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Volume 26 Issue 12, December 2019

Opening up T-box RNA

Structural elucidation of T-box–tRNA complexes provides new insights into the mechanisms of tRNA decoding and aminoacylation sensing by T-box riboswitches.

See Li, Su et al., Battaglia et al., Suddala and Zhang

Image: composite by Erin Dewalt using image from Yevgen Romanenko / Moment / Getty and structures of T-box–tRNA complex in ribbon representation prepared by Jacob Weaver and Alexander Serganov. Cover Design: Erin Dewalt.

News & Views

  • Bacterial T-boxes are regulatory mRNA regions that control the transcription or translation of factors involved in amino acid supply. T-boxes act by directly binding to non-aminoacylated tRNA in response to amino acid starvation. Three studies now capture three-dimensional structures of tRNA–T-box complexes and reveal a set of RNA features that are required for the recognition of specific tRNAs and modulation of gene expression.

    • Jacob W. Weaver
    • Alexander Serganov
    News & Views


  • Finally, the architecture of the translocase of the mitochondrial outer membrane (TOM complex) is revealed, after 20 years of anticipation. Two groups have now determined the near-atomic structures of the TOM complex. These findings improve understanding of the mechanisms by which TOM facilitates the passage of about 1,000 different proteins from the cytosol into the mitochondria.

    • Doron Rapaport
    News & Views
  • Chromatin is compartmentalized spatially and temporally at multiple levels, but the precise organization of chromatin and mechanisms underlying its restructuring remain unclear. Two studies published in Cell and Nature now demonstrate the ability of chromatin to undergo liquid–liquid phase separation under physiological conditions and show that this intrinsic physicochemical property of chromatin can be regulated.

    • Yi Zhang
    • Tatiana G. Kutateladze
    News & Views
  • Stabilization of the 3D genome architecture surrounding DNA lesions is critical for the maintenance of genome integrity. A new report by Ochs et al. shows how 53BP1 and RIF1 assemble a higher-order structure in the vicinity of damaged chromatin to protect it from unscheduled DNA-end resection.

    • Indrajeet Ghodke
    • Evi Soutoglou
    News & Views
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