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The E3 ubiquitin ligase UBR 5 interacts with the H/ ACA ribonucleoprotein complex and regulates ribosomal RNA biogenesis in embryonic stem cells
Author(s) -
Saez Isabel,
Gerbracht Jennifer V.,
Koyuncu Seda,
Lee Hyun Ju,
Horn Moritz,
Kroef Virginia,
Denzel Martin S.,
Dieterich Christoph,
Gehring Niels H.,
Vilchez David
Publication year - 2020
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1002/1873-3468.13559
Subject(s) - ubiquitin ligase , ribonucleoprotein , rna ligase , microbiology and biotechnology , rna , chemistry , rna binding protein , embryonic stem cell , biology , ubiquitin , biochemistry , gene
UBR 5 is an E3 ubiquitin ligase involved in distinct processes such as transcriptional regulation and development. UBR 5 is highly upregulated in embryonic stem cells ( ESC s), whereas its expression decreases with differentiation, suggesting a role for UBR 5 in ESC function. However, little is known about how UBR 5 regulates ESC identity. Here, we define the protein interactome of UBR 5 in ESC s and find interactions with distinct components of the H/ ACA ribonucleoprotein complex, which is required for proper maturation of ribosomal RNA ( rRNA ). Notably, loss of UBR 5 induces an abnormal accumulation of rRNA processing intermediates, resulting in diminished ribosomal levels. Consequently, lack of UBR 5 triggers an increase in p53 levels and a concomitant decrease in cellular proliferation rates. Thus, our results indicate a link between UBR 5 and rRNA maturation.