Dynamic fuzziness during linker histone action

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Abstract

Linker histones are multi-domain nucleosome binding proteins that stabilize higher order chromatin structures and engage in specific protein-protein interactions. Here we emphasize the structural and functional properties of the linker histone C-terminal domain (CTD), focusing on its intrinsic disorder, interaction-induced secondary structure formation and dynamic fuzziness. We argue that the fuzziness inherent in the CTD is a primary molecular mechanism underlying linker histone function in the nucleus. © 2012 Landes Bioscience and Springer Science+Business Media.

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McBryant, S. J., & Hansen, J. C. (2012). Dynamic fuzziness during linker histone action. Advances in Experimental Medicine and Biology, 725, 15–26. https://doi.org/10.1007/978-1-4614-0659-4_2

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