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FEBS Lett. 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.

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1
Engelhardt Institute of Molecular Biology, the Russian Academy of Sciences, Vavilov str. 32, Moscow 119991, Russia.

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.

PMID:
19796638
PMCID:
PMC2857517
DOI:
10.1016/j.febslet.2009.09.044
[Indexed for MEDLINE]
Free PMC Article
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