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Mechanistic insights into RNA surveillance by the canonical poly(A) polymerase Pla1 of the MTREC complex

Komal Soni1, Anusree Sivadas2, Attila Horvath2

  • 1Heidelberg University Biochemistry Center (BZH), INF 328, D-69120, Heidelberg, Germany.

Nature Communications
|February 11, 2023
PubMed

Insights

The Mtl1-Red1 Core (MTREC) complex in fission yeast interacts with poly(A) polymerase Pla1, enhancing the degradation of unstable RNA transcripts. This interaction also aids in forming facultative heterochromatic islands.

Area of Science:

  • Molecular Biology
  • RNA Biology
  • Biochemistry

Background:

  • The Mtl1-Red1 Core (MTREC) complex is crucial for degrading cryptic unstable transcripts (CUTs) via the nuclear RNA exosome.
  • Polyadenylation, mediated by poly(A) polymerase Pla1 (part of CPF/CPSF), is essential for nascent RNA processing.

Purpose of the Study:

  • To identify and characterize the interaction between Pla1 and MTREC core component Red1.
  • To analyze the in vivo functional relevance of the Red1-Pla1 interaction.

Main Methods:

  • Crystal structure determination of the Pla1-Red1 complex.
  • Site-directed mutagenesis of the Pla1-Red1 interaction interface.
  • In vivo functional assays in fission yeast.

Main Results:

  • A 58-residue fragment of Red1 binds to the RNA recognition motif of Pla1, tethering it to the MTREC complex.
  • Mutations disrupting the Red1-Pla1 interaction impair hyper-adenylation of CUTs and their degradation.
  • The Red1-Pla1 interaction is essential for efficient assembly of fission yeast facultative heterochromatic islands.

Conclusions:

  • The Red1-Pla1 interaction within the MTREC complex is vital for efficient RNA surveillance and degradation of CUTs.
  • This interaction plays a dual role, also influencing the formation of facultative heterochromatic islands.
  • Suggests a significant interplay between RNA surveillance and 3'-end processing pathways.

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