Proteomics

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TRNA as an assembly chaperone for a macromolecular transcription-processing complex

ABSTRACT: tRNAs are widely recognized for their role in translation. Here we describe a previously unidentified function of tRNA as an assembly chaperone. During poxviral infection tRNAGln/Arg lacking the anticodon mcm5s2U modification is specifically recruited from the cellular tRNA pool to a multi-subunit poxviral RNA polymerase complex (vRNAP), where it controls the transition to the pre-initiation complex upon infection. Cryo-EM analysis of assembly intermediates illustrates how tRNAGln/Arg orchestrates the recruitment of transcription and mRNA processing factors to vRNAP. The atomic vRNAP structures reveal an induced-fit mechanism that internalizes anticodon base G36 into the anticodon stem creating a non-canonical tRNA structure and selecting a defined tRNA modification pattern. The role of tRNA as assembly chaperone extends to the pathogenic MPXV due to the high conservation of vRNAP.

INSTRUMENT(S):

ORGANISM(S): Vaccinia Virus Glv-1h68 Homo Sapiens (human)

TISSUE(S): Hela-s3 Cell, Malignant Cell

SUBMITTER: Julian Bender  

LAB HEAD: Bettina Warscheid

PROVIDER: PXD057359 | Pride | 2025-11-24

REPOSITORIES: Pride

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Publications

Transfer RNAs (tRNAs) are widely recognized for their role in translation. Here, we describe a previously unidentified function of tRNA as an assembly chaperone. During poxviral infection, tRNA<sup>Gln/Arg</sup> lacking the anticodon mcm<sup>5</sup>s<sup>2</sup>U34 modification is specifically sequestered from the cellular tRNA pool to promote formation of a multisubunit poxviral RNA polymerase complex (vRNAP). Cryo-electron microscopy analysis of assembly intermediates illustrates how tRNA<sup>  ...[more]

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