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Izzo, A.* ; Kamieniarz, K.* ; Schneider, R.*

The histone H1 family: Specific members, specific functions?

Biol. Chem. 389, 333-343 (2008)
DOI PMC
Open Access Gold as soon as Publ. Version/Full Text is submitted to ZB.
The linker histone H1 binds to the DNA entering and exiting the nucleosomal core particle and has an important role in establishing and maintaining higher order chromatin structures. H1 forms a complex family of related proteins with distinct species, tissue and developmental specificity. In higher eukaryotes all H1 variants have the same general structure, consisting of a central conserved globular domain and less conserved N-terminal and C-terminal tails. These tails are moderately conserved among species, but differ among variants, suggesting a specific function for each H1 variant. Due to compensatory mechanisms and to the lack of proper tools, it has been very difficult to study the biological role of individual variants in chromatin-mediated processes. Our knowledge about H1 variants is indeed limited, and in vitro and in vivo observations have often been contradictory. Therefore, H1 variants were considered to be functionally redundant. However, recent knockout studies and biochemical analyses in different organisms have revealed exciting new insights into the specificity and mechanisms of actions of the H1 family members. Here, we collect and compare the available literature about H1 variants and discuss possible specific roles that challenge the concept of H1 being a mere structural component of chromatin and a general repressor of transcription.
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Publication type Article: Journal article
Document type Scientific Article
Language english
Publication Year 2008
HGF-reported in Year 0
ISSN (print) / ISBN 1431-6730
e-ISSN 1437-4315
Quellenangaben Volume: 389, Issue: 4, Pages: 333-343 Article Number: , Supplement: ,
Publisher de Gruyter
Reviewing status Peer reviewed
POF-Topic(s) 30203 - Molecular Targets and Therapies
Research field(s) Helmholtz Diabetes Center
PSP Element(s) G-502800-001
PubMed ID 18208346
Erfassungsdatum 2008-12-31