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The structure and function of ATP‐dependent chromatin remodeling complexes
Author(s) -
Bartholomew Blaine,
Dechassa Mekonnen Lemma,
Hota Swetansu K,
Prasad Punit,
Sen Payel,
Gosh Sujana,
Hemeryck Christine S.,
Pugh Frank,
Pondugula Santhi,
Kladde Michael P.
Publication year - 2010
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.24.1_supplement.310.1
Subject(s) - chromatin remodeling , chromatin , nucleosome , biology , microbiology and biotechnology , histone code , histone modifying enzymes , chia pet , histone , chip sequencing , swi/snf , genetics , chromatin structure remodeling (rsc) complex , dna
ATP‐dependent chromatin remodelers are key regulators of the epigenome and have important roles in transcription, replication, repair and recombination of DNA. These remodelers all have the basic ability to translocate along DNA in an ATP‐dependent manner. The remodelers use this activity in various ways to reorganize chromatin fibers through nucleosome mobilization, histone exchange, and/or nucleosome disassembly. The interactions with chromatin of three of the four major families of ATP‐dependent chromatin remodelers are examined to find some of their fundamental differences. The subunits and protein domains that bind nucleosomes have been mapped. The mechanism of chromatin remodeling has been studied using a variety of techniques to capture the intermediate states and to map changes in protein‐DNA and protein‐protein interactions. Deletion and point mutagenesis of protein domains have further delineated the functional role of particular domains in chromatin remodeling both in vitro and in vivo and has provided additional insights into the mechanism of chromatin remodeling. Three basic models for chromatin remodeling will be presented that account for some of the diversity among chromatin remodelers.