Physical and functional association of RNA polymerase II and the proteasome.
Recent studies from a number of laboratories have revealed a surprising number of connections between RNA polymerase II transcription and the ubiquitin/proteasome pathway. We now find yet another intersection of these pathways by showing that the 26S proteasome associates with regions of the GAL1, GAL10, and HSP82 genes, including the 3' ends, in a transcription-dependent fashion. The appearance of the proteasome on these inducible genes correlates with both the accumulation of transcripts and the buildup of RNA polymerase II complexes in the same region. Furthermore, the 26S proteasome and RNA polymerase II coimmunoprecipitate, and inhibition of 26S proteolytic activity leads to increased read through of a transcription termination site. We suggest that the proteasome is generally recruited to the DNA at sites of stalled RNA polymerase and may act to resolve these complexes.
Gillette
Thomas G
TG
Center for Biomedical Inventions and Departments of Internal Medicine, Molecular Biology, and Microbiology, 5323 Harry Hines Boulevard, University of Texas Southwestern Medical Center, Dallas, TX 75390-8573, USA.
Gonzalez
Fernando
F
Delahodde
Agnes
A
Johnston
Stephen Albert
SA
Kodadek
Thomas
T
D003546:Cysteine Endopeptidases / Q000378:metabolism / Q000502:physiology*; D006868:Hydrolysis; D009097:Multienzyme Complexes / Q000378:metabolism / Q000502:physiology*; D011233:Precipitin Tests; D046988:Proteasome Endopeptidase Complex; D012319:RNA Polymerase II / Q000378:metabolism / Q000502:physiology*; D014158:Transcription, Genetic
D009097:Multienzyme Complexes; D012319:RNA Polymerase II; D003546:Cysteine Endopeptidases; D046988:Proteasome Endopeptidase Complex