scholarly journals ISWI Regulates Higher-Order Chromatin Structure and Histone H1 Assembly In Vivo

PLoS Biology ◽  
2007 ◽  
Vol 5 (9) ◽  
pp. e232 ◽  
Author(s):  
Davide F. V Corona ◽  
Giorgia Siriaco ◽  
Jennifer A Armstrong ◽  
Natalia Snarskaya ◽  
Stephanie A McClymont ◽  
...  
Keyword(s):  
Chromatin Structure ◽  
Histone H1 ◽  
Higher Order

scholarly journals MTA1 regulates higher-order chromatin structure and histone H1-chromatin interaction in-vivo

2014 ◽  
Vol 9 (1) ◽  
pp. 218-235 ◽  
Author(s):  
Jian Liu ◽  
Haijuan Wang ◽  
Fei Ma ◽  
Dongkui Xu ◽  
Yanan Chang ◽  
...  
Keyword(s):  
Chromatin Structure ◽  
Histone H1 ◽  
Higher Order ◽  
Chromatin Interaction

scholarly journals The Drosophila Mi-2 Chromatin-Remodeling Factor Regulates Higher-Order Chromatin Structure and Cohesin Dynamics In Vivo

PLoS Genetics ◽  
2012 ◽  
Vol 8 (8) ◽  
pp. e1002878 ◽  
Author(s):  
Barbara Fasulo ◽  
Renate Deuring ◽  
Magdalena Murawska ◽  
Maria Gause ◽  
Kristel M. Dorighi ◽  
...  
Keyword(s):  
Chromatin Remodeling ◽  
Chromatin Structure ◽  
Higher Order

scholarly journals The ISWI Chromatin-Remodeling Protein Is Required for Gene Expression and the Maintenance of Higher Order Chromatin Structure In Vivo

2000 ◽  
Vol 5 (2) ◽  
pp. 355-365 ◽  
Author(s):  
Renate Deuring ◽  
Laura Fanti ◽  
Jennifer A Armstrong ◽  
Melinda Sarte ◽  
Ophelia Papoulas ◽  
...  
Keyword(s):  
Gene Expression ◽  
Chromatin Remodeling ◽  
Chromatin Structure ◽  
Higher Order

scholarly journals Highly disordered histone H1−DNA model complexes and their condensates

2018 ◽  
Vol 115 (47) ◽  
pp. 11964-11969 ◽  
Author(s):  
Abigail L. Turner ◽  
Matthew Watson ◽  
Oscar G. Wilkins ◽  
Laura Cato ◽  
Andrew Travers ◽  
...  
Keyword(s):  
Posttranslational Modifications ◽  
Chromatin Condensation ◽  
Bound State ◽  
Histone H1 ◽  
Higher Order ◽  
Disordered Proteins ◽  
Order Structure ◽  
Dependent Manner ◽  
Model Complexes

Disordered proteins play an essential role in a wide variety of biological processes, and are often posttranslationally modified. One such protein is histone H1; its highly disordered C-terminal tail (CH1) condenses internucleosomal linker DNA in chromatin in a way that is still poorly understood. Moreover, CH1 is phosphorylated in a cell cycle-dependent manner that correlates with changes in the chromatin condensation level. Here we present a model system that recapitulates key aspects of the in vivo process, and also allows a detailed structural and biophysical analysis of the stages before and after condensation. CH1 remains disordered in the DNA-bound state, despite its nanomolar affinity. Phase-separated droplets (coacervates) form, containing higher-order assemblies of CH1/DNA complexes. Phosphorylation at three serine residues, spaced along the length of the tail, has little effect on the local properties of the condensate. However, it dramatically alters higher-order structure in the coacervate and reduces partitioning to the coacervate phase. These observations show that disordered proteins can bind tightly to DNA without a disorder-to-order transition. Importantly, they also provide mechanistic insights into how higher-order structures can be exquisitely sensitive to perturbation by posttranslational modifications, thus broadening the repertoire of mechanisms that might regulate chromatin and other macromolecular assemblies.

scholarly journals Parathymosin Affects the Binding of Linker Histone H1 to Nucleosomes and Remodels Chromatin Structure

2005 ◽  
Vol 280 (16) ◽  
pp. 16143-16150 ◽  
Author(s):  
Goran Martic ◽  
Zoe Karetsou ◽  
Katerina Kefala ◽  
Anastasia S. Politou ◽  
Cedric R. Clapier ◽  
...  
Keyword(s):  
Chromatin Structure ◽  
Histone H1 ◽  
Higher Order ◽  
Linker Histone ◽  
Laser Scanning Microscopy ◽  
Micrococcal Nuclease ◽  
Confocal Laser ◽  
Dependent Manner ◽  
Linker Histone H1

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.

scholarly journals Alleviation of histone H1-mediated transcriptional repression and chromatin compaction by the acidic activation region in chromosomal protein HMG-14.

1997 ◽  
Vol 17 (10) ◽  
pp. 5843-5855 ◽  
Author(s):  
H F Ding ◽  
M Bustin ◽  
U Hansen
Keyword(s):  
Rna Polymerase Ii ◽  
Chromatin Structure ◽  
Transcriptional Activation ◽  
Transcriptional Repression ◽  
Simian Virus 40 ◽  
Histone H1 ◽  
Simian Virus ◽  
Higher Order ◽  
Chromosomal Protein ◽  
C Terminus

Histone H1 promotes the generation of a condensed, transcriptionally inactive, higher-order chromatin structure. Consequently, histone H1 activity must be antagonized in order to convert chromatin to a transcriptionally competent, more extended structure. Using simian virus 40 minichromosomes as a model system, we now demonstrate that the nonhistone chromosomal protein HMG-14, which is known to preferentially associate with active chromatin, completely alleviates histone H1-mediated inhibition of transcription by RNA polymerase II. HMG-14 also partially disrupts histone H1-dependent compaction of chromatin. Both the transcriptional enhancement and chromatin-unfolding activities of HMG-14 are mediated through its acidic, C-terminal region. Strikingly, transcriptional and structural activities of HMG-14 are maintained upon replacement of the C-terminal fragment by acidic regions from either GAL4 or HMG-2. These data support the model that the acidic C terminus of HMG-14 is involved in unfolding higher-order chromatin structure to facilitate transcriptional activation of mammalian genes.

Influence of linker histone H1 on chromatin remodeling

2001 ◽  
Vol 79 (3) ◽  
pp. 317-324 ◽  
Author(s):  
David A Hill
Keyword(s):  
Key Words ◽  
Chromatin Remodeling ◽  
Chromatin Structure ◽  
Central Area ◽  
Histone H1 ◽  
Higher Order ◽  
Linker Histone ◽  
Linker Histone H1 ◽  
Chromatin Remodeling Complexes ◽  
Cellular Dna

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.

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