Translation termination in pyrrolysine-utilizing archaea.
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.
Alkalaeva
Elena
E
Engelhardt Institute of Molecular Biology, the Russian Academy of Sciences, Vavilov str. 32, Moscow 119991, Russia.
Eliseev
Boris
B
Ambrogelly
Alexandre
A
Vlasov
Peter
P
Kondrashov
Fyodor A
FA
Gundllapalli
Sharath
S
Frolova
Lyudmila
L
Söll
Dieter
D
Kisselev
Lev
L
D000595:Amino Acid Sequence; D019843:Archaeal Proteins / Q000737:chemistry / Q000378:metabolism; D018388:Codon, Terminator / Q000235:genetics / Q000378:metabolism; D020745:Genome, Archaeal; D006801:Humans; D008239:Lysine / Q000031:analogs & derivatives* / Q000378:metabolism; D017019:Methanosarcinaceae / Q000235:genetics* / Q000378:metabolism*; D008969:Molecular Sequence Data; D010454:Peptide Termination Factors / Q000737:chemistry / Q000378:metabolism; D010802:Phylogeny; D014176:Protein Biosynthesis
D019843:Archaeal Proteins; D018388:Codon, Terminator; D010454:Peptide Termination Factors; C456839:pyrrolysine; D008239:Lysine