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Nucleic Acids Research Advance Access originally published online on December 17, 2007
Nucleic Acids Research 2008 36(3):905-914; doi:10.1093/nar/gkm1112
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Nucleic Acids Research, 2008, Vol. 36, No. 3 905-914
© 2007 The Author(s)
This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/2.0/uk/) which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.

Molecular Biology

Human Pcf11 enhances degradation of RNA polymerase II-associated nascent RNA and transcriptional termination

Steven West and Nicholas J. Proudfoot*

Sir William Dunn School of Pathology, South Parks Road, Oxford, OX1 3RE, UK

*To whom correspondence should be addressed. Tel: +01865 275 566; Fax: +01865 275 556; Email: nicholas.proudfoot{at}path.ox.ac.uk

Received October 29, 2007. Revised November 22, 2007. Accepted November 28, 2007.

The poly(A) (pA) signal possesses a dual function in 3' end processing of pre-mRNA and in transcriptional termination of RNA polymerase II (Pol II) for most eukaryotic protein-coding genes. A key protein factor in yeast and Drosophila Pol II transcriptional termination is the 3'-end processing factor, Pcf11. In vitro studies suggest that Pcf11 is capable of promoting the dissociation of Pol II elongation complexes from DNA. Moreover, several mutant alleles of yeast Pcf11 effect termination in vivo. However, functions of human Pcf11 (hPcf11) in Pol II termination have not been explored. Here we show that depletion of hPcf11 from HeLa cells reduces termination efficiency. Furthermore, we provide evidence that hPcf11 is required for the efficient degradation of the 3' product of pA site cleavage. Finally, we show that these functions of hPcf11 require an intact pA signal.


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