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Structural and Functional Analysis of Histone Chaperones
Author(s) -
Gu Yajie,
Bergeron Serge,
Krzizike Daniel,
Luger Karolin
Publication year - 2016
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.30.1_supplement.379.3
Subject(s) - nucleosome , histone , histone code , microbiology and biotechnology , histone methylation , histone h1 , chaperone (clinical) , biology , histone h2a , histone modifying enzymes , chromatin , genetics , dna , gene , gene expression , medicine , pathology , dna methylation
Nucleosomes are large macromolecular complexes that are assembled and disassembled in a stepwise manner. Nucleosome assembly and disassembly processes are essential during DNA replication, transcription, and repair, and are orchestrated by multiple protein complexes. Histone chaperones are multifunctional proteins that bind and shuttle histones into the nucleus, assemble and disassemble nucleosomes in an ATP‐independent manner, and regulate transcription through largely unknown mechanisms. Several structurally unrelated types of histone chaperones, each with multiple family members, are known. Some histone chaperones operate equally well with all types of histones, whereas others are specific to types of histones, or even histone variants and function exclusively in replication‐independent pathways. Some histone chaperones act synergistically with ATP‐dependent chromatin remodeling factors. We will discuss various aspects of histone chaperone function during nucleosome assembly and disassembly, and highlight different mode(s) of histone chaperone – histone interactions with possible roles in histone folding.