The chaperone-histone partnership: for the greater good of histone traffic and chromatin plasticity.

Abstract:

:Histones are highly positively charged proteins that wrap our genome. Their surface properties also make them prone to nonspecific interactions and aggregation. A class of proteins known as histone chaperones is dedicated to safeguard histones by aiding their proper incorporation into nucleosomes. Histone chaperones facilitate ordered nucleosome assembly and disassembly reactions through the formation of semi-stable histone-chaperone intermediates without requiring ATP, but merely providing a complementary protein surface for histones to dynamically interact with. Recurrent 'chaperoning' mechanisms involve the masking of the histone's positive charge and the direct blocking of crucial histone surface sites, including those required for H3-H4 tetramerization or the binding of nucleosomal DNA. This shielding prevents histones from engaging in premature or unwanted interactions with nucleic acids and other cellular components. In this review, we analyze recent structural studies on chaperone-histone interactions and discuss the implications of this vital partnership for nucleosome assembly and disassembly pathways.

journal_name

Curr Opin Struct Biol

authors

Hondele M,Ladurner AG

doi

10.1016/j.sbi.2011.10.003

subject

Has Abstract

pub_date

2011-12-01 00:00:00

pages

698-708

issue

6

eissn

0959-440X

issn

1879-033X

pii

S0959-440X(11)00175-8

journal_volume

21

pub_type

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