RNF12 catalyzes BRF1 ubiquitination and regulates RNA polymerase III-dependent transcription.

RNA polymerase III (Pol III) is responsible for the production of small noncoding RNA species, including tRNAs and 5S rRNA. Pol III-dependent transcription is generally enhanced in transformed cells and tumors, but the underlying mechanisms remain not well-understood. It has been demonstrated that the BRF1 subunit of TFIIIB is essential ...
for the accurate initiation of Pol III-dependent transcription. However, it is not known whether BRF1 undergoes ubiquitin modification and whether BRF1 ubiquitination regulates Pol III-dependent transcription. Here, we show that RNF12, a RING domain-containing ubiquitin E3 ligase, physically interacts with BRF1. Via direct interaction, RNF12 catalyzes Lys27- and Lys33-linked polyubiquitination of BRF1. Furthermore, RNF12 is able to negatively regulate Pol III-dependent transcription and cell proliferation via BRF1. These findings uncover a novel mechanism for the regulation of BRF1 and reveal RNF12 as an important regulator of Pol III-dependent transcription.
Mesh Terms:
Cell Proliferation, HEK293 Cells, HeLa Cells, Humans, RNA Polymerase III, TATA-Binding Protein Associated Factors, Transcription, Genetic, Ubiquitin-Protein Ligases, Ubiquitination
J. Biol. Chem.
Date: Dec. 04, 2018
Download Curated Data For This Publication
219640
Switch View:
  • Interactions 53