[The role of the 3'-CCA sequence in the interaction of tRNA(Phe) from E. coli and Thermus thermophilus with homologous phenylalanyl-tRNA-synthetases].
The 3'-CCA end of tRNA(Phe) from E. coli and Thermus thermophilus was modified by stepwise degradation and ligation of the shortened tRNA with different trinucleotides (pUpUpA, (pA)3, (pC)3, (pU)3). Kinetic parameters for the aminoacylation reaction of modified tRNAs have been determined. The role of the 3'-terminal trinucleotide of tRNA(Phe) in tRNA binding and aminoacylation by phenylalanyl-tRNA synthetases from E. coli and Thermus thermophilus is postulated.
Moor
N A
NA
Stepanov
V G
VG
Repkova
M N
MN
Ven'iaminova
A G
AG
Vratskikh
L V
LV
Iamkovoĭ
V I
VI
Motorin
Iu A
IuA
Lavrik
O I
OI
D000215:Acylation; D001665:Binding Sites; D004926:Escherichia coli / Q000201:enzymology / Q000235:genetics*; D007700:Kinetics; D010652:Phenylalanine-tRNA Ligase / Q000378:metabolism*; D012360:RNA, Transfer, Phe / Q000235:genetics / Q000378:metabolism*; D016963:Thermus thermophilus / Q000201:enzymology / Q000235:genetics*
D012360:RNA, Transfer, Phe; D010652:Phenylalanine-tRNA Ligase
Rol' 3'-CCA-posledovatel'nosti vo vzaimodeĭstvii tRNA(Phe) iz E. coli i Thermus thermophilus s gomologichnymi fenilalanil-tRNK-sintetazami.