Journal
GENES & DEVELOPMENT
Volume 19, Issue 13, Pages 1572-1580Publisher
COLD SPRING HARBOR LAB PRESS, PUBLICATIONS DEPT
DOI: 10.1101/gad.1296305
Keywords
polyadenylation; termination; RNA polymerase II; Pcf 11; CTD
Categories
Funding
- NIGMS NIH HHS [GM47477, R01 GM047477] Funding Source: Medline
Ask authors/readers for more resources
Pcf11 is one of numerous proteins involved in pre-mRNA T-end processing and transcription termination. Using elongation complexes (ECs) formed from purified yeast RNA polymerase II (Pol II), we show that a 140-amino acid polypeptide from yeast Pcf11 is capable of dismantling the EC in vitro. This action depends on the C-terminal domain (CTD) of the largest subunit of Pol 11 and the CTD-interaction domain (CID) of Pcf11. Our experiments reveal a novel termination mechanism whereby Pcf11 bridges the CTD to the nascent transcript and causes dissociation of both Pol II and the nascent transcript from the DNA in the absence of nucleotide hydrolysis. We posit that conformational changes in the CTD are transduced through Pcf11 to the nascent transcript to cause termination.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available