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

*この研究の対応する著者

研究成果: Article査読

146 被引用数 (Scopus)

抄録

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.

本文言語English
ページ(範囲)7855-7863
ページ数9
ジャーナルNucleic acids research
17
19
DOI
出版ステータスPublished - 1989 10月 11
外部発表はい

ASJC Scopus subject areas

  • 遺伝学

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