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Journal Article

Analysis of phosphorylation-dependent protein-protein interactions of histone H3.

MPS-Authors
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Gelato,  K. A.
Research Group of Chromatin Biochemistry, MPI for biophysical chemistry, Max Planck Society;

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Fischle,  W.
Research Group of Chromatin Biochemistry, MPI for biophysical chemistry, Max Planck Society;

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Schwarzer,  D.
Research Group of Reaction Dynamics, MPI for biophysical chemistry, Max Planck Society;

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Supplementary Material (public)

2111455_Suppl_1.pdf
(Supplementary material), 355KB

2111455_Suppl_2.xls
(Supplementary material), 5MB

2111455_Suppl_3.xls
(Supplementary material), 4MB

Citation

Klingberg, R., Jost, J. O., Schümann, M., Gelato, K. A., Fischle, W., Krause, E., et al. (2015). Analysis of phosphorylation-dependent protein-protein interactions of histone H3. ACS Chemical Biology, 10(1), 138-145. doi:10.1021/cb500563n.


Cite as: http://hdl.handle.net/11858/00-001M-0000-0025-6C23-9
Abstract
Multiple posttranslational modifications (PTMs) of histone proteins including site-specific phosphorylation of serine and threonine residues govern the accessibility of chromatin. According to the histone code theory, PTMs recruit regulatory proteins or block their access to chromatin. Here, we report a general strategy for simultaneous analysis of both of these effects based on a SILAC MS scheme. We applied this approach for studying the biochemical role of phosphorylated S10 of histone H3. Differential pull-down experiments with H3-tails synthesized from l- and d-amino acids uncovered that histone acetyltransferase 1 (HAT1) and retinoblastoma-binding protein 7 (RBBP7) are part of the protein network, which interacts with the unmodified H3-tail. An additional H3-derived bait containing the nonhydrolyzable phospho-serine mimic phosphonomethylen-alanine (Pma) at S10 recruited several isoforms of the 14-3-3 family and blocked the recruitment of HAT1 and RBBP7 to the unmodified H3-tail. Our observations provide new insights into the many functions of H3S10 phosphorylation. In addition, the outlined methodology is generally applicable for studying specific binding partners of unmodified histone tails.