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<p>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>Gln/Arg</sup> orchestrates the recruitment of transcription and mRNA processing factors to vRNAP where it controls the transition to the preinitiation complex. This is achieved by an induced fit mechanism that internalizes anticodon base G36 into the anticodon stem, creating a noncanonical tRNA structure and selecting a defined tRNA modification pattern. The role of tRNA as an assembly chaperone extends to the pathogenic Mpox virus, which features a similar vRNAP.</p>

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

  • 期刊论文

  • 出版模式：

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  • 发表日期：

    2025年9月4日

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  • Julia Bartuli,
  • Stefan Jungwirth,
  • Manisha Dixit,
  • Takumi Okuda,
  • Johannes Patrick Zimmermann,
  • Matthias Erlacher,
  • Tao Pan,
  • Asisa Volz,
  • Alexander Hüttenhofer,
  • Bettina Warscheid,
  • Claudia Höbartner,
  • Clemens Grimm,
  • Utz Fischer

摘要

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, tRNAGln/Arg lacking the anticodon mcm5s2U34 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 tRNAGln/Arg orchestrates the recruitment of transcription and mRNA processing factors to vRNAP where it controls the transition to the preinitiation complex. This is achieved by an induced fit mechanism that internalizes anticodon base G36 into the anticodon stem, creating a noncanonical tRNA structure and selecting a defined tRNA modification pattern. The role of tRNA as an assembly chaperone extends to the pathogenic Mpox virus, which features a similar vRNAP.