Activation of a novel ubiquitin-independent proteasome pathway when RNA polymerase II encounters a protein roadblock

Yi Ban, Chia Wen Ho, Ren Kuo Lin, Yi Lisa Lyu, Leroy-Fong Liu

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17 Citations (Scopus)


Topoisomerase IIβ (Top2β)-DNA cleavage complexes are known to arrest elongating RNA polymerase II (RNAPII), triggering a proteasomal degradation of the RNAPII large subunit (RNAPII LS) and Top2β itself as a prelude to DNA repair. Here, we demonstrate that the degradation of Top2β 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 Top2β cleavage complex and coordinating its degradation by 20S proteasome when RNAPII is persistently stalled by the Top2β 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.

Original languageEnglish
Pages (from-to)4008-4016
Number of pages9
JournalMolecular and Cellular Biology
Issue number20
Publication statusPublished - 2013


ASJC Scopus subject areas

  • Molecular Biology
  • Cell Biology

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