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A Phosphotyrosine Switch Controls the Association of Histone Mark Readers with Methylated Proteins

Lookup NU author(s): Dr Olivier Binda


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Although histone post-translational modifications play a paramount role in controlling access to genetic information, our understanding of the precise mechanisms regulating chromatin signaling remains superficial. For instance, histone H3 trimethylated on lysine 9 (H3K9me3) favors the association of chromo-domain proteins such as HP1α with chromatin. However, HP1α and other such chromatin proteins are not covering all specific histone marks at all times. Thus, how are these reader-histone interactions regulated? We propose tyrosine phosphorylation within the aromatic cage of histone mark readers as a molecular switch that can either turn ON or OFF and even alter specificity of reader-histone interactions. We have identified tyrosine phosphorylation events on the chromatin proteins HP1α and MPP8 that regulate their association with methylated histones in vitro (synthetic peptides, calf thymus purified histones, and nucleosomes), but also in cells, thus controlling access to genetic information.

Publication metadata

Author(s): Irving-Hooper BK, Binda O

Publication type: Article

Publication status: Published

Journal: Biochemistry

Year: 2016

Volume: 55

Issue: 11

Pages: 1631-1634

Print publication date: 22/03/2016

Online publication date: 12/11/2015

Acceptance date: 12/11/2015

ISSN (print): 0006-2960

ISSN (electronic): 1520-4995

Publisher: American Chemical Society


DOI: 10.1021/acs.biochem.5b01223

PubMed id: 26562627


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Funder referenceFunder name
Newcastle's Biomedical Fellowship Programme
Wellcome Trust's Institutional Strategic Support Fund
2013MaySP005Breast Cancer Campaign charity Grant