@article{feb8084bbc444bd4ac1e334856ebce10,
title = "The yeast Rat1 exonuclease promotes transcription termination by RNA polymerase II",
abstract = "The carboxy-terminal domain (CTD) of the RNA polymerase II (RNApII) largest subunit consists of multiple heptapeptide repeats with the consensus sequence YSPTSPS. Different CTD phosphorylation patterns act as recognition sites for the binding of various messenger RNA processing factors, thereby coupling transcription and mRNA processing. Polyadenylation factors are co-transcriptionally recruited by phosphorylation of CTD serine 2 (ref. 2) and these factors are also required for transcription termination. RNApII transcribes past the poly(A) site, the RNA is cleaved by the polyadenylation machinery, and the RNA downstream of the cleavage site is degraded. Here we show that Rtt103 and the Rat1/Rai1 5′ → 3′ exonuclease are localized at 3′ ends of protein coding genes. In rat1-1 or rai1 Δ cells, RNA 3′ to polyadenylation sites is greatly stabilized and termination defects are seen at many genes. These findings support a model in which poly(A) site cleavage and subsequent degradation of the 3′-downstream RNA by Rat1 trigger transcription termination.",
author = "Minkyu Kim and Krogan, {Nevan J.} and Lidia Vasiljeva and Rando, {Oliver J.} and Eduard Nedea and Greenblatt, {Jack F.} and Stephen Buratowski",
note = "Funding Information: Acknowledgements We thank M. Springer, D. Picot, R. Gi{\'e}g{\'e}, F. Allemand, V. Arluison and F. Dardel for discussions, S. Fieulaine and M. Pirocchi for help with the beam-line BM30A at the European Synchrotron Radiation Facility, and J.L. Popot for use of crystallography facilities and X-ray generator at the IBPC. This work was supported by the CNRS (UPR 9073), Universit{\'e} Paris VII-Denis Diderot, PRFMMIP 2001/2003, and ACI Jeunes Chercheurs from the Minist{\`e}re de l{\textquoteright}Education Nationale. Funding Information: Acknowledgements We thank C. Moore and her laboratory for advice on polyadenylation reactions; N. Proudfoot, S. McCracken and B. Blencowe for sharing unpublished information; and the Taplin Mass Spectroscopy facility at Harvard Medical School and D. Richards of Affinium Pharmaceuticals for mass spectroscopy. N.J.K. was supported by a Doctoral Fellowship from the Canadian Institutes of Health Research (CIHR). O.J.R. is supported by funding from the Bauer Center for Genomics Research. This research was supported by grants to S.B. from the US National Institutes of Health, and to J.F.G. from the Canadian Institutes of Health Research, the Ontario Genomics Institute, and the National Cancer Institute of Canada with funds from the Canadian Cancer Society. L.V. is a Fellow and S.B. is a Scholar of the Leukemia and Lymphoma Society.",
year = "2004",
month = nov,
day = "25",
doi = "10.1038/nature03041",
language = "English (US)",
volume = "432",
pages = "517--522",
journal = "Nature",
issn = "0028-0836",
publisher = "Nature Research",
number = "7016",
}