Translation termination in pyrrolysine-utilizing archaea |
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Authors: | Elena Alkalaeva,Alexandre Ambrogelly,Fyodor A. Kondrashov,Lyudmila Frolova,Dieter Sö ll,Lev Kisselev |
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Affiliation: | a Engelhardt Institute of Molecular Biology, the Russian Academy of Sciences, Vavilov str. 32, Moscow 119991, Russia b Bioinformatics and Genomics Programme, Centre for Genomic Regulation, 08003 Barcelona, Spain c Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT 06520-8114, USA d Department of Chemistry, Yale University, New Haven, CT 06520-8114, USA |
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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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Keywords: | Translation termination Archeon Pyrrolysine-utilizing archea aRF1 Polypeptide release factor |
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