Correlation Engine 2.0
Clear Search sequence regions

  • C subunits (1)
  • cellular (1)
  • endonucleases (2)
  • gene (1)
  • Mpe1 (1)
  • mrna (6)
  • multiprotein complexes (2)
  • pre mrna (1)
  • rna (3)
  • subunit (5)
  • UBC4 (1)
  • ubiquitin (8)
  • yeast protein (1)
  • Ysh1 (7)
  • Sizes of these terms reflect their relevance to your search.

    Mutation of the essential yeast protein Ipa1 has previously been demonstrated to cause defects in pre-mRNA 3' end processing and growth, but the mechanism underlying these defects was not clear. In this study, we show that the ipa1-1 mutation causes a striking depletion of Ysh1, the evolutionarily conserved endonuclease subunit of the 19-subunit mRNA Cleavage/Polyadenylation (C/P) complex, but does not decrease other C/P subunits. YSH1 overexpression rescues both the growth and 3' end processing defects of the ipa1-1 mutant. YSH1 mRNA level is unchanged in ipa1-1 cells, and proteasome inactivation prevents Ysh1 loss and causes accumulation of ubiquitinated Ysh1. Ysh1 ubiquitination is mediated by the Ubc4 ubiquitin-conjugating enzyme and Mpe1, which in addition to its function in C/P, is also a RING ubiquitin ligase. In summary, Ipa1 affects mRNA processing by controlling the availability of the C/P endonuclease and may represent a regulatory mechanism that could be rapidly deployed to facilitate reprogramming of cellular responses.


    Susan D Lee, Hui-Yun Liu, Joel H Graber, Daniel Heller-Trulli, Katarzyna Kaczmarek Michaels, Juan Francisco Cerezo, Claire L Moore. Regulation of the Ysh1 endonuclease of the mRNA cleavage/polyadenylation complex by ubiquitin-mediated degradation. RNA biology. 2020 May;17(5):689-702

    Expand section icon Mesh Tags

    Expand section icon Substances

    PMID: 32009536

    View Full Text