Literature DB >> 17380162

Histone acetyltransferase complexes: one size doesn't fit all.

Kenneth K Lee1, Jerry L Workman.   

Abstract

Over the past 10 years, the study of histone acetyltransferases (HATs) has advanced significantly, and a number of HATs have been isolated from various organisms. It emerged that HATs are highly diverse and generally contain multiple subunits. The functions of the catalytic subunit depend largely on the context of the other subunits in the complex. We are just beginning to understand the specialized roles of HAT complexes in chromosome decondensation, DNA-damage repair and the modification of non-histone substrates, as well as their role in the broader epigenetic landscape, including the role of protein domains within HAT complexes and the dynamic interplay between HAT complexes and existing histone modifications.

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Year:  2007        PMID: 17380162     DOI: 10.1038/nrm2145

Source DB:  PubMed          Journal:  Nat Rev Mol Cell Biol        ISSN: 1471-0072            Impact factor:   94.444


  426 in total

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5.  Protein arginine methyltransferase 7 regulates cellular response to DNA damage by methylating promoter histones H2A and H4 of the polymerase δ catalytic subunit gene, POLD1.

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8.  Chromatin regulators and their impact on DNA repair and G2 checkpoint recovery.

Authors:  Veronique A J Smits; Ignacio Alonso-de Vega; Daniël O Warmerdam
Journal:  Cell Cycle       Date:  2020-07-30       Impact factor: 4.534

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