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Area of Science:

  • Molecular Biology
  • Structural Biology
  • RNA Biology

Background:

  • U6 small nuclear RNA (snRNA) is a ribozyme essential for pre-messenger RNA (pre-mRNA) splicing.
  • Epitranscriptomic modifications, including oligo-uridylylation by terminal uridylyltransferase 1 (TUT1), occur on U6 snRNA.
  • The 3'-oligo-uridylylated tail of U6 snRNA is vital for U4/U6 di-snRNP formation and efficient pre-mRNA splicing.

Purpose of the Study:

  • To elucidate the structural basis of the interaction between human TUT1 and U6 snRNA.
  • To understand how TUT1 specifically recognizes and binds U6 snRNA for oligo-uridylylation.

Main Methods:

  • Cryo-electron microscopy (cryo-EM) was used to determine the structure of the human TUT1:U6 snRNA complex.

Main Results:

  • The structure reveals how TUT1's multiple domains clamp and grip U6 snRNA, positioning its 3'-end in the catalytic pocket.
  • Specific motifs and domains of TUT1, including the N-terminal zinc finger (ZF)-RNA recognition motif, catalytic Palm, Fingers, and C-terminal kinase-associated 1 domain, mediate the interaction.
  • TUT1 anchors the U6 snRNA body, preventing dissociation during the oligo-uridylylation process.

Conclusions:

  • TUT1 exhibits high specificity for U6 snRNA, utilizing its entire structure to ensure accurate oligo-uridylylation.
  • The detailed structural insights explain the mechanism of U6 snRNA recognition and binding by TUT1, highlighting its role in splicing regulation.