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Structural insights into dynamics of the BMV TLS aminoacylation

ABSTRACT: We performed Biotinylated RNA pull-down coupled with mass spectrometry, which enables the identification of TLS-binding proteins. Using in vitro synthesized BMV TLS and protein extracts derived from Nicotiana tabacum L.'s leaves, mass spectrometry results demonstrated the enrichment of ribosome-associated proteins

ORGANISM(S): 'nicotiana Tabacum' Yellowing Phytoplasma

SUBMITTER: Kaiming Zhang

PROVIDER: PXD057815 | iProX | Wed Nov 13 00:00:00 GMT 2024

REPOSITORIES: iProX

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Structural insights into dynamics of the BMV TLS aminoacylation.

Yang Wen W Yi Ran R Yao Jing J Gao Yongxiang Y Li Shanshan S Gong Qingguo Q Zhang Kaiming K

Nature communications 20250203 1

Brome Mosaic Virus (BMV) utilizes a tRNA-like structure (TLS) within its 3' untranslated region to mimic host tRNA functions, aiding aminoacylation and viral replication. This study explores the structural dynamics of BMV TLS interacting with tyrosyl-tRNA synthetase (TyrRS) during aminoacylation. Using cryo-EM, we capture multiple states of the TLS-TyrRS complex, including unbound TLS, pre-1a, post-1a, and catalysis states, with resolutions of 4.6 Å, 3.5 Å, 3.7 Å, and 3.85 Å, respectively. These ...[more]

PMID: 39900568

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