Literature DB >> 33993059

Mechanistic similarities in recognition of histone tails and DNA by epigenetic readers.

Kendra R Vann1, Brianna J Klein1, Tatiana G Kutateladze2.   

Abstract

The past two decades have witnessed rapid advances in the identification and characterization of epigenetic readers, capable of recognizing or reading post-translational modifications in histones. More recently, a new set of readers with the ability to interact with the nucleosome through concomitant binding to histones and DNA has emerged. In this review, we discuss mechanistic insights underlying bivalent histone and DNA recognition by newly characterized readers and highlight the importance of binding to DNA for their association with chromatin.
Copyright © 2021 Elsevier Ltd. All rights reserved.

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Year:  2021        PMID: 33993059      PMCID: PMC8589874          DOI: 10.1016/j.sbi.2021.04.003

Source DB:  PubMed          Journal:  Curr Opin Struct Biol        ISSN: 0959-440X            Impact factor:   6.809


  50 in total

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4.  Quantitative chemical proteomics approach to identify post-translational modification-mediated protein-protein interactions.

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5.  YEATS2 is a selective histone crotonylation reader.

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Journal:  Nat Chem Biol       Date:  2016-04-18       Impact factor: 15.040

7.  Bivalent interaction of the PZP domain of BRPF1 with the nucleosome impacts chromatin dynamics and acetylation.

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8.  ENL links histone acetylation to oncogenic gene expression in acute myeloid leukaemia.

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9.  The double PHD finger domain of MOZ/MYST3 induces α-helical structure of the histone H3 tail to facilitate acetylation and methylation sampling and modification.

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10.  Molecular mechanism of the MORC4 ATPase activation.

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Journal:  Nat Commun       Date:  2020-10-29       Impact factor: 14.919

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