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  Structure and carboxyl-terminal domain (CTD) binding of the Set2 SRI domain that couples histone H3 Lys36 methylation to transcription.

Vojnic, E., Simon, B., Strahl, B. D., Sattler, M., & Cramer, P. (2006). Structure and carboxyl-terminal domain (CTD) binding of the Set2 SRI domain that couples histone H3 Lys36 methylation to transcription. The Journal of Biological Chemistry, 281(1), 13-15. doi:10.1074/jbc.C500423200.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0015-83ED-C Version Permalink: http://hdl.handle.net/11858/00-001M-0000-0027-C63F-C
Genre: Journal Article

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 Creators:
Vojnic, E., Author
Simon, B., Author
Strahl, B. D., Author
Sattler, M., Author
Cramer, P.1, Author              
Affiliations:
1Department of Molecular Biology, MPI for Biophysical Chemistry, Max Planck Society, ou_1863498              

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 Abstract: During mRNA elongation, the SRI domain of the histone H3 methyltransferase Set2 binds to the phosphorylated carboxyl-terminal domain (CTD) of RNA polymerase II. The solution structure of the yeast Set2 SRI domain reveals a novel CTD-binding fold consisting of a left-handed three-helix bundle. NMR titration shows that the SRI domain binds an Ser2/Ser5-phosphorylated CTD peptide comprising two heptapeptide repeats and three flanking NH2-terminal residues, whereas a single CTD repeat is insufficient for binding. Residues that show strong chemical shift perturbations upon CTD binding cluster in two regions. Both CTD tyrosine side chains contact the SRI domain. One of the tyrosines binds in the region with the strongest chemical shift perturbations, formed by the two NH2-terminal helices. Unexpectedly, the SRI domain fold resembles the structure of an RNA polymerase-interacting domain in bacterial σ factors (domain σ2 in σ70).

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Language(s): eng - English
 Dates: 2005-11-142006-01-06
 Publication Status: Published in print
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 Rev. Type: Peer
 Identifiers: DOI: 10.1074/jbc.C500423200
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Title: The Journal of Biological Chemistry
Source Genre: Journal
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Pages: - Volume / Issue: 281 (1) Sequence Number: - Start / End Page: 13 - 15 Identifier: -