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Phenylalanyl-tRNA synthetase from the archaebacterium Methanosarcina barkeri

Rauhut, R.; Gabius, H.J.; Kühn, W.; Cramer, F.

Journal of Biological Chemistry 259(10): 6340-6345

1984

ISSN/ISBN: 0021-9258
PMID: 6373755
Accession: 018050770
Phenylalanyl-tRNA synthetase from the archaebacterium Methanosarcina barkeri was purified 1620-fold with 24% overall yield. It appears to be a tetrameric enzyme with a molecular mass of 270 kDa, as determined by gel filtration, with a subunit structure of alpha 2 beta 2 (alpha = 63 kDa, beta = 70 kDa), as determined by sodium dodecyl sulfate gel electrophoresis. No conservation of common antigenic determinants is noted with polyclonal antibodies raised against the enzymes of Escherichia coli, yeast, and hen liver. Heterologous aminoacylation of tRNA with high selectivity for archaebacterial tRNA and substrate properties of ATP analogues reveals a unique pattern, reflecting the supposed genealogical difference between the urkingdoms of archaebacteria, eubacteria, and eukaryotes.

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Related References

Rauhut, R.; Gabius, H.J.; Engelhardt, R. 1985: Archaebacterial phenylalanyl-tRNA synthetase. Accuracy of the phenylalanyl-tRNA synthetase from the archaebacterium Methanosarcina barkeri, Zn(II)-dependent synthesis of diadenosine 5',5'''-P1,P4-tetraphosphate, and immunological relationship of phenylalanyl-tRNA synthetases from different urkingdoms Journal of Biological Chemistry 260: 2-7
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Schwark, D.G.; Schmitt, M.A.; Fisk, J.D. 2021: Directed Evolution of the Methanosarcina barkeri Pyrrolysyl tRNA/aminoacyl tRNA Synthetase Pair for Rapid Evaluation of Sense Codon Reassignment Potential International Journal of Molecular Sciences 22(2)
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Bartmann, P.; Hanke, T.; Hammer-Raber, B.; Holler, E. 1974: Selective labelling of the beta-subunit of L-phenylalanyl-tRNA synthetase from E. coli with N-bromoacetyl-L-phenylalanyl-tRNA Phe Biochemical and Biophysical Research Communications 60(2): 743-747
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