Interaction of aminoacyl-tRNA with bacterial elongation factor Tu: GTP complex: effects of the amino group of amino acid esterified to tRNA, the amino acid side chain, and tRNA structure.

Abstract:

:The present investigation was undertaken to see to what extent the alpha-amino group of the amino acid, the side chain of the amino acid of aminoacyl-tRNA, and the tRNA structure are involved in determining the affinity of aminoacyl-tRNA for bacterial elongation factor Tu-GTP complex. Various aminoacyl-tRNAs, mis-aminoacylated tRNAs, and formylated aminoacyl-tRNAs were prepared, and the dissociation constants of the ternary complexes of aminoacyl-tRNA with ET-Tu: GTP were determined by the RNase-resistance assay. The results indicated that the free amino-acid group of the amino acids in aminoacyl-tRNA is strongly required for binding with EF-Tu : GTP. In this concentration, the biological significance of formylation for Met-tRNAMetf species is discussed.

journal_name

J Biochem

journal_title

Journal of biochemistry

authors

Tanada S,Kawakami M,Nishio K,Takemura S

doi

10.1093/oxfordjournals.jbchem.a133687

subject

Has Abstract

pub_date

1982-01-01 00:00:00

pages

291-9

issue

1

eissn

0021-924X

issn

1756-2651

journal_volume

91

pub_type

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