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tRNA as an assembly chaperone for a macromolecular transcription-processing complex.

Julia Bartuli1, Stefan Jungwirth1, Manisha Dixit1,2

  • 1Department of Biochemistry 1, Theodor Boveri-Institute, University of Würzburg, Würzburg, Germany.

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|September 4, 2025
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Summary
This summary is machine-generated.

Transfer RNAs (tRNAs) act as assembly chaperones during poxvirus infection, facilitating viral RNA polymerase complex formation. This novel function involves specific, unmodified tRNAGln/Arg sequestration and recruitment of viral transcription factors.

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Area of Science:

  • Molecular Biology
  • Virology
  • Structural Biology

Background:

  • Transfer RNAs (tRNAs) are primarily known for their essential role in protein translation.
  • Poxviruses, such as the Mpox virus, encode their own RNA polymerase (vRNAP) for replication.
  • The precise assembly mechanisms of viral macromolecular complexes are not fully understood.

Purpose of the Study:

  • To investigate a novel function of tRNAs beyond translation.
  • To elucidate the role of specific tRNAs in the assembly of poxviral RNA polymerase (vRNAP).
  • To understand the structural mechanisms by which tRNAs regulate viral transcription complex formation.

Main Methods:

  • Cryo-electron microscopy (Cryo-EM) to visualize assembly intermediates.
  • Biochemical assays to study tRNA sequestration and factor recruitment.
  • Analysis of tRNA structure and modification patterns.

Main Results:

  • Identified tRNAGln/Arg lacking specific modifications as an assembly chaperone for poxviral vRNAP.
  • Demonstrated that this modified tRNA orchestrates the recruitment of transcription and mRNA processing factors.
  • Revealed an induced fit mechanism involving anticodon base G36 internalization, forming a noncanonical tRNA structure.
  • Showed this mechanism controls the transition to the preinitiation complex.

Conclusions:

  • Transfer RNAs (tRNAs) possess a previously unrecognized function as assembly chaperones in viral replication.
  • The specific sequestration and structural adaptation of tRNAGln/Arg are critical for poxviral vRNAP assembly and function.
  • This tRNA-mediated assembly mechanism is conserved in pathogenic Mpox virus, highlighting its biological significance.