Mitochondrial methionyl-tRNA transformylase from bovine liver.

N. Takeuchi*, M. Kawakami, T. Ueda, L. L. Spremulli, K. Watanabe

*この研究の対応する著者

研究成果: Article査読

3 被引用数 (Scopus)

抄録

Substrate specificities of mammalian mitochondrial methionyl-tRNA transformylase (MTFmt) toward tRNA substrates were characterized in vitro. The MTFmt is able to formylate E. coli initiator methionyl-tRNA (Met-tRNA(fMet)) as efficiently as mammalian mitochondrial methionyl-tRNA. Furthermore, E. coli elongator methionyl-tRNA (Met-tRNA(mMet)) also serves as a substrate for mt MTF, whereas E. coli MTF rigorously excludes E. coli Met-tRNA(mMet) from formylation reaction. Thus, mammal mt MTF is suggested to have recognition mechanism different from E. coli MTF. To pursue the relationship between protein structure and unexpected substrate specificity of mammalian MTFmt, the nucleotide sequence of MTFmt gene was determined and its amino acids sequence was compared to other MTFs of prokaryotic origin.

本文言語English
ページ(範囲)195-196
ページ数2
ジャーナルNucleic acids symposium series
37
出版ステータスPublished - 1997
外部発表はい

ASJC Scopus subject areas

  • 医学(全般)

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