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Updated: Aug 19, 2026

Residue-specific Incorporation of Noncanonical Amino Acids into Model Proteins Using an Escherichia coli Cell-free Transcription-translation System
11:47

Residue-specific Incorporation of Noncanonical Amino Acids into Model Proteins Using an Escherichia coli Cell-free Transcription-translation System

Published on: August 1, 2016

グルタミンニル-tRNA合成酵素によるアンチコドンループ認識の構造的基礎

M A Rould1, J J Perona, T A Steitz

  • 1Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, Connecticut 06511.

Nature
|July 18, 1991
PubMed
まとめ

移転RNA (tRNA) とATPに結合するグルタミンニル移転RNA合成酵素のアンチコドンループは,ユニークな構造変化を示しています. これらの変化は特定の結合を可能にし,酵素が正しいtRNAを正確に選択することを可能にします.

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Transfer RNA Synthesis02:36

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Transfer RNA Synthesis02:36

Transfer RNA Synthesis

One of the unique features of tRNA is the presence of modified bases. In some tRNAs, modified bases account for nearly 20% of the total bases in the molecule. Altogether, these unusual bases protect the tRNA from enzymatic degradation by RNases.
Each of these chemical modifications is carried by a specific enzyme, post-transcription. All of these enzymes have unique base and site-specificity. Methylation, the most common chemical modification, is carried by at least nine different enzymes, with...
tRNA Activation02:26

tRNA Activation

Aminoacyl-tRNA synthetases are present in both eukaryotes and bacteria. Though eukaryotes have 20 different aminoacyl-tRNA synthetases to couple to 20 amino acids, many bacteria do not have genes for all of these aminoacyl-tRNA synthetases. Despite this, they still use all 20 amino acids to synthesize their proteins. For instance, some bacteria do not have the gene encoding the enzyme that couples glutamine with its partner tRNA. In these organisms, one enzyme adds glutamic acid to all of the...