Influence of linker histone H1 on chromatin remodeling

2001 ◽  
Vol 79 (3) ◽  
pp. 317-324 ◽  
Author(s):  
David A Hill

Chromatin-remodeling complexes have been a central area of focus for research dealing with accessing cellular DNA sequestered in chromatin. Although the linker histone H1 plays a major role in promoting and maintaining higher-order chromatin structure, it has been noticeably absent from assays utilizing chromatin-remodeling enzymes. This review focuses on two ATP-dependent chromatin-remodeling complexes, Drosophila ISWI and mammalian SWI/SNF, that have been assayed using chromatin templates containing histone H1.Key words: SWI/SNF, ISWI, chromatin remodeling, histone H1.

2005 ◽  
Vol 280 (16) ◽  
pp. 16143-16150 ◽  
Author(s):  
Goran Martic ◽  
Zoe Karetsou ◽  
Katerina Kefala ◽  
Anastasia S. Politou ◽  
Cedric R. Clapier ◽  
...  

Linker histone H1 is the major factor that stabilizes higher order chromatin structure and modulates the action of chromatin-remodeling enzymes. We have previously shown that parathymosin, an acidic, nuclear protein binds to histone H1in vitroandin vivo. Confocal laser scanning microscopy reveals a nuclear punctuate staining of the endogenous protein in interphase cells, which is excluded from dense heterochromatic regions. Using anin vitrochromatin reconstitution system under physiological conditions, we show here that parathymosin (ParaT) inhibits the binding of H1 to chromatin in a dose-dependent manner. Consistent with these findings, H1-containing chromatin assembled in the presence of ParaT has reduced nucleosome spacing. These observations suggest that interaction of the two proteins might result in a conformational change of H1. Fluorescence spectroscopy and circular dichroism-based measurements on mixtures of H1 and ParaT confirm this hypothesis. Human sperm nuclei challenged with ParaT become highly decondensed, whereas overexpression of green fluorescent protein- or FLAG-tagged protein in HeLa cells induces global chromatin decondensation and increases the accessibility of chromatin to micrococcal nuclease digestion. Our data suggest a role of parathymosin in the remodeling of higher order chromatin structure through modulation of H1 interaction with nucleosomes and point to its involvement in chromatin-dependent functions.


2012 ◽  
Vol 76 (12) ◽  
pp. 2261-2266 ◽  
Author(s):  
Eloise PRIETO ◽  
Kohji HIZUME ◽  
Toshiro KOBORI ◽  
S. H. YOSHIMURA ◽  
Kunio TAKEYASU

FEBS Letters ◽  
2018 ◽  
Vol 592 (14) ◽  
pp. 2414-2424 ◽  
Author(s):  
Satoshi Funaya ◽  
Masatoshi Ooga ◽  
Masataka G. Suzuki ◽  
Fugaku Aoki

2014 ◽  
Vol 14 (1) ◽  
pp. 33-42 ◽  
Author(s):  
Andrzej Kowalski ◽  
Jan Pałyga

Abstract A purpose of this study was to evaluate genetic diversity in duck populations based on polymorphic variants (H1.a, H1.b and H1.z) of linker histone H1. The study was performed using conservative brown-feathered Khaki Campbell (Kh1) and Orpington (Or) populations and white-feathered Pekin (P77) duck breeding line. While no significant distortion between both brown-feathered duck populations was noted (P>0.05), the allele frequencies at histone H1 polymorphic loci were found to differ significantly between brown-feathered and white-feathered duck flocks (P<0.001). While the alleles a1, b1 and z1 were detected in all three duck lines, the alleles a2 and b2 missed in the line P77 were found in the Kh1 and Or populations. A rare allele z2 not detected in a homozygous state during screening our duck populations was found to occur only in heterozygous P77 duck individuals (z1z2). After a purpose mating of these heterozygous P77 birds, the homozygous individuals (z2) were obtained in their offspring. The uneven distribution of the alleles for polymorphic histone H1 variants among duck populations seems to suggest that they are not functionally equivalent and, therefore, might have a differential influence on chromatin structure and/or function leading to line-specific phenotypic effects in duck.


2021 ◽  
Vol 12 (1) ◽  
Author(s):  
Eva Höllmüller ◽  
Simon Geigges ◽  
Marie L. Niedermeier ◽  
Kai-Michael Kammer ◽  
Simon M. Kienle ◽  
...  

AbstractDecoding the role of histone posttranslational modifications (PTMs) is key to understand the fundamental process of epigenetic regulation. This is well studied for PTMs of core histones but not for linker histone H1 in general and its ubiquitylation in particular due to a lack of proper tools. Here, we report on the chemical synthesis of site-specifically mono-ubiquitylated H1.2 and identify its ubiquitin-dependent interactome on a proteome-wide scale. We show that site-specific ubiquitylation of H1 at position K64 modulates interactions with deubiquitylating enzymes and the deacetylase SIRT1. Moreover, it affects H1-dependent chromatosome assembly and phase separation resulting in a more open chromatosome conformation generally associated with a transcriptionally active chromatin state. In summary, we propose that site-specific ubiquitylation plays a general regulatory role for linker histone H1.


2021 ◽  
Vol 12 (1) ◽  
Author(s):  
Pierre Bourguet ◽  
Colette L. Picard ◽  
Ramesh Yelagandula ◽  
Thierry Pélissier ◽  
Zdravko J. Lorković ◽  
...  

AbstractIn flowering plants, heterochromatin is demarcated by the histone variant H2A.W, elevated levels of the linker histone H1, and specific epigenetic modifications, such as high levels of DNA methylation at both CG and non-CG sites. How H2A.W regulates heterochromatin organization and interacts with other heterochromatic features is unclear. Here, we create a h2a.w null mutant via CRISPR-Cas9, h2a.w-2, to analyze the in vivo function of H2A.W. We find that H2A.W antagonizes deposition of H1 at heterochromatin and that non-CG methylation and accessibility are moderately decreased in h2a.w-2 heterochromatin. Compared to H1 loss alone, combined loss of H1 and H2A.W greatly increases accessibility and facilitates non-CG DNA methylation in heterochromatin, suggesting co-regulation of heterochromatic features by H2A.W and H1. Our results suggest that H2A.W helps maintain optimal heterochromatin accessibility and DNA methylation by promoting chromatin compaction together with H1, while also inhibiting excessive H1 incorporation.


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