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

Siebers, B., Zaparty, M., Raddatz, G., Tjaden, B., Albers, S., Bell, S., et al. (2011). The Complete Genome Sequence of Thermoproteus tenax: A Physiologically Versatile Member of the Crenarchaeota. PLoS One, 6(10): e24222. doi:10.1371/journal.pone.0024222.

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Siebers, B, Autor
Zaparty, M, Autor
Raddatz, G1, Autor           
Tjaden, B, Autor
Albers, SV, Autor
Bell, SD, Autor
Blombach, F, Autor
Kletzin, A, Autor
Kyrpides, N, Autor
Lanz, C, Autor           
Plagens, A, Autor
Rampp, M, Autor
Rosinus, A, Autor           
von Jan, M, Autor
Makarova, KS, Autor
Klenk, HP, Autor
Schuster, SC, Autor           
Hensel, R, Autor
Affiliations:
1Department High-Field Magnetic Resonance, Max Planck Institute for Biological Cybernetics, Max Planck Society, ou_1497796              

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 Zusammenfassung: Here, we report on the complete genome sequence of the hyperthermophilic Crenarchaeum Thermoproteus tenax (strain Kra1, 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°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/H₂) 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 A₀A₁-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.

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Sprache(n): eng - English
 Datum: 2011-10
 Publikationsstatus: Erschienen
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 Ort, Verlag, Ausgabe: -
 Inhaltsverzeichnis: -
 Art der Begutachtung: Expertenbegutachtung
 Identifikatoren: DOI: 10.1371/journal.pone.0024222
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Titel: PLoS One
  Kurztitel : PLoS One
Genre der Quelle: Zeitschrift
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Ort, Verlag, Ausgabe: San Francisco, CA : Public Library of Science
Seiten: 13 Band / Heft: 6 (10) Artikelnummer: e24222 Start- / Endseite: - Identifikator: ISSN: 1932-6203
CoNE: https://pure.mpg.de/cone/journals/resource/1000000000277850