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.
Engelhardt Institute of Molecular Biology, the Russian Academy of Sciences, Vavilov str. 32, Moscow 119991, Russia.
Elena
E
Alkalaeva
Boris
B
Eliseev
Alexandre
A
Ambrogelly
Peter
P
Vlasov
Fyodor A
FA
Kondrashov
Sharath
S
Gundllapalli
Lyudmila
L
Frolova
Dieter
D
Söll
Lev
L
Kisselev
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