| First Author | Ban Y | Year | 2013 |
| Journal | Mol Cell Biol | Volume | 33 |
| Issue | 20 | Pages | 4008-16 |
| PubMed ID | 23938298 | Mgi Jnum | J:205008 |
| Mgi Id | MGI:5543867 | Doi | 10.1128/MCB.00403-13 |
| Citation | Ban Y, et al. (2013) Activation of a novel ubiquitin-independent proteasome pathway when RNA polymerase II encounters a protein roadblock. Mol Cell Biol 33(20):4008-16 |
| abstractText | Topoisomerase IIbeta (Top2beta)-DNA cleavage complexes are known to arrest elongating RNA polymerase II (RNAPII), triggering a proteasomal degradation of the RNAPII large subunit (RNAPII LS) and Top2beta itself as a prelude to DNA repair. Here, we demonstrate that the degradation of Top2beta occurs through a novel ubiquitin-independent mechanism that requires only 19S AAA ATPases and 20S proteasome. Our results suggest that 19S AAA ATPases play a dual role in sensing the Top2beta cleavage complex and coordinating its degradation by 20S proteasome when RNAPII is persistently stalled by the Top2beta protein roadblock. Clarification of this transcription-associated proteasome pathway could shed light on a general role of 19S AAA ATPases in processing tight protein-DNA complexes during transcription elongation. |
