Phenylalanyl-tRNA synthetase from Thermus thermophilus can attach two molecules of phenylalanine to tRNA(Phe).
Phenylalanyl-tRNA synthetase from the extreme thermophilic bacterium Thermus thermophilus can incorporate more than one molecule of phenylalanine into the tRNA(Phe). It is shown that the 'hyperaminoacylated' tRNA(Phe) is the bis-2',3'-O-phenylalanyl-tRNA(Phe), and its formation is typical for the thermophilic enzyme but does not occur for E. coli phenylalanyl-tRNA synthetase under the same conditions.
Stepanov
V G
VG
Novosibirsk Institute of Bioorganic Chemistry, Siberian Division, Russian Academy of Sciences.
Moor
N A
NA
Ankilova
V N
VN
Lavrik
O I
OI
D001345:Autoradiography / Q000379:methods; D002250:Carbon Radioisotopes; D002855:Chromatography, Thin Layer; D007700:Kinetics; D010652:Phenylalanine-tRNA Ligase / Q000378:metabolism*; D011485:Protein Binding; D012360:RNA, Transfer, Phe / Q000302:isolation & purification / Q000378:metabolism*; D011865:Radioisotope Dilution Technique; D016963:Thermus thermophilus / Q000201:enzymology*
D002250:Carbon Radioisotopes; D012360:RNA, Transfer, Phe; D010652:Phenylalanine-tRNA Ligase