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Functions for S. cerevisiae Swd2p in 3' end formation of specific mRNAs and snoRNAs and global histone 3 lysine 4 methylation

Dichtl, Bernhard, Aasland, Rein and Keller, Walter 2004, Functions for S. cerevisiae Swd2p in 3' end formation of specific mRNAs and snoRNAs and global histone 3 lysine 4 methylation, RNA, vol. 10, no. 6, pp. 965-977, doi: 10.1261/rna.7090104.

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Title Functions for S. cerevisiae Swd2p in 3' end formation of specific mRNAs and snoRNAs and global histone 3 lysine 4 methylation
Author(s) Dichtl, BernhardORCID iD for Dichtl, Bernhard orcid.org/0000-0001-5514-4982
Aasland, Rein
Keller, Walter
Journal name RNA
Volume number 10
Issue number 6
Start page 965
End page 977
Total pages 13
Publisher Cold Spring Harbor Laboratory Press
Place of publication Woodbury, N. Y.
Publication date 2004-06
ISSN 1355-8382
1469-9001
Keyword(s) 3′ end formation
RNA polymerase II transcription termination
snoRNAs
histone methylation
WD-40 repeat
Summary The Saccharomyces cerevisiae WD-40 repeat protein Swd2p associates with two functionally distinct multiprotein complexes: the cleavage and polyadenylation factor (CPF) that is involved in pre-mRNA and snoRNA 3′ end formation and the SET1 complex (SET1C) that methylates histone 3 lysine 4. Based on bioinformatic analysis we predict a seven-bladed β-propeller structure for Swd2p proteins. Northern, transcriptional run-on and in vitro 3′ end cleavage analyses suggest that temperature sensitive swd2 strains were defective in 3′ end formation of specific mRNAs and snoRNAs. Protein–protein interaction studies support a role for Swd2p in the assembly of 3′ end formation complexes. Furthermore, histone 3 lysine 4 di-and tri-methylation were adversely affected and telomeres were shortened in swd2 mutants. Underaccumulation of the Set1p methyltransferase accounts for the observed loss of SET1C activity and suggests a requirement for Swd2p for the stability or assembly of this complex. We also provide evidence that the roles of Swd2p as component of CPF and SET1C are functionally independent. Taken together, our results establish a dual requirement for Swd2p in 3′ end formation and histone tail modification.
Language eng
DOI 10.1261/rna.7090104
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 ©2004, Cold Spring Harbor Laboratory Press
Persistent URL http://hdl.handle.net/10536/DRO/DU:30039333

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