Premium
Modification of the amino acid acceptor stem of E. coli tRNA f Met by ligation of chemically synthesized ribooligonucleotides
Author(s) -
Doi Takefumi,
Morioka Hiroshi,
Matsugi Jitsuhiro,
Ohtsuka Eiko,
Ikehara Mono
Publication year - 1985
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(85)80441-5
Subject(s) - trimer , random hexamer , chemistry , acceptor , formylation , nuclease , methionine , transfer rna , stereochemistry , amino acid , serine , aminoacyl trna synthetase , biochemistry , dna , enzyme , rna , organic chemistry , dimer , catalysis , physics , condensed matter physics , gene
The single‐stranged region of the amino acid acceptor stem corresponding to the 3'‐end of E. coli tRNA Met f was replaced by ligation of chemically synthesized ribooligonucleotides, in order to change the length of the single‐stranded CCA terminus. The chemically synthesized ribooligomers, CCA, ACCA, AACCA and CAACCA, were ligated to nuclease‐treated E. coli tRNA Met f , which lacked the ACCA sequence at the 3'‐end. The methionine acceptor activities of these modified tRNAs were examined using E. coli methionyl‐tRNA synthetase. Ligation of the chemically synthesized pentamer (AACCA) to the acceptor terminus restored the methionine acceptor activity, whereas ligation of the hexamer (CAACCA) or trimer (CCA) to the acceptor terminus did not Modification of the acceptor terminus had no effect on the formylation of accepted methionine.