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

Research output: Contribution to journalArticle

16 Citations (Scopus)

Abstract

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
Volume33
Issue number20
DOIs
Publication statusPublished - 2013

Fingerprint

RNA Polymerase II
Proteasome Endopeptidase Complex
Ubiquitin
Adenosine Triphosphatases
Type II DNA Topoisomerase
DNA Cleavage
Proteins
DNA Repair
DNA

ASJC Scopus subject areas

  • Molecular Biology
  • Cell Biology

Cite this

Activation of a novel ubiquitin-independent proteasome pathway when RNA polymerase II encounters a protein roadblock. / Ban, Yi; Ho, Chia Wen; Lin, Ren Kuo; Lyu, Yi Lisa; Liu, Leroy-Fong.

In: Molecular and Cellular Biology, Vol. 33, No. 20, 2013, p. 4008-4016.

Research output: Contribution to journalArticle

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