Histone chaperone exploits intrinsic disorder to switch acetylation specificity
Histone chaperone exploits intrinsic disorder to switch acetylation specificity
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Publisher
London: Nature Publishing Group UK
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Language
English
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London: Nature Publishing Group UK
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Histones, the principal protein components of chromatin, contain long disordered sequences, which are extensively post-translationally modified. Although histone chaperones are known to control both the activity and specificity of histone-modifying enzymes, the mechanisms promoting modification of highly disordered substrates, such as lysine-acetyl...
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Full title
Histone chaperone exploits intrinsic disorder to switch acetylation specificity
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TN_cdi_doaj_primary_oai_doaj_org_article_0b7982cadac74428b575ac9e21c9f021
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https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_doaj_primary_oai_doaj_org_article_0b7982cadac74428b575ac9e21c9f021
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ISSN
2041-1723
E-ISSN
2041-1723
DOI
10.1038/s41467-019-11410-7
