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Yhh1p/Cft1p directly links poly(A) site recognition and RNA polymerase II transcription termination

journal contribution
posted on 2002-08-01, 00:00 authored by Bernhard DichtlBernhard Dichtl, D Blank, M Sadowski, W Hubner, S Weiser, W Keller
RNA polymerase II (pol II) transcription termination requires co-transcriptional recognition of a functional polyadenylation signal, but the molecular mechanisms that transduce this signal to pol II remain unclear. We show that Yhh1p/Cft1p, the yeast homologue of the mammalian AAUAAA interacting protein CPSF 160, is an RNA-binding protein and provide evidence that it participates in poly(A) site recognition. Interestingly, RNA binding is mediated by a central domain composed of predicted -propeller-forming repeats, which occurs in proteins of diverse cellular functions. We also found that Yhh1p/Cft1p bound specifically to the phosphorylated C-terminal domain (CTD) of pol II in vitro and in a two-hybrid test in vivo. Furthermore, transcriptional run-on analysis demonstrated that yhh1 mutants were defective in transcription termination, suggesting that Yhh1p/Cft1p functions in the coupling of transcription and 3'-end formation. We propose that direct interactions of Yhh1p/Cft1p with both the RNA transcript and the CTD are required to communicate poly(A) site recognition to elongating pol II to initiate transcription termination.

History

Journal

EMBO journal

Volume

21

Issue

15

Pagination

4125 - 4135

Publisher

Nature Publishing Group

Location

London

ISSN

0261-4189

eISSN

1460-2075

Language

eng

Publication classification

C1.1 Refereed article in a scholarly journal

Copyright notice

2002, Nature Publishing Group