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  Accessibility of different histone H3-binding domains of UHRF1 is allosterically regulated by phosphatidylinositol 5-phosphate.

Gelato, K. A., Tauber, M., Ong, M. S., Winter, S., Hamada, K., Sindlinger, J., et al. (2014). Accessibility of different histone H3-binding domains of UHRF1 is allosterically regulated by phosphatidylinositol 5-phosphate. Molecular Cell, 54(6), 905-919. doi:10.1016/j.molcel.2014.04.004.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0019-DD56-C Version Permalink: http://hdl.handle.net/11858/00-001M-0000-0028-1D53-D
Genre: Journal Article

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 Creators:
Gelato, K. A.1, Author              
Tauber, M.1, Author              
Ong, M. S., Author
Winter, S.1, Author              
Hamada, K.1, Author              
Sindlinger, J., Author
Lemak, A., Author
Bultsma, Y., Author
Houliston, S., Author
Schwarzer, D., Author
Divecha, N., Author
Arrowsmith, C. H., Author
Fischle, W.1, Author              
Affiliations:
1Research Group of Chromatin Biochemistry, MPI for biophysical chemistry, Max Planck Society, ou_578604              

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 Abstract: UHRF1 is a multidomain protein crucially linking histone H3 modification states and DNA methylation. While the interaction properties of its specific domains are well characterized, little is known about the regulation of these functionalities. We show that UHRF1 exists in distinct active states, binding either unmodified H3 or the H3 lysine 9 trimethylation (H3K9me3) modification. A polybasic region (PBR) in the C terminus blocks interaction of a tandem tudor domain (TTD) with H3K9me3 by occupying anessential peptide-binding groove. In this state the plant homeodomain (PHD) mediates interaction with the extreme N terminus of the unmodified H3 tail. Binding of the phosphatidylinositol phosphate PI5P to the PBR of UHRF1 results in a conformational rearrangement of the domains, allowing the TTD to bind H3K9me3. Our results define an allosteric mechanism controlling heterochromatin association of an essential regulatory protein of epigenetic states and identify a functional role for enigmatic nuclear phosphatidylinositol phosphates.

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Language(s): eng - English
 Dates: 2014-06-19
 Publication Status: Published in print
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 Rev. Method: Peer
 Identifiers: DOI: 10.1016/j.molcel.2014.04.004
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Title: Molecular Cell
Source Genre: Journal
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Pages: - Volume / Issue: 54 (6) Sequence Number: - Start / End Page: 905 - 919 Identifier: -