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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.
Author(s): Irving-Hooper BK, Binda O
Publication type: Article
Publication status: Published
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
PubMed id: 26562627
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