Premium
Alterations at the 3′‐CCA end of Escherichia coli and Thermus thermophilus tRNA Phe do not abolish their acceptor activity
Author(s) -
Moor N.A.,
Repkova M.N.,
Yamkovoy V.I.,
Lavrik O.I.
Publication year - 1994
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(94)00841-8
Subject(s) - thermus thermophilus , escherichia coli , transfer rna , chemistry , acceptor , biochemistry , rna , physics , gene , condensed matter physics
The 3′‐CCA end of tRNA Phe from Escherichia coli and Thermus thermophilus was changed to AAA, CCC, UUU and UUA by the stepwise degradation procedure of the 3′‐CCA end of tRNA Phe followed by the ligation with oligoribotrinucleotides. Substrate activity of tRNAU Phe UUA and tRNA Phe CCC in tRNA aminoacylation was shown. tRNA Phe AAA is a bad substrate for E. coli and Th. thermophilus phenylalanyl‐tRNA synthetases. tRNA Phe UUU has no detectable activity in tRNA aminoacylation. Therefore the nature of the 3′‐end of tRNA Phe plays an important role in tRNA binding and its substrate efficiency. Nevertheless the CCA sequence at the 3′‐end of tRNA Phe does not seem to be an absolute requirement for tRNA aminoacylation.