrification [5,6] and thiocyanate utilization [7,8].
Apart from playing an important role in the sulfur cycle of soda lakes, Thioalkalivibrio species also are being used for the sustainable removal of sulfide from wastewater and gas streams [9,10]. In this process hydrogen sulfide is absorbed to a high salt alkaline solution, which is subsequently transferred to a bioreactor in which Thioalkalivibrio spp. oxidize HS- to elemental sulfur. The produced biosulfur can then be used as a fertilizer or fungicide .
To get a comprehensive understanding of the molecular mechanism by which Thioalkalivibrio sp. K90mix oxidize sulfur compounds and adapts to extreme alkaline (up to pH 10.5) and hypersaline conditions (up to 4 M of Na+ or 3.6 M of K+) it is necessary to identify the genes that are involved in these adaptations. The most important issues in this are the mechanism of sulfide oxidation, carbon assimilation at high pH, and bioenergetic adaptation to high salt and high pH. Here we present a summary classification and a set of features for Thioalkalivibrio sp. K90mix together with the description of the genomic sequencing and annotation.
Because of limited solubility of sodium carbonates in the biodesulfurization process, we made a series of enrichment cultures with an increasing ratio of potassium to sodium carbonate (potassium carbonates have a 2–5 times higher solubility than sodium carbonates). Thioalkalivibrio sp. K90mix was isolated from a culture that was inoculated with a mixture of sediment samples from different hypersaline soda lakes and was grown at the maximal possible substitution of sodium for potassium, 3.6 M K+/0.4 M Na+ (90% substitution).
Classification and general features of Thioalkalivibrio sp. K90mix according to the MIGS recommendations .
Species Thioalkalivibrio sp. K90mix
Mesophile; maximum at 41°C
0.2–4.0 M Na+ (opt. 0.3 M)
Sulfide/polysulfide, thiosulfate, sulfur, sulfite
Soda lake sediments
Kulunda Steppe, Altai, Russia
Sample collection time
Genome project history
Genome sequencing project information
6kb and 40kb Sanger and 454 standard libraries
ABI-3730, 454 GS FLX Titanium
10.0× Sanger, 32.1× pyrosequence
Less than one error per 100 kb
Gene calling method
GenBank date of release
February 21, 2010
NCBI project ID
IMG Taxon ID
Source material identifier
Personal culture collection, Winogradsky Institute of Microbiology, Moscow
Growth conditions and DNA isolation
Thioalkalivibrio sp. K90mix was grown with 40 mM thiosulfate as an energy source in standard sodium carbonate-bicarbonate medium at pH 10 and 2 M Na+  at 35oC with shaking at 200 rpm. The cells were harvested by centrifugation and stored at minus 80°C for DNA extraction. Genomic DNA was obtained using phenol-chloroform-isoamylalcohol (PCI) extraction. The genomic DNA was extracted using PCI and precipitated with ethanol. The pellet was dried under vacuum and subsequently dissolved in water. The quality and quantity of the extracted DNA was evaluated using the DNA Mass Standard Kit provided by the JGI.
Genome sequencing and assembly
The genome of Thioalkalivibrio sp. K90mix was sequenced using a combination of Sanger and 454 sequencing platforms. All general aspects of library construction and sequencing can be found at the JGI website . Pyrosequencing reads were assembled using the Newbler assembler version 1.1.02.15 (Roche). Large Newbler contigs were broken into 3,292 overlapping fragments of 1,000 bp and entered into assembly as pseudo-reads. The sequences were assigned quality scores based on Newbler consensus q-scores with modifications to account for overlap redundancy and adjust inflated q-scores. A hybrid 454/Sanger assembly was made using the PGA assembler. Possible mis-assemblies were corrected and gaps between contigs were closed by editing in Consed, by custom primer walks from sub-clones or PCR products. A total of 181 Sanger finishing reads were produced to close gaps, to resolve repetitive regions, and to raise the quality of the finished sequence. Illumina reads were used to improve the final consensus quality using an in-house developed tool (the ‘Polisher’ ). The error rate of the completed genome sequence is less than 1 in 100,000. Together, the combination of the Sanger and 454 sequencing platforms provided 42.1× coverage of the genome. The final assembly contains 28,443 Sanger reads (10.0×) and 419,015 pyrosequencing reads (32.1×).
Genes were identified using Prodigal  as part of the Oak Ridge National Laboratory genome annotation pipeline followed by a round of manual curation using the JGI GenePRIMP pipeline . The predicted CDSs were translated and used to search the National Center for Biotechnology Information (NCBI) nonredundant database, UniProt, TIGRFam, Pfam, PRIAM, KEGG, COG, and InterPro, databases. Additional gene prediction analysis and functional annotation was performed within the Integrated Microbial Genomes Expert Review (IMG-ER) platform .
% of Total
Genome size (bp)
DNA coding region (bp)
DNA G+C content (bp)
Number of replicons
Extrachromosomal elements (plasmid)
Genes in paralog clusters
Genes assigned to COGs
Genes assigned Pfam domains
Genes with signal peptides
Number of genes associated with the general COG functional categories.
Translation, ribosomal structure and biogenesis
RNA processing and modification
Replication, recombination and repair
Chromatin structure and dynamics
Cell cycle control, mitosis and meiosis
Signal transduction mechanisms
Cell wall/membrane biogenesis
Intracellular trafficking and secretion
Posttranslational modification, protein turnover, chaperones
Energy production and conversion
Carbohydrate transport and metabolism
Amino acid transport and metabolism
Nucleotide transport and metabolism
Coenzyme transport and metabolism
Lipid transport and metabolism
Inorganic ion transport and metabolism
Secondary metabolites biosynthesis, transport and catabolism
General function prediction only
Not in COGs
The Hdr complex plays a function in the energy metabolism of methanogens  and sulfate-reducing prokaryotes . In methanogens, the enzyme complex catalyzes the reversible reduction of the disulfide (CoM-S-S-CoB) of the two methanogenic thiol-coenzymes, coenzyme M (CoM-SH) and coenzyme B (CoB-SH); in sulfate reducing microorganisms the substrate (X-S-S-X) is not known. Recently, the genes encoding the Hdr complex have also been detected in the genomes of the acidophilic sulfur oxidizing bacteria Acidithiobacillus ferrooxidans  and Acidithiobacillus caldus . Quantrini and co-workers  hypothesized that Hdr, like the dissimilatory sulfite reductase (dsr), is working in reverse, whereby sulfur (i.e., sulfane atom) is oxidized to sulfite, and electrons are donated to the quinone pool. Although the role of the Hdr complex in the sulfur metabolism still has to be confirmed by expression analysis, Hdr genes have not yet been detected in the genomes of the neutrophilic chemolithotrophic sulfur-oxidizing bacteria Thiomicrospira crunogena and Thiobacillus denitrificans or of phototrophic sulfur-oxidizing bacteria Allochromatium vinosum and Halorhodospira halophila. The absence of a reverse dsr pathway in Thioalkalivibrio sp. K90mix might be the reason why it can only tolerate sulfide concentrations up to 1 mM. Sulfite can be oxidized further to sulfate, either directly by sulfite dehydrogenase (sorA; TK90_0686) or indirectly via adenosine-5’-phosphosulfate (APS) by APS reductase encoded by aprBA (TK90_0064 and TK90_0065) and ATP sulfurylase encoded by sat (TK90_0062) . All these genes are present in the investigated genome.
Energy metabolism and pH homeostasis
At this time, it is not clear how Thioalkalivibrio sp. K90mix can withstand the harsh conditions of high pH and salinity. The difference between the pH of the environment (pH 10) and the pH in the cell (pH 8) causes a reversed ΔpH and consequently lowers the proton motive force (PMF). Therefore, Thioalkalivibrio requires a special molecular mechanisms to obtain enough energy for growth. It certainly needs this energy, because the production of osmolytes, to withstand the high concentrations of salts, costs 55 molecules of ATP for one molecule of glycine betaine, and 110 molecules of ATP for 1 molecule of sucrose . In addition, the chemolithoautotrophic life style of CO2 fixation is energetically very expensive. The redox potential of the substrate couple S°/HS- (−260 mV) is more positive that the potential of NAD+/NADH (-340 mV) and therefore the direct reduction of NAD+ in order to supply reducing equivalents for CO2 fixation is not possible. Reverse electron transport is necessary in order to produce enough NADH, necessary for CO2 fixation, which costs extra energy. In addition, because of the large pH gradient over the cell membrane Thioalkalivibrio needs special mechanisms to keep the intracellular pH around neutral (pH homeostasis), which again is an energy requiring process.
The genome has revealed genes encoding similar proteins as those found for “Thioalkalivibrio sulfidophilus” HL-EbGr7 . We found genes for a proton-driven F0F1-type ATP synthase (i.e., subunit A TK90_2593, B TK90_2591, and C TK90_2592of the F0 subcomplex, and subunit alpha (TK90_2589), beta (TK90_2587), gamma (TK90_2588), delta (TK90_2590), and epsilon (TK90_2586) of the F1 subcomplex), genes encoding the proton-translocating NADH dehydrogenase (nuoABCDEFGHIJKLMN) (TK90_0708 to TK90_0721), as well as the genes for a putative primary sodium pump Rnf  (rnfABCDGE) (TK90_1790 to TK90_1795). In addition, we found several genes encoding different secondary sodium-dependent pumps, such as the Na+/H+ antiporters NhaP (TK90_1831) and Mrp (mnhA-G) (TK90_0748 to TK90_0752), which according to Padan et al.  both play an essential role in alkaline pH homeostasis. In addition, we found genes encoding transporters belonging to the SulP family (TK90_0019, TK90_0897, TK90_0985). Transporters of this group could be involved in the low affinity, but high flux of bicarbonate uptake . In addition, genes encoding the sodium-depending flagellar motor PomA/B (TK90_1180 and TK90_1181) are also present in the genome (see below for more details). As Thioalkalivibrio sp. K90mix can stand high concentrations of potassium, we also searched for K+-transporters and found genes encoding the following transporters: TrkA-C (TK90_0502), TrkA-N (TK90_2266) and TrkH (TK90_2267) that are part of the potassium uptake system .
Chemotaxis and motility
We found different genes encoding methyl-accepting chemotaxis sensory transducers (TK90_0580, TK90_0949, TK90_1402, TK90_2562, TK90_2397) that are involved in chemotaxis. One of these genes, Aer (TK90_0580), encodes a redox sensor involved in aerotaxis. In E. coli, Aer regulates the motility behavior in gradients of oxygen, redox potential and certain nutrients by interacting with the CheA-CheW complex. We found genes encoding several different proteins of this complex, CheA (TK90_1178), CheW (TK90_1183 and TK90_1184), CheY (TK90_1176), CheZ (TK90_1177), CheB (TK90_1179), CheV (TK90_0924) and CheR (TK90_0925). Chemotaxis consists of a complex cascade of different reactions: the redox sensor Aer senses a difference in redox potential induced by a change in the environmental oxygen concentration, which leads to the autophosphorylation of the histidine protein kinase CheA. CheA phosphorylates CheY, which will switch on the flagellar motor (see  for a detailed overview). CheW acts as an adaptor protein, while CheB, CheR, CheZ, and CheV are involved in feedback regulation.
Transposases and environmental stress
Comparative analysis of the genomes of “Thioalkalivibrio sulfidophilus” HL-EbGr7  and Thioalkalivibrio sp. K90mix showed a greater abundance of genes encoding different transposases (i.e., COG2801, COG3328, COG3547) in the latter. Transposases are enzymes that can move specific sequences of DNA, known as transposons or transposable elements, within the genome. Krulwich  found that the genome of the alkaliphilic bacterium Bacillus halodurans C125 contained 112 transposase genes as compared to 10 in the genome of its closest non-alkaliphilic relative B. subtilis. She suggested that this might be one of the mechanisms of alkaliphilic adaptation at the genome level. Although strains HL-EbGr7 and K90mix are both obligately alkaliphilic, they differ in salt tolerance. HL-EbGr7 can tolerate only low (up to 1.5 M) salt concentrations, while K90mix can tolerate high (up to 4 M) salinities.
Capy et al.  mentioned that environmental stress might stimulate transposition and consequently increase the genetic variability, which can be beneficial for the adaptation to novel environmental conditions. Foti et al.  used rep-PCR  to study the genetic diversity within the genus Thioalkalivibrio and found a relatively high diversity of 56 genotypes among 85 strains that were isolated from different soda lakes in Africa and Asia. In addition, preliminary enrichment experiments with potassium carbonate instead of sodium carbonate and higher concentrations of chloride selected populations of high salt-tolerant Thioalkalivibrio strains with different rep-PCR patterns (unpublished results), which might be an indication that transposition might occur more frequently in strains with a wide range of salt tolerance.
Reactive oxygen species (ROS), such as superoxides (O2-) and hydrogen peroxidase (H2O2), are naturally produced at hypersaline conditions and are deleterious to cellular macromolecules. To protect themselves from this oxidative stress, Thioalkalivibrio sp. K90mix and “Thioalkalivibrio sulfidophilus” HL-EbGr7 have several defense mechanisms. Superoxides are converted to oxygen and hydrogen peroxide by the enzyme superoxide dismutase (TK90_0947, Tgr7_2463), while hydrogen peroxide is converted to oxygen by hydroperoxidase (TK90_0947, Tgr7_1107) or to H2O by the cytochrome C peroxidase (TK90_0812, Tgr7_2739). In addition, Thioalkalivibrio sp. K90mix produces high concentrations of a specific membrane-bound yellow pigment named ‘natronochrome’ . The pigment has a high degree of unsaturation and might also play a role in the protection against reactive oxygen species (ROS). The gene(s) responsible for the synthesis of this anti-oxidant remains to be identified.
Thioalkalivibrio sp. K90mix is an extremely salt-tolerant bacterium. It can grow in saturated sodium and potassium carbonate and sodium sulfate brines containing up to 4 M Na+/K+ but, in contrast to halo-alkaliphiles, it is inhibited by high concentrations of chloride. So, a more proper term for such an extremophile would be an “extreme natronophile”. To withstand these extreme salinities, it synthesizes glycine betaine as the main compatible solute; the genome contains the genes for glycine sarcosine N-methyltransferase (TK90_0179) and sarcosine dimethylglycine methyltransferase (TK90_0180). In addition, the genome contains the gene for sucrose phosphate synthase (TK90_2312) to produce sucrose as a compatible solute. Genes for ectoine were not found.
This work was performed under the auspices of the US Department of Energy Office of Science, Biological and Environmental Research Program, and by the University of California, Lawrence Berkeley National Laboratory under contract No. DE-AC02-05CH11231, Lawrence Livermore National Laboratory under Contract No. DE-AC52-07NA27344, and Los Alamos National Laboratory under contract No. DE-AC02-06NA25396, UT-Battelle and Oak Ridge National Laboratory under contract DE-AC05-00OR22725. Dimitry Sorokin was supported financially by RFBR grant 10-04-00152.
- Sorokin DY, Kuenen JG. Haloalkaliphilic sulfur-oxidizing bacteria from soda lakes. FEMS Microbiol Rev 2005; 29:685–702. PubMed doi:10.1016/j.femsre.2004.10.005View ArticlePubMedGoogle Scholar
- Sorokin DY, Banciu H, Robertson LA, Kuenen JG. Haloalkaliphilic sulfur-oxidizing bacteria. In: The Prokaryotes. Volume 2: Ecophysiology and Biochemistry 2006; pp. 969–984. Dworkin, M., Falkow S, Rosenberg E, Schleifer KH, Stackebrandt E. (Ed’s). Springer, New York.View ArticleGoogle Scholar
- Sorokin DY, van den Bosch PLF, Abbas B, Janssen AJH, Muyzer G. Microbiological analysis of the population of extremely haloalkaliphilic sulfur-oxidizing bacteria dominating in lab-scale sulfide-removing bioreactors. Appl Microbiol Biotechnol 2008; 80:965–975. PubMed doi:10.1007/s00253-008-1598-8View ArticlePubMedGoogle Scholar
- Foti M, Ma S, Sorokin DY, Rademaker JLW, Kuenen GJ, Muyzer G. Genetic diversity and bio-geography of haloalkaliphilic sulfur-oxidizing bacteria beloning to the genus Thioalkalivibrio. FEMS Microbiol Ecol 2006; 56:95–101. PubMed doi:10.1111/j.1574-6941.2006.00068.xView ArticlePubMedGoogle Scholar
- Sorokin DY, Kuenen JG, Jetten M. Denitrification at extremely alkaline conditions in obligately autotrophic alkaliphilic sulfur-oxidizing bacterium “Thioalkalivibrio denitrificans”. Arch Microbiol 2001; 175:94–101. PubMed doi:10.1007/s002030000210View ArticlePubMedGoogle Scholar
- Sorokin DY, Antipov AN, Kuenen JG. Complete denitrification in a coculture of haloalkaliphilic sulfur-oxidizing bacteria from a soda lake. Arch Microbiol 2003; 180:127–133. PubMed doi:10.1007/s00203-003-0567-yView ArticlePubMedGoogle Scholar
- Sorokin DY, Tourova TP, Lysenko AM, Kuenen JG. Microbial thiocyanate utilization under high alkaline conditions. Appl Environ Microbiol 2001; 67:528–538. PubMed doi:10.1128/AEM.67.2.528-538.2001PubMed CentralView ArticlePubMedGoogle Scholar
- Sorokin DY, Tourova TP, Antipov AN, Muyzer G, Kuenen JG. Anaerobic growth of the haloalkaliphilic denitrifying sulfur-oxidizing bacterium Thialkalivibrio thiocyanodenitrificans sp. nov. with thiocyanate. Microbiology 2004; 150:2435–2442. PubMed doi:10.1099/mic.0.27015-0View ArticlePubMedGoogle Scholar
- Janssen AJ, Lens PN, Stams AJ, Plugge CM, Sorokin DY, Muyzer G, Dijkman H, Van Zessen E, Luimes P, Buisman CJ. Application of bacteria involved in the biological sulfur cycle for paper mill effluent purification. Sci Total Environ 2009; 407:1333–1343. PubMed doi:10.1016/j.scitotenv.2008.09.054View ArticlePubMedGoogle Scholar
- van den Bosch PLF, Sorokin DY, Buisman CJN, Janssen AJH. The effect of pH on thiosulfate formation in a new biotechnological process for the removal of hydrogen sulfide from gas streams. Environ Sci Technol 2008; 42:2637–2642. PubMed doi:10.1021/es7024438View ArticlePubMedGoogle Scholar
- Field D, Garrity G, Gray T, Morrison N, Selengut J, Sterk P, Tatusova T, Thomson N, Allen MJ, Angiuoli SV, et al. The minimum information about a genome sequence (MIGS) specification. Nat Biotechnol 2008; 26:541–547. PubMed doi:10.1038/nbt1360PubMed CentralView ArticlePubMedGoogle Scholar
- Woese CR, Kandler O, Wheelis ML. Towards a natural system of organisms: proposal for the domains Archaea, Bacteria, and Eucarya. Proc Natl Acad Sci USA 1990; 87:4576–4579. PubMed doi:10.1073/pnas.87.12.4576PubMed CentralView ArticlePubMedGoogle Scholar
- Garrity GM, Bell JA, Lilburn T. Phylum XIV. Proteobacteria phyl. nov. In: Garrity GM, Brenner DJ, Krieg NR, Staley JT (eds), Bergey’s Manual of Systematic Bacteriology, Second Edition, Volume 2, Part B, Springer, New York, 2005, p. 1.View ArticleGoogle Scholar
- List Editor. Validation of publication of new names and new combinations previously effectively published outside the IJSEM. List No. 106. Int J Syst Evol Microbiol 2005; 55:2235–2238. doi:10.1099/ijs.0.64108-0Google Scholar
- Garrity GM, Bell JA, Lilburn T. Class III. Gamma-proteobacteria class. nov. In: Garrity GM, Brenner DJ, Krieg NR, Staley JT (eds), Bergey’s Manual of Systematic Bacteriology, Second Edition, Volume 2, Part B, Springer, New York, 2005, p. 1.View ArticleGoogle Scholar
- Imhoff J. Order I. Chromatiales ord. nov. In: Garrity GM, Brenner DJ, Krieg NR, Staley JT (eds), Bergey’s Manual of Systematic Bacteriology, Second Edition, Volume 2, Part B, Springer, New York, 2005, p. 1–3.View ArticleGoogle Scholar
- Imhoff JF. Reassignment of the genus Ectothiorhodospira Pelsh 1936 to a new family, Ectothiorhodospiraceae fam. nov., and emended description of the Chromatiaceae Bavendamm 1924. Int J Syst Bacteriol 1984; 34:338–339. doi:10.1099/00207713-34-3-338View ArticleGoogle Scholar
- Sorokin DY, Lysenko AM, Mityushina LL, Tourova TP, Jones BE, Rainey FA, Robertson LA, Kuenen GJ. Thioalkalimicrobium aerophilum gen. nov., sp. nov. and Thioalkalimicrobium sibericum sp. nov., and Thioalkalivibrio versutus gen. nov., sp. nov., Thioalkalivibrio nitratis sp.nov., novel and Thioalkalivibrio denitrificancs sp. nov., novel obligately alkaliphilic and obligately chemolithoautotrophic sulfur-oxidizing bacteria from soda lakes. Int J Syst Evol Microbiol 2001; 51:565–580. PubMedView ArticlePubMedGoogle Scholar
- Banciu H, Sorokin DY, Galinski EA, Muyzer G, Kleerebezem R, Kuenen JG. Thialkalivibrio halophilus sp. nov., a novel obligately chemolithoautotrophic, facultatively alkaliphilic, and extremely salt-tolerant, sulfur-oxidizing bacterium from a hypersaline alkaline lake. Extremophiles 2004; 8:325–334. PubMed doi:10.1007/s00792-004-0391-6PubMedGoogle Scholar
- List Editor. Notification that new names and new combinations have appeared in volume 51, part 2, of the IJSEM. Int J Syst Evol Microbiol 2001; 51:795–796. PubMed doi:10.1099/00207713-51-3-795Google Scholar
- De Vos P, Trüper HG, Tindall BJ. Judicial Commission of the International Committee on Systematics of Prokaryotes Xth International (IUMS) Congress of Bacteriology and Applied Microbiology. Minutes of the meetings, 28, 29 and 31 July and 1 August 2002, Paris, France. Int J Syst Evol Microbiol 2005; 55:525–532. doi:10.1099/ijs.0.63585-0View ArticleGoogle Scholar
- Classification of Bacteria and Archaea in risk groups. www.baua.de TRBA 466.
- Pruesse E, Quast C, Knittel K, Fuchs B, Ludwig W, Peplies J, Glöckner FO. SILVA: a comprehensive online resource for quality checked and aligned ribosomal RNA sequence data compatible with ARB. Nucleic Acids Res 2007; 35:7188–7196. PubMed doi:10.1093/nar/gkm864PubMed CentralView ArticlePubMedGoogle Scholar
- Ludwig W, Strunk O, Westram R, Richter L, Meier H. Yadhukumar, Buchner A, Lai T, Steppi S, Jobb G. ARB: a software environment for sequence data. Nucleic Acids Res 2004; 32:1363–1371. PubMed doi:10.1093/nar/gkh293PubMed CentralView ArticlePubMedGoogle Scholar
- Liolios K, Chen IM, Mavromatis K, Tavernarakis N, Hugenholtz P, Markowitz VM, Kyrpides NC. The Genomes OnLine Database (GOLD) in 2009: status of genomic and metagenomic projects and their associated metadata. Nucleic Acids Res 2010; 38:D346–D354. PubMed doi:10.1093/nar/gkp848PubMed CentralView ArticlePubMedGoogle Scholar
- DOE Joint Genome Institute. http://www.jgi.doe.gov/
- Lapidus A, LaButti K, Foster B, Lowry S, Trong S, Goltsman E. POLISHER: An effective tool for using ultra short reads in microbial genome assembly and finishing. AGBT, Marco Island, FL, 2008.Google Scholar
- Hyatt D, Chen GL, LoCascio PF, Land ML, Larimer FW, Hauser LJ. Prodigal: prokaryotic gene recognition and translation initiation site identification. BMC Bioinformatics 2010; 11:119. PubMed doi:10.1186/1471-2105-11-119PubMed CentralView ArticlePubMedGoogle Scholar
- Pati A, Ivanova NN, Mikhailova N, Ovchinnikova G, Hooper SD, Lykidis A, Kyrpides NC. GenePRIMP: a gene prediction improvement pipeline for prokaryotic genomes. Nat Methods 2010; 7:455–457. PubMed doi:10.1038/nmeth.1457View ArticlePubMedGoogle Scholar
- Markowitz VM, Szeto E, Palaniappan K, Grechkin Y, Chu K, Chen IM, Dubchak I, Anderson I, Lykidis A, Mavromatis K, et al. The integrated microbial genomes (IMG) system in 2007: data content and analysis tools extensions. Nucleic Acids Res 2008; 36:D528–D533. PubMed doi:10.1093/nar/gkm846PubMed CentralView ArticlePubMedGoogle Scholar
- Muyzer G, Sorokin DY, Mavromatis K, Lapidus A, Clum A, Ivanova N, Pati A, d’Haeseleer P, Woyke T, Kyrpides NC. Complete genome sequence of “Thioalkalivibrio sulfidophilus” HL-EbGR7. Stand Genomic Sci 2011; 4:23–35. PubMed doi:10.4056/sigs.1483693PubMed CentralView ArticlePubMedGoogle Scholar
- Shibata M, Katoh H, Sonoda M, Ohkawat H, Shimoyama M, Fukuzawa H, Kaplan A, Ogawa T. Genes essential to sodium-dependent bicarbonate transport in cyanobacteria. J Biol Chem 2002; 277:18658–18664. PubMed doi:10.1074/jbc.M112468200View ArticlePubMedGoogle Scholar
- Gibson J, Pfennig N, Waterbury JB. Chloroherpeton thalassium gen. nov. et spec. nov., a non-filamentous, flexing and gliding green sulfur bacterium. Arch Microbiol 1984; 138:96–101. PubMed doi:10.1007/BF00413007View ArticlePubMedGoogle Scholar
- Frigaard N-U, Dahl C. Sulfur metabolism in phototrophic sulfur bacteria. Advances in Microbial Physiology, 2009; 54: 1–3–200.Google Scholar
- Hanson TE, Tabita FR. A ribulose-1,5-biphosphate carboxylase/oxygenase (RubisCO)-like protein from Chlorobium tepidum that is involved with sulfur metabolism and the response to oxidative stress. Proc Natl Acad Sci USA 2001; 98:4397–4402. PubMed doi:10.1073/pnas.081610398PubMed CentralView ArticlePubMedGoogle Scholar
- Rohwerder T, Sand W. The sulfane sulfur of persulfides is the actual substrate of the sulfur-oxidizing enzymes from Acidithiobacillus and Acidiphillum spp. Microbiology 2003; 149:1699–1710. PubMed doi:10.1099/mic.0.26212-0View ArticlePubMedGoogle Scholar
- Hedderich R, Hamann N, Bennati M. Heterodi-sulfide reductase from methanogenic archaea: a new catalytic role of iron-sulfur cluster. Biol Chem 2005; 386:961–970. PubMed doi:10.1515/BC.2005.112View ArticlePubMedGoogle Scholar
- Mander GJ, Pierik AJ, Huber H, Hedderich R. Two distinct heterodisulfide reductase-like enzymes in the sulfate-reducing archaeon Archaeoglobus profundus. Eur J Biochem 2004; 271:1106–1116. PubMed doi:10.1111/j.1432-1033.2004.04013.xView ArticlePubMedGoogle Scholar
- Quatrini R, Appia-Ayme C, Denis Y, Jedlicki E, Holmes DS, Bonnefoy V. Extending the model for iron and sulfur oxidation in the extreme acidophile Acidithiobacillus ferrooxidans. BMC Genomics 2009; 10:394. PubMed doi:10.1186/1471-2164-10-394PubMed CentralView ArticlePubMedGoogle Scholar
- Mangold S, Valdés J, Holmes DS, Dopson M. Sulfur metabolism in the extreme acidophile Acidithiobacillus caldus. Front Microbiol 2011; 2:1–13. PubMedView ArticleGoogle Scholar
- Kappler U. Bacterial sulfite-oxidizing enzymes. Biochim Biophys Acta 2011; 1807: 1–10.View ArticlePubMedGoogle Scholar
- Oren A. Thermodynamic limits to microbial life at high salt concentrations. [PubMed]. Environ Microbiol 2011; 11:1908–1923. PubMedView ArticleGoogle Scholar
- Biegel E, Müller V. Bacterial Na+-translocating ferridoxins: NAD+ oxidoreductase. Proc Natl Acad Sci USA 2010; 107:18138–18142. PubMed doi:10.1073/pnas.1010318107PubMed CentralView ArticlePubMedGoogle Scholar
- Padan E, Bibi E, Ito M, Krulwich TA. Alkaline pH homeostasis in bacteria: New insights. Biochim Biophys Acta 2005; 1717:67–88. PubMed doi:10.1016/j.bbamem.2005.09.010PubMed CentralView ArticlePubMedGoogle Scholar
- Price GD, Woodger FJ, Badger MR, Howitt SM, Tucker L. Identification of a SulP-type bicarbonate transporter in marine cyanobacteria. Proc Natl Acad Sci USA 2004; 101:18228–18233. PubMed doi:10.1073/pnas.0405211101PubMed CentralView ArticlePubMedGoogle Scholar
- Corratgé-Faillie C, Jabnoune M, Zimmerman S, Very AA, Fizames C, Sentenac H. Potassium and sodium transport in non-animals cells: the Trk/Ktr/HKT transporter system. Cell Mol Life Sci 2010; 67:2511–2532. PubMed doi:10.1007/s00018-010-0317-7View ArticlePubMedGoogle Scholar
- Porter SL, Wadhams GH, Armitage JP. Signal processing in complex Chemotaxis pathways. Nat Rev Microbiol 2011; 9:153–165. PubMed doi:10.1038/nrmicro2505View ArticlePubMedGoogle Scholar
- Pallen MJ, Matzke NJ. From the origin of species to the origin of bacterial flagella. Nat Rev Microbiol 2006; 4:784–790. PubMed doi:10.1038/nrmicro1493View ArticlePubMedGoogle Scholar
- Krulwich TA. Bioenergetic adaptations that support alkaliphily. 2007. In: Physiology and biochemistry of extremophiles. Eds. Gerday C, Glansdorff N. ASM Press, Washington, D.C. pp. 311–329.View ArticleGoogle Scholar
- Krulwich TA. Alkaliphily. 2003. In: Extremophiles (Life under extreme conditions) [Eds. Gerday C, Glansdorff N], in Encyclopedia of Life Support Systems (EOLSS). UNESCO-EOLSS.Google Scholar
- Capy P, Gasperi G, Biémont C, Bazin C. Stress and transposable element: co-evolution or useful parasites? Heredity 2000; 85:101–106. PubMed doi:10.1046/j.1365-2540.2000.00751.xView ArticlePubMedGoogle Scholar
- Versalovic J, de Bruijn FJ, Lupski JR. Genomic fingerprinting of bacteria using repetitive sequence based PCR 9rep-PCR). Meth Cell Mol Biol 1994; 5:25–40.Google Scholar
- Takaichi S, Maoka T, Akimoto N, Sorokin DY, Banciu H, Kuenen JG. Two novel yellow pigments natronochrome and chloronatronochrome from the natrono(alkali)philic sulfur-oxidizing bacterium Thialkalivibrio versutus ALJ 15. Tetrahedron Lett 2004; 45:8303–8305. doi:10.1016/j.tetlet.2004.09.073View ArticleGoogle Scholar