Phenylalanyl-tRNA synthetase from the archaebacterium Methanosarcina barkeri.

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.