Imino Chemical Shift Assignments of TRNA, TRNA and TRNA from Escherichia Coli

Overview

Journal Biomol NMR Assign

Publisher Springer

Specialties Molecular Biology
Nuclear Medicine

Date 2024 Oct 4

PMID 39365419

Authors

Marcel-Joseph Yared

Carine Chagneau

Pierre Barraud

Affiliations

Soon will be listed here.

Abstract

Transfer RNAs (tRNAs) are an essential component of the protein synthesis machinery. In order to accomplish their cellular functions, tRNAs go through a highly controlled biogenesis process leading to the production of correctly folded tRNAs. tRNAs in solution adopt the characteristic L-shape form, a stable tertiary conformation imperative for the cellular stability of tRNAs, their thermotolerance, their interaction with protein and RNA complexes and their activity in the translation process. The introduction of post-transcriptional modifications by modification enzymes, the global conformation of tRNAs, and their cellular stability are highly interconnected. We aim to further investigate this existing link by monitoring the maturation of bacterial tRNAs in E. coli extracts using NMR. Here, we report on the H, N chemical shift assignment of the imino groups and some amino groups of unmodified and modified E. coli tRNA, tRNA and tRNA, which are essential for characterizing their maturation process using NMR spectroscopy.

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