Regulation of the Ysh1 endonuclease of the mRNA cleavage/polyadenylation complex by ubiquitinmediated degradation.
Autor: Lee, Susan D.; Liu, Hui-Yun; Graber, Joel H.; Heller-Trulli, Daniel; Michaels, Katarzyna Kaczmarek; Cerezo, Juan Francisco; Moore, Claire L.
Resumen: Mutation of the essential yeast protein Ipa1 has previously been demonstrated to cause defects in premRNA 3ʹ 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 3ʹ 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.
Identificador universal: http://hdl.handle.net/10641/2612
Fecha: 2020
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