Selenoprotein synthesis in archaea

Research output: Contribution to journalShort survey/ReviewContributedpeer-review

Contributors

  • Michael Rother - , Ludwig Maximilian University of Munich (Author)
  • Armin Resch - , Ludwig Maximilian University of Munich (Author)
  • Reinhard Wilting - , Ludwig Maximilian University of Munich, Novo Nordisk Foundation (Author)
  • August Böck - , Ludwig Maximilian University of Munich (Author)

Abstract

The availability of the genome sequences from several archaea has facilitated the identification of the encoded selenoproteins and also of most of the components of the machinery for selenocysteine biosynthesis and insertion. Until now, selenoproteins have been identified solely in species of the genera Methanococcus (M.) and Methanopyrus. Apart from selenophosphate synthetase, they include only enzymes with a function in energy metabolism. Like in bacteria and eukarya, selenocysteine insertion is directed by a UGA codon in the mRNA and involves the action of a specific tRNA and of selenophosphate as the selenium donor. Major differences to the bacterial system, however, are that no homolog for the bacterial selenocysteine synthase was found and, especially, that the SECIS element of the mRNA is positioned in the 3′ nontranslated region. The characterisation of a homolog for the bacterial SelB protein showed that it does not bind to the SECIS element necessitating the activity of at least a second protein. The use of the genetic system of M. maripaludis allowed the heterologous expression of a selenoprotein gene from M. jannaschii and will facilitate the elucidation of the mechanism of the selenocysteine insertion process in the future.

Details

Original languageEnglish
Pages (from-to)75-83
Number of pages9
JournalBioFactors
Volume14
Issue number1-4
Publication statusPublished - 2001
Peer-reviewedYes
Externally publishedYes

External IDs

PubMed 11568443

Keywords

Keywords

  • Archaea, Methanococcus sp, Methanopyrus sp, SECIS, SelB, Selenoprotein synthesis