Role of the extra G-C pair at the end of the acceptor stem of tRNAHb in aminoacylation

Hyouta Himeno*, Tsunemi Hasegawa, Takuya Ueda, Kimitsuna Watanabe, Kin Ichiro Miura, Mikio Shimizu

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

165 Citations (Scopus)


All sequenced histidine tRNAs have one additional nucleotide at the 5′ end compared with other tRNA species. To Investigate the role of this unique structure in aainoacylation, we constructed in vitro transcripts corresponding to the E. coli histidine tRNA sequence and its variants at the G-1-C73 base pair, by using T7 RNA polymerase transcription systm. A transcript having a wild-type sequence with no modified bases was a good substrate for histidyl-tRNA synthetase (HisRS), and aminoacylation activity was affected by introduction of a triphosphate at the 5′ terminus. Base replacements at position 73 caused a marked decrease of Vmax, and deletion and substitution of the G-1 had a remarkable effect on the aminoacylation. A mutant having an A-1-U73 pair was also not a good substrate for HisRS. Comparison among G-1-deficient mutants showed that A was preferable rather than C as the base at position 73. These data demonstrate that the set of the G-1-C73 pair at the end of the acceptor stem of histidine tRNA is crucial for the catalytic process of aminoacylation.

Original languageEnglish
Pages (from-to)7855-7863
Number of pages9
JournalNucleic acids research
Issue number19
Publication statusPublished - 1989 Oct 11
Externally publishedYes

ASJC Scopus subject areas

  • Genetics


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