UCL Discovery
UCL home » Library Services » Electronic resources » UCL Discovery

The Complete Genome Sequence of Thermoproteus tenax: A Physiologically Versatile Member of the Crenarchaeota

Siebers, B; Zaparty, M; Raddatz, G; Tjaden, B; Albers, SV; Bell, SD; Blombach, F; ... Hensel, R; + view all (2011) The Complete Genome Sequence of Thermoproteus tenax: A Physiologically Versatile Member of the Crenarchaeota. PLOS ONE , 6 (10) , Article e24222. 10.1371/journal.pone.0024222. Green open access

[thumbnail of 1326366.pdf]
Preview
PDF
1326366.pdf

Download (479kB)

Abstract

Here, we report on the complete genome sequence of the hyperthermophilic Crenarchaeum Thermoproteus tenax (strain Kra 1, DSM 2078(T)) a type strain of the crenarchaeotal order Thermoproteales. Its circular 1.84-megabase genome harbors no extrachromosomal elements and 2,051 open reading frames are identified, covering 90.6% of the complete sequence, which represents a high coding density. Derived from the gene content, T. tenax is a representative member of the Crenarchaeota. The organism is strictly anaerobic and sulfur-dependent with optimal growth at 86 degrees C and pH 5.6. One particular feature is the great metabolic versatility, which is not accompanied by a distinct increase of genome size or information density as compared to other Crenarchaeota. T. tenax is able to grow chemolithoautotrophically (CO2/H-2) as well as chemoorganoheterotrophically in presence of various organic substrates. All pathways for synthesizing the 20 proteinogenic amino acids are present. In addition, two presumably complete gene sets for NADH:quinone oxidoreductase (complex I) were identified in the genome and there is evidence that either NADH or reduced ferredoxin might serve as electron donor. Beside the typical archaeal A(0)A(1)-ATP synthase, a membrane-bound pyrophosphatase is found, which might contribute to energy conservation. Surprisingly, all genes required for dissimilatory sulfate reduction are present, which is confirmed by growth experiments. Mentionable is furthermore, the presence of two proteins (ParA family ATPase, actin-like protein) that might be involved in cell division in Thermoproteales, where the ESCRT system is absent, and of genes involved in genetic competence (DprA, ComF) that is so far unique within Archaea.

Type: Article
Title: The Complete Genome Sequence of Thermoproteus tenax: A Physiologically Versatile Member of the Crenarchaeota
Open access status: An open access version is available from UCL Discovery
DOI: 10.1371/journal.pone.0024222
Publisher version: http://dx.doi.org/10.1371/journal.pone.0024222
Language: English
Additional information: This is an open-access article, free of all copyright, and may be freely reproduced, distributed, transmitted, modified, built upon, or otherwise used by anyone for any lawful purpose. The work is made available under the Creative Commons CC0 public domain dedication. This work was supported by the University of Duisburg-Essen (Germany) and the Deutsche Forschungsgemeinschaft (DFG; SPP1112) by grant He1238/16-2, 3 (Dr. Hensel). Dr. Albers was supported by a VIDI grant of the Dutch Science Organization (NWO) and intramural funds of the Max Planck society. The funders had no role in study design, data collection and analysis, decision to publish, or preparation of the manuscript.
Keywords: CENTRAL CARBOHYDRATE-METABOLISM, RIBULOSE MONOPHOSPHATE PATHWAY, TRANSFER-RNA GENES, METHANOBACTERIUM-THERMOAUTOTROPHICUM, SULFOLOBUS-SOLFATARICUS, BINDING-PROTEIN, PYROBACULUM-AEROPHILUM, IGNICOCCUS-HOSPITALIS, ACIDIANUS-AMBIVALENS, DNA-REPLICATION
UCL classification: UCL
UCL > Provost and Vice Provost Offices > School of Life and Medical Sciences
UCL > Provost and Vice Provost Offices > School of Life and Medical Sciences > Faculty of Life Sciences
UCL > Provost and Vice Provost Offices > School of Life and Medical Sciences > Faculty of Life Sciences > Div of Biosciences
UCL > Provost and Vice Provost Offices > School of Life and Medical Sciences > Faculty of Life Sciences > Div of Biosciences > Structural and Molecular Biology
URI: https://discovery.ucl.ac.uk/id/eprint/1326366
Downloads since deposit
0Downloads
Download activity - last month
Download activity - last 12 months
Downloads by country - last 12 months

Archive Staff Only

View Item View Item