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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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 Creators:
Siebers, B, Author
Zaparty, M, Author
Raddatz, G, Author           
Tjaden, B, Author
Albers, SV, Author
Bell, SD, Author
Blombach, F, Author
Kletzin, A, Author
Kyrpides, N, Author
Lanz, C1, Author           
Plagens, A, Author
Rampp, M, Author
Rosinus, A1, Author           
von Jan, M, Author
Makarova, KS, Author
Klenk, HP, Author
Schuster, SC, Author           
Hensel, R, Author
Affiliations:
1Genome Center, Max Planck Institute for Developmental Biology, Max Planck Society, ou_3394560              

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 Abstract: 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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Language(s): eng - English
 Dates: 2011-10
 Publication Status: Issued
 Pages: -
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: DOI: 10.1371/journal.pone.0024222
PMID: 22003381
 Degree: -

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Title: PLoS One
  Abbreviation : PLoS One
Source Genre: Journal
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Publ. Info: San Francisco, CA : Public Library of Science
Pages: 13 Volume / Issue: 6 (10) Sequence Number: e24222 Start / End Page: - Identifier: ISSN: 1932-6203
CoNE: https://pure.mpg.de/cone/journals/resource/1000000000277850