Phenylalanyl-tRNA synthetase from the archaeon Methanobacterium thermoautotrophicum is an (alphabeta)2 heterotetrameric protein.
Phenylalanyl-tRNA synthetase from the methanogenic archaeon Methanobacterium thermoautotrophicum was purified to apparent homogeneity. The catalytically active enzyme is a heterotetramer composed of two subunits, alpha and beta. N-terminal sequence data were obtained for both subunits and the open reading frames MT770 and MT742 of the genome sequence of M. thermoautotrophicum were identified as coding for these proteins. Two ORFs with similarity to non-archaeal PheRSs alpha-subunits had previously been found in the genome sequence, but these results show that only one of them, MT742, is part of the active PheRS.
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Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, Connecticut 06520-8114 USA.
Vothknecht
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D000595:Amino Acid Sequence; D004591:Electrophoresis, Polyacrylamide Gel; D020745:Genome, Archaeal; D017014:Methanobacterium / Q000201:enzymology* / Q000235:genetics; D008970:Molecular Weight; D016366:Open Reading Frames; D010652:Phenylalanine-tRNA Ligase / Q000737:chemistry* / Q000235:genetics / Q000302:isolation & purification; D020836:Protein Structure, Quaternary
D010652:Phenylalanine-tRNA Ligase