FEBS Letters
Volume 583, Issue 21 , Pages 3455-3460, 3 November 2009

Translation termination in pyrrolysine-utilizing archaea

Edited by Michael Ibba

In memory of Lev Kisselev

  • Elena Alkalaeva

      Affiliations

    • Engelhardt Institute of Molecular Biology, the Russian Academy of Sciences, Vavilov str. 32, Moscow 119991, Russia
  • ,
  • Boris Eliseev

      Affiliations

    • Engelhardt Institute of Molecular Biology, the Russian Academy of Sciences, Vavilov str. 32, Moscow 119991, Russia
  • ,
  • Alexandre Ambrogelly

      Affiliations

    • Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT 06520-8114, USA
  • ,
  • Peter Vlasov

      Affiliations

    • Engelhardt Institute of Molecular Biology, the Russian Academy of Sciences, Vavilov str. 32, Moscow 119991, Russia
  • ,
  • Fyodor A. Kondrashov

      Affiliations

    • Bioinformatics and Genomics Programme, Centre for Genomic Regulation, 08003 Barcelona, Spain
  • ,
  • Sharath Gundllapalli

      Affiliations

    • Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT 06520-8114, USA
  • ,
  • Lyudmila Frolova

      Affiliations

    • Engelhardt Institute of Molecular Biology, the Russian Academy of Sciences, Vavilov str. 32, Moscow 119991, Russia
    • Corresponding Author InformationCorresponding author. Fax: +7 (499) 135 14 05.
  • ,
  • Dieter Söll

      Affiliations

    • Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT 06520-8114, USA
    • Department of Chemistry, Yale University, New Haven, CT 06520-8114, USA
  • ,
  • Lev Kisselev

      Affiliations

    • Engelhardt Institute of Molecular Biology, the Russian Academy of Sciences, Vavilov str. 32, Moscow 119991, Russia
    • Deceased April 12, 2008.

Received 28 August 2009; accepted 24 September 2009. published online 30 September 2009.

Abstract 

Although some data link archaeal and eukaryotic translation, the overall mechanism of protein synthesis in archaea remains largely obscure. Both archaeal (aRF1) and eukaryotic (eRF1) single release factors recognize all three stop codons. The archaeal genus Methanosarcinaceae contains two aRF1 homologs, and also uses the UAG stop to encode the 22nd amino acid, pyrrolysine. Here we provide an analysis of the last stage of archaeal translation in pyrrolysine-utilizing species. We demonstrated that only one of two Methanosarcina barkeri aRF1 homologs possesses activity and recognizes all three stop codons. The second aRF1 homolog may have another unknown function. The mechanism of pyrrolysine incorporation in the Methanosarcinaceae is discussed.

Keywords: Translation termination, Archeon, Pyrrolysine-utilizing archea, aRF1, Polypeptide release factor

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PII: S0014-5793(09)00744-3

doi:10.1016/j.febslet.2009.09.044

FEBS Letters
Volume 583, Issue 21 , Pages 3455-3460, 3 November 2009