Abstract
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.
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