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

Hondele, Maria and Ladurner, Andreas G.. (2011) The chaperone-histone partnership: for the greater good of histone traffic and chromatin plasticity. Current Opinion in Structural Biology, 21 (6). pp. 698-708.

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Official URL: https://edoc.unibas.ch/79413/

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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.
Faculties and Departments:05 Faculty of Science > Departement Biozentrum > Growth & Development > Biochemistry (Hondele)
UniBasel Contributors:Hondele, Maria
Item Type:Article
Article Subtype:Research Article
Note:Publication type according to Uni Basel Research Database: Journal article
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Last Modified:30 Nov 2020 16:28
Deposited On:30 Nov 2020 16:28

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