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The genome sequence of the thermoacidophilic scavenger Thermoplasma acidophilum

Author

Listed:
  • Andreas Ruepp

    (Max-Planck-Institut für Biochemie)

  • Werner Graml

    (Max-Planck-Institut für Biochemie)

  • Martha-Leticia Santos-Martinez

    (Max-Planck-Institut für Biochemie)

  • Kristin K. Koretke

    (Bioinformatics, Smith Kline Beecham Pharmaceuticals)

  • Craig Volker

    (Bioinformatics, Smith Kline Beecham Pharmaceuticals)

  • H. Werner Mewes

    (GSF-Forschungszentrum für Umwelt und Gesundheit, Munich Information Center for Protein Sequences)

  • Dmitrij Frishman

    (GSF-Forschungszentrum für Umwelt und Gesundheit, Munich Information Center for Protein Sequences)

  • Susanne Stocker

    (GSF-Forschungszentrum für Umwelt und Gesundheit, Munich Information Center for Protein Sequences)

  • Andrei N. Lupas

    (Bioinformatics, Smith Kline Beecham Pharmaceuticals)

  • Wolfgang Baumeister

    (Max-Planck-Institut für Biochemie)

Abstract

Thermoplasma acidophilum is a thermoacidophilic archaeon that thrives at 59 °C and pH 2, which was isolated from self-heating coal refuse piles and solfatara fields1,2. Species of the genus Thermoplasma do not possess a rigid cell wall, but are only delimited by a plasma membrane. Many macromolecular assemblies from Thermoplasma , primarily proteases and chaperones, have been pivotal in elucidating the structure and function of their more complex eukaryotic homologues3,4. Our interest in protein folding and degradation led us to seek a more complete representation of the proteins involved in these pathways by determining the genome sequence of the organism. Here we have sequenced the 1,564,905-base-pair genome in just 7,855 sequencing reactions by using a new strategy. The 1,509 open reading frames identify Thermoplasma as a typical euryarchaeon with a substantial complement of bacteria-related genes; however, evidence indicates that there has been much lateral gene transfer between Thermoplasma and Sulfolobus solfataricus, a phylogenetically distant crenarchaeon inhabiting the same environment. At least 252 open reading frames, including a complete protein degradation pathway and various transport proteins, resemble Sulfolobus proteins most closely.

Suggested Citation

  • Andreas Ruepp & Werner Graml & Martha-Leticia Santos-Martinez & Kristin K. Koretke & Craig Volker & H. Werner Mewes & Dmitrij Frishman & Susanne Stocker & Andrei N. Lupas & Wolfgang Baumeister, 2000. "The genome sequence of the thermoacidophilic scavenger Thermoplasma acidophilum," Nature, Nature, vol. 407(6803), pages 508-513, September.
  • Handle: RePEc:nat:nature:v:407:y:2000:i:6803:d:10.1038_35035069
    DOI: 10.1038/35035069
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    Cited by:

    1. Fernando Maiello & Gloria Gallo & Camila Coelho & Fernanda Sucharski & Leon Hardy & Martin Würtele, 2020. "Crystal structure of Thermus thermophilus methylenetetrahydrofolate dehydrogenase and determinants of thermostability," PLOS ONE, Public Library of Science, vol. 15(5), pages 1-19, May.

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