NDLI: Post-translational modifications of the intrinsically disordered terminal domains of histone H1: effects on secondary structure and chromatin dynamics

Content Provider	Springer Nature Link
Author	Roque, A. Ponte, I. Suau, P.
Copyright Year	2016
Abstract	H1 linker histones are involved both in the maintenance of chromatin higher-order structure and in gene regulation. H1 binds to linker DNA regions on the surface of the nucleosome. In higher eukaryotes, H1 contains three distinct domains: a short N-terminal domain (NTD), a central globular domain, and a long C-terminal domain (CTD). Terminal domains determine subtype specificity and to a large extent the linker DNA binding and chromatin condensing properties of histone H1. This review is focused on the recent numerous studies that have provided insights in the role of H1 terminal domains in chromatin dynamics. The N- and C-terminal domains behave as intrinsically disordered proteins with coupled binding and folding. We examine the potential kinetic advantages of intrinsic disorder in the recognition of the specific H1 binding sites in chromatin. As typical intrinsically disordered regions, H1 terminal domains are post-translationally modified. Post-translational modifications in the NTD determine the interaction of histone H1 with other proteins involved in heterochromatin formation and transcriptional regulation, while phosphorylation by cyclin-dependent kinases modulates the secondary structure of the CTD and chromatin condensation. We review the arguments in favor of the involvement of H1 hyperphosphorylation in metaphase chromatin condensation and of partial phosphorylation in interphase chromatin relaxation. In addition, the interplay of histone H1 and other chromatin architectural proteins, such as proteins of the high-mobility group, protamines, and MeCP2, is associated with changes in chromatin structure.
Starting Page	83
Ending Page	91
Page Count	9
File Format	PDF
ISSN	00095915
Journal	Chromosoma
Volume Number	126
Issue Number	1
e-ISSN	14320886
Language	English
Publisher	Springer Berlin Heidelberg
Publisher Date	2016-04-21
Publisher Place	Berlin, Heidelberg
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	Histone H1 Intrinsic disorder Post-translational modifications Chromatin dynamics structure Chromatin condensation Cell Biology Developmental Biology Biochemistry Human Genetics Animal Genetics and Genomics Eukaryotic Microbiology
Content Type	Text
Resource Type	Article
Subject	Genetics Genetics (clinical)

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