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The role of the yeast cleavage and polyadenylation factor subunit Ydh1p/Cft2p in pre-mRNA 3' end formation

Kyburz, Andrea, Sadowski, Martin, Dichtl, Bernhard and Keller, Walter 2003, The role of the yeast cleavage and polyadenylation factor subunit Ydh1p/Cft2p in pre-mRNA 3' end formation, Nucleic acids research, vol. 31, no. 14, pp. 3936-3945, doi: 10.1093/nar/gkg478.

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Title The role of the yeast cleavage and polyadenylation factor subunit Ydh1p/Cft2p in pre-mRNA 3' end formation
Author(s) Kyburz, Andrea
Sadowski, Martin
Dichtl, BernhardORCID iD for Dichtl, Bernhard orcid.org/0000-0001-5514-4982
Keller, Walter
Journal name Nucleic acids research
Volume number 31
Issue number 14
Start page 3936
End page 3945
Total pages 10
Publisher Oxford University Press
Place of publication Oxford, England
Publication date 2003-07-15
ISSN 0305-1048
1362-4962
Keyword(s) cleavage and polyadenylation specificity factor
messenger RNA precursor
mutant protein
polyadenylic acid
protein subunit
protein Ydh1p
RNA
RNA polymerase II
Summary Cleavage and polyadenylation factor (CPF) is a multi‐protein complex that functions in pre‐mRNA 3′‐end formation and in the RNA polymerase II (RNAP II) transcription cycle. Ydh1p/Cft2p is an essential component of CPF but its precise role in 3′‐end processing remained unclear. We found that mutations in YDH1 inhibited both the cleavage and the polyadenylation steps of the 3′‐end formation reaction in vitro. Recently, we demonstrated that an important function of CPF lies in the recognition of poly(A) site sequences and RNA binding analyses suggesting that Ydh1p/Cft2p interacts with the poly(A) site region. Here we show that mutant ydh1 strains are deficient in the recognition of the ACT1 cleavage site in vivo. The C‐terminal domain (CTD) of RNAP II plays a major role in coupling 3′‐end processing and transcription. We provide evidence that Ydh1p/Cft2p interacts with the CTD of RNAP II, several other subunits of CPF and with Pcf11p, a component of CF IA. We propose that Ydh1p/Cft2p contributes to the formation of important interaction surfaces that mediate the dynamic association of CPF with RNAP II, the recognition of poly(A) site sequences and the assembly of the polyadenylation machinery on the RNA substrate.
Language eng
DOI 10.1093/nar/gkg478
Field of Research 060199 Biochemistry and Cell Biology not elsewhere classified
Socio Economic Objective 970106 Expanding Knowledge in the Biological Sciences
HERDC Research category C1.1 Refereed article in a scholarly journal
Copyright notice ©2003, Oxford University Press
Persistent URL http://hdl.handle.net/10536/DRO/DU:30039315

Document type: Journal Article
Collection: School of Life and Environmental Sciences
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