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Histone and factor covalent modifications in genome regulation
Author(s) -
Berger Shelley L.
Publication year - 2009
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.23.1_supplement.89.3
Subject(s) - histone , epigenetics , chromatin , sumo protein , transcription factor , biology , acetylation , histone modifying enzymes , microbiology and biotechnology , genetics , epigenomics , computational biology , histone methyltransferase , dna methylation , ubiquitin , dna , gene , gene expression
Genomic structure and function is regulated in part through covalent post‐translational modifications (PTMs) of factors and histones, including acetylation (ac), methylation (me), phosphorylation (ph), ubiquitylation (ub), and sumoylation (su). There are an enormous number of factor and histone PTMs. To make sense of this bewildering complexity, we focus on patterns, temporal sequences, and cross‐talk between PTMs in various models, including in yeast S. cerevisiae and in mammalian cells. In yeast we focus on dynamic changes in histone PTMs during transcription and other processes. We are trying to unravel the molecular outcomes of these PTMs, as well as their role in complex physiological processes, such as during gametogenesis and during replicative cell aging. We use the genetic approaches available in yeast to determine whether altered function of chromatin may have a direct role in these epigenetic pathways. In mammals we study PTMs of DNA‐bound transcription factors, using the tumor suppressor and transcription factor p53 as a model. We currently focus on methylation and phosphorylation of specific residues in the N and C termini of p53. We are investigating cross‐talk between these PTMs on p53, and mechanistically‐interrelated PTMs on histones. Such PTM cascades may play a central role in signaling to chromatin.