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1

Wirsen, C. O., T. Brinkhoff, J. Kuever, G. Muyzer, S. Molyneaux, and H. W. Jannasch. "Comparison of a New Thiomicrospira Strain from the Mid-Atlantic Ridge with Known Hydrothermal Vent Isolates." Applied and Environmental Microbiology 64, no. 10 (October 1, 1998): 4057–59. http://dx.doi.org/10.1128/aem.64.10.4057-4059.1998.

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ABSTRACT A new autotrophic Thiomicrospira strain, MA-3, was isolated from the surface of a polymetal sulfide deposit collected at a Mid-Atlantic Ridge hydrothermal vent site. The DNA homology among three vent isolates, Thiomicrospira crunogena,Thiomicrospira sp. strain L-12, andThiomicrospira sp. strain MA-3, was 99.3% or higher, grouping them as the same species, T. crunogena (type strain, ATCC 35932). The fact that T. crunogena andThiomicrospira sp. strain L-12 were isolated from Pacific vent sites demonstrates a cosmopolitan distribution of this species.
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2

Tourova, Tatjana P., Elizaveta M. Spiridonova, Ivan A. Berg, Boris B. Kuznetsov, and Dimitry Yu Sorokin. "Occurrence, phylogeny and evolution of ribulose-1,5-bisphosphate carboxylase/oxygenase genes in obligately chemolithoautotrophic sulfur-oxidizing bacteria of the genera Thiomicrospira and Thioalkalimicrobium." Microbiology 152, no. 7 (July 1, 2006): 2159–69. http://dx.doi.org/10.1099/mic.0.28699-0.

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The occurrence of the different genes encoding ribulose-1,5-bisphosphate carboxylase/oxygenase (RubisCO), the key enzyme of the Calvin–Benson–Bassham cycle of autotrophic CO2 fixation, was investigated in the members of the genus Thiomicrospira and the relative genus Thioalkalimicrobium, all obligately chemolithoautotrophic sulfur-oxidizing Gammaproteobacteria. The cbbL gene encoding the ‘green-like’ form I RubisCO large subunit was found in all analysed species, while the cbbM gene encoding form II RubisCO was present only in Thiomicrospira species. Furthermore, species belonging to the Thiomicrospira crunogena 16S rRNA-based phylogenetic cluster also possessed two genes of green-like form I RubisCO, cbbL-1 and cbbL-2. Both 16S-rRNA- and cbbL-based phylogenies of the Thiomicrospira–Thioalkalimicrobium–Hydrogenovibrio group were congruent, thus supporting its monophyletic origin. On the other hand, it also supports the necessity for taxonomy reorganization of this group into a new family with four genera.
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3

Sorokin, Dimitry Yu, Tatjana P. Tourova, Tatjana V. Kolganova, Elizaveta M. Spiridonova, Ivan A. Berg, and Gerard Muyzer. "Thiomicrospira halophila sp. nov., a moderately halophilic, obligately chemolithoautotrophic, sulfur-oxidizing bacterium from hypersaline lakes." International Journal of Systematic and Evolutionary Microbiology 56, no. 10 (October 1, 2006): 2375–80. http://dx.doi.org/10.1099/ijs.0.64445-0.

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Enrichments at 2 M NaCl and pH 7.5–8, with thiosulfate or sulfide as electron donor, inoculated with sediments from hypersaline chloride–sulfate lakes of the Kulunda Steppe (Altai, Russia) resulted in the domination of two different groups of moderately halophilic, chemolithoautotrophic, sulfur-oxidizing bacteria. Under fully aerobic conditions with thiosulfate, bacteria belonging to the genus Halothiobacillus dominated while, under microaerophilic conditions, a highly motile, short vibrio-shaped phenotype outcompeted the halothiobacilli. Three genetically and phenotypically highly similar vibrio-shaped isolates were obtained in pure culture and one of them, strain HL 5T, was identified as a member of the Thiomicrospira crunogena cluster by 16S rRNA gene sequencing. The new isolates were able to grow with thiosulfate as electron donor within a broad salinity range from 0.5 to 3.5 M NaCl with an optimum at 1.5 M and within a pH range from 6.5 to 8.5 with an optimum at pH 7.5–7.8. Comparative analysis of ribulose-1,5-bisphosphate carboxylase/oxygenase (RuBisCO) gene sequences demonstrated that strain HL 5T possessed two genes, cbbL-1 and cbbL-2, of the form I RuBisCO and a cbbM gene of the form II RuBisCO, similar to the other members of the Thiomicrospira crunogena cluster. On the basis of phenotypic and genetic comparison, the new halophilic isolates are proposed to be placed into a novel species, Thiomicrospira halophila sp. nov. (type strain HL 5T=DSM 15072T=UNIQEM U 221T).
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4

Dobrinski, Kimberly P., Amanda J. Boller, and Kathleen M. Scott. "Expression and Function of Four Carbonic Anhydrase Homologs in the Deep-Sea Chemolithoautotroph Thiomicrospira crunogena." Applied and Environmental Microbiology 76, no. 11 (April 16, 2010): 3561–67. http://dx.doi.org/10.1128/aem.00064-10.

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ABSTRACT The hydrothermal vent chemolithoautotroph Thiomicrospira crunogena grows rapidly in the presence of low concentrations of dissolved inorganic carbon (DIC) (= CO2 + HCO3 − + CO3 −2). Its genome encodes α-carbonic anhydrase (α-CA), β-CA, carboxysomal β-like CA (CsoSCA), and a protein distantly related to γ-CA. The purposes of this work were to characterize the gene products, determine whether they were differentially expressed, and identify those that are necessary for DIC uptake and fixation. When expressed in Escherichia coli, CA activity was detectable for α-CA, β-CA, and CsoSCA but not for the γ-CA-like protein. α-CA and CsoSCA but not β-CA were inhibited by sulfonamide inhibitors. CsoSCA was also inhibited by dithiothreitol. When grown under DIC limitation in chemostats, T. crunogena transcribed csoSCA more frequently than when ammonia limited, while genes encoding α-CA and β-CA were not differentially transcribed under these conditions. Cell extracts from T. crunogena grown under both DIC- and ammonia-limited conditions had CA activity that was strongly inhibited by sulfonamides, though extracts from nitrogen-limited cells had some CA activity that was resistant, perhaps due to a higher level of β-CA activity. Based on predictions from the SignalP software program, subcellular location when expressed in E. coli, and carbonic anhydrase assays conducted on intact T. crunogena cells, α-CA is located in the periplasm. However, inhibition of α-CA by acetazolamide had only a minor impact on rates of DIC uptake or fixation. Conversely, inhibition of CsoSCA with ethoxyzolamide inhibited carbon fixation but not DIC uptake, consistent with this enzyme functioning to facilitate DIC interconversion and fixation within carboxysomes.
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5

Takai, Ken, Hisako Hirayama, Tatsunori Nakagawa, Yohey Suzuki, Kenneth H. Nealson, and Koki Horikoshi. "Thiomicrospira thermophila sp. nov., a novel microaerobic, thermotolerant, sulfur-oxidizing chemolithomixotroph isolated from a deep-sea hydrothermal fumarole in the TOTO caldera, Mariana Arc, Western Pacific." International Journal of Systematic and Evolutionary Microbiology 54, no. 6 (November 1, 2004): 2325–33. http://dx.doi.org/10.1099/ijs.0.63284-0.

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A novel thermotolerant bacterium, designated strain I78T, was isolated from a self-temperature-recording in situ colonization system deployed in a hydrothermal diffusing flow (maximal temperature 78 °C) at the TOTO caldera in the Mariana Arc, Western Pacific. Cells were highly motile curved rods with a single polar flagellum. Growth was observed at 15–55 °C (optimum 35–40 °C; 60 min doubling time) and pH 5·0–8·0 (optimum pH 6·0). The isolate was a microaerobic chemolithomixotroph capable of using thiosulfate, elemental sulfur or sulfide as the sole energy source, and molecular oxygen as the sole electron acceptor. The isolate was able to grow chemolithoautotrophically with carbon dioxide. Various organic substrates such as complex proteinaceous compounds, carbohydrates, organic acids, amino acids and sugars could also support growth as the carbon source instead of carbon dioxide with sulfur oxidation. The G+C content of the genomic DNA was 43·8 mol%. Phylogenetic analysis based on 16S rRNA gene sequences indicated that the isolate belonged to the genus Thiomicrospira and was most closely related to Thiomicrospira crunogena strain TH-55T and Thiomicrospira sp. strain L-12, while DNA–DNA hybridization demonstrated that the novel isolate could be genetically differentiated from previously described strains of Thiomicrospira. On the basis of its physiological and molecular properties the isolate is representative of a novel Thiomicrospira species, for which the name Thiomicrospira thermophila sp. nov. is proposed (type strain, I78T=JCM 12397T=DSM 16397T).
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6

Scott, Kathleen M., Stefan M. Sievert, Fereniki N. Abril, Lois A. Ball, Chantell J. Barrett, Rodrigo A. Blake, Amanda J. Boller, et al. "The Genome of Deep-Sea Vent Chemolithoautotroph Thiomicrospira crunogena XCL-2." PLoS Biology 4, no. 12 (November 14, 2006): e383. http://dx.doi.org/10.1371/journal.pbio.0040383.

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7

Dobrinski, Kimberly P., Dana L. Longo, and Kathleen M. Scott. "The Carbon-Concentrating Mechanism of the Hydrothermal Vent Chemolithoautotroph Thiomicrospira crunogena." Journal of Bacteriology 187, no. 16 (August 15, 2005): 5761–66. http://dx.doi.org/10.1128/jb.187.16.5761-5766.2005.

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8

Dobrinski, K. P., S. A. Enkemann, S. J. Yoder, E. Haller, and K. M. Scott. "Transcriptional Response of the Sulfur Chemolithoautotroph Thiomicrospira crunogena to Dissolved Inorganic Carbon Limitation." Journal of Bacteriology 194, no. 8 (February 10, 2012): 2074–81. http://dx.doi.org/10.1128/jb.06504-11.

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9

JANNASCH, H. W., C. O. WIRSEN, D. C. NELSON, and L. A. ROBERTSON. "Thiomicrospira crunogena sp. nov., a Colorless, Sulfur-Oxidizing Bacterium from a Deep-Sea Hydrothermal Vent." International Journal of Systematic Bacteriology 35, no. 4 (October 1, 1985): 422–24. http://dx.doi.org/10.1099/00207713-35-4-422.

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10

Javor, Barbara J., David B. Wilmot, and Russell D. Vetter. "pH-Dependent metabolism of thiosulfate and sulfur globules in the chemolithotrophic marine bacterium Thiomicrospira crunogena." Archives of Microbiology 154, no. 3 (August 1990): 231–38. http://dx.doi.org/10.1007/bf00248960.

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11

Mahon, Brian P., Natalia A. Díaz-Torres, Melissa A. Pinard, Chingkuang Tu, David N. Silverman, Kathleen M. Scott, and Robert McKenna. "Activity and anion inhibition studies of the α-carbonic anhydrase from Thiomicrospira crunogena XCL-2 Gammaproteobacterium." Bioorganic & Medicinal Chemistry Letters 25, no. 21 (November 2015): 4937–40. http://dx.doi.org/10.1016/j.bmcl.2015.05.001.

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12

Vullo, Daniela, Avni Bhatt, Brian P. Mahon, Robert McKenna, and Claudiu T. Supuran. "Sulfonamide inhibition studies of the α-carbonic anhydrase from the gammaproteobacterium Thiomicrospira crunogena XCL-2, TcruCA." Bioorganic & Medicinal Chemistry Letters 26, no. 2 (January 2016): 401–5. http://dx.doi.org/10.1016/j.bmcl.2015.11.104.

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13

Menning, Kristy J., Balaraj B. Menon, Gordon Fox, and Kathleen M. Scott. "Dissolved inorganic carbon uptake in Thiomicrospira crunogena XCL-2 is Δp- and ATP-sensitive and enhances RubisCO-mediated carbon fixation." Archives of Microbiology 198, no. 2 (November 18, 2015): 149–59. http://dx.doi.org/10.1007/s00203-015-1172-6.

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14

Mahon, Brian P., Avni Bhatt, Daniela Vullo, Claudiu T. Supuran, and Robert McKenna. "Exploration of anionic inhibition of the α-carbonic anhydrase from Thiomicrospira crunogena XCL-2 gammaproteobacterium: A potential bio-catalytic agent for industrial CO2 removal." Chemical Engineering Science 138 (December 2015): 575–80. http://dx.doi.org/10.1016/j.ces.2015.07.030.

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15

Mangiapia, Mary, Terry-René W. Brown, Dale Chaput, Edward Haller, Tara L. Harmer, Zahra Hashemy, Ryan Keeley, et al. "Proteomic and Mutant Analysis of the CO2 Concentrating Mechanism of Hydrothermal Vent Chemolithoautotroph Thiomicrospira crunogena." Journal of Bacteriology 199, no. 7 (January 23, 2017). http://dx.doi.org/10.1128/jb.00871-16.

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ABSTRACT Many autotrophic microorganisms are likely to adapt to scarcity in dissolved inorganic carbon (DIC; CO2 + HCO3 − + CO3 2−) with CO2 concentrating mechanisms (CCM) that actively transport DIC across the cell membrane to facilitate carbon fixation. Surprisingly, DIC transport has been well studied among cyanobacteria and microalgae only. The deep-sea vent gammaproteobacterial chemolithoautotroph Thiomicrospira crunogena has a low-DIC inducible CCM, though the mechanism for uptake is unclear, as homologs to cyanobacterial transporters are absent. To identify the components of this CCM, proteomes of T. crunogena cultivated under low- and high-DIC conditions were compared. Fourteen proteins, including those comprising carboxysomes, were at least 4-fold more abundant under low-DIC conditions. One of these proteins was encoded by Tcr_0854; strains carrying mutated copies of this gene, as well as the adjacent Tcr_0853, required elevated DIC for growth. Strains carrying mutated copies of Tcr_0853 and Tcr_0854 overexpressed carboxysomes and had diminished ability to accumulate intracellular DIC. Based on reverse transcription (RT)-PCR, Tcr_0853 and Tcr_0854 were cotranscribed and upregulated under low-DIC conditions. The Tcr_0853-encoded protein was predicted to have 13 transmembrane helices. Given the mutant phenotypes described above, Tcr_0853 and Tcr_0854 may encode a two-subunit DIC transporter that belongs to a previously undescribed transporter family, though it is widespread among autotrophs from multiple phyla. IMPORTANCE DIC uptake and fixation by autotrophs are the primary input of inorganic carbon into the biosphere. The mechanism for dissolved inorganic carbon uptake has been characterized only for cyanobacteria despite the importance of DIC uptake by autotrophic microorganisms from many phyla among the Bacteria and Archaea. In this work, proteins necessary for dissolved inorganic carbon utilization in the deep-sea vent chemolithoautotroph T. crunogena were identified, and two of these may be able to form a novel transporter. Homologs of these proteins are present in 14 phyla in Bacteria and also in one phylum of Archaea, the Euryarchaeota. Many organisms carrying these homologs are autotrophs, suggesting a role in facilitating dissolved inorganic carbon uptake and fixation well beyond the genus Thiomicrospira.
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16

McGill, Susan E., and Daniel Barker. "Comparison of the protein-coding genomes of three deep-sea, sulfur-oxidising bacteria: “Candidatus Ruthia magnifica”, “Candidatus Vesicomyosocius okutanii” and Thiomicrospira crunogena." BMC Research Notes 10, no. 1 (July 20, 2017). http://dx.doi.org/10.1186/s13104-017-2598-5.

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