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. 2009 Nov 3;583(21):3455-60.
doi: 10.1016/j.febslet.2009.09.044. Epub 2009 Sep 29.

Translation termination in pyrrolysine-utilizing archaea

Elena Alkalaeva  1 , Boris Eliseev, Alexandre Ambrogelly, Peter Vlasov, Fyodor A Kondrashov, Sharath Gundllapalli, Lyudmila Frolova, Dieter Söll, Lev Kisselev
Affiliations

Translation termination in pyrrolysine-utilizing archaea

Elena Alkalaeva et al. FEBS Lett. .

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.

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Figures

Fig. 1
Fig. 1
Multiple sequence alignment of the N-terminal domains of release factors from different archaea, eukaryotes and bacteria.
Fig. 2
Fig. 2
Release activity of aRF1s from Pyl-utilizing and non-Pyl-utilizing archaea in a reconstituted eukaryotic translation system. Filled circles – activity in the presence of UAA stop codon; empty circles – activity in the presence of UAG stop codon; filled triangles – activity in the presence of UGA stop codon.
Fig. 3
Fig. 3
Phylogenetic tree of aRF1 genes from Methanosarcinaceae, Pyl-utilizing archaeal family, and M. maripaludis aRF1, a non-Pyl-utilizing organism.
See this image and copyright information in PMC

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