scholarly journals Participation of core histone "tails" in the stabilization of the chromatin solenoid.

1982 ◽  
Vol 93 (2) ◽  
pp. 285-297 ◽  
Author(s):  
J Allan ◽  
N Harborne ◽  
D C Rau ◽  
H Gould
Keyword(s):  
Core Histone ◽  
Order Structure ◽  
Histone Tails ◽  
Linker Histones ◽  
Nucleosome Core ◽  
The Core ◽  
Core Histones ◽  
Minor Part ◽  
Core Histone Tail ◽  
A Minor

We show here that the solenoid is maintained by the combination of linker histones and the nonglobular, highly basic "tails" of the core histones, which play only a minor part in the formation of the nucleosome core (Whitlock and Simpson, 1977. J. Biol. Chem. 252:6,516--6,520; Lilley and Tatchell, 1977. Nucleic Acids Res. 4:2,039--2,055; and Whitlock and Stein, 1978. J. Biol. Chem. 253:3,857--3,861). Polynucleosomes that contain core histones devoid of tails remain substantially unfolded under conditions otherwise favorable for the formation of solenoids. The tails can be replaced by extraneous basic polypeptides and in the presence of the linker histones the solenoid structure is then spontaneously recovered, as judged by a wide variety of structural criteria. The inference is that the core histone tail segments function by providing electrostatic shielding of the DNA charge and at the same time bridging adjacent nucleosomes in the solenoid. Our results carry the further implication that posttranscriptional modifications, such as acetylation of epsilon-amino groups, that reduce the positive charge of the core histone tails will tend to destabilize the higher-order structure and could thus render the DNA with which they are associated more readily available for transcription.

Formation and dynamics of Saturn and its disk simulated by using a new N-body model

Open Physics ◽  
2003 ◽  
Vol 1 (4) ◽  
Author(s):  
A. Pavlov ◽  
Y. Pavlova
Keyword(s):  
Surface Density ◽  
Electromagnetic Interaction ◽  
The Core ◽  
Body Model ◽  
Magnetic Forces ◽  
Axis Of Rotation ◽  
Gravitational Model ◽  
Minor Part ◽  
Body Self ◽  
A Minor

AbstractThe formation of Saturn and its disk is simulated using a new N-body self-gravitational model. It is demonstrated that the formation of the disk and the planet is the result of gravitational contraction of a slowly rotated particle cloud that have a shape of slightly deformed sphere. The sphere was flattened by a coefficient of 0.8 along the axis of rotation. During the gravitational contraction, the major part of the cloud transformed into a planet and a minor part transformed into a disk. The thin structured disk is a result of the electromagnetic interaction in which the magnetic forces acting on charged particles of the cloud originate in the core of the planet. The simulation program gives such parameters of Saturn as the escape velocity of about 35 km/s at the surface, density, rotational velocities of the rings and temperature distribution.

Diversification of the Histone Fold Motif in Plants: Evolution of New Functional Roles

2016 ◽  
Vol 1 (1) ◽  
pp. 63 ◽  
Author(s):  
Amish Kumar ◽  
Gitanjali Yadav
Keyword(s):  
Gene Families ◽  
Chromatin Accessibility ◽  
Core Histone ◽  
Alpha Helices ◽  
Functional Roles ◽  
Histone Fold ◽  
Nuclear Factor Y ◽  
The Core ◽  
Large Gene ◽  
Core Histones

<p>The Histone fold motif (HFM) is one of the most conserved structural motifs in biology, mainly found in the core histone sub-units of all eukaryotes. The HFM represents a helix-strand-helix motif having three alpha helices connected by two loops/beta strands. This helix-strand-helix motif has the unique property of binding strongly with proteins as well as with DNA. Apart from core histones, the HFM has been reported in a variety of other proteins in all forms of life. In this work, we review the various classes of proteins that contain the HFM, as well as the diverse roles played by these proteins in the plant kingdom. As will be clear from this review, formation of the core histones through multi-merisation is not the only role played by this conserved fold, although the characteristic ability of the HFM to dimerize with suitable partner proteins has been used by nature to perform several non-core-histone functions. Most of the information about plant HFM containing proteins, such as identification and classification, has been done based on homology with yeast and animal counterparts. However, the ability of plants genomes to duplicate extensively has led to the existence of large gene families of the HFM containing proteins, unlike other eukaryotes. Plant HFM containing proteins can broadly be classified under the following major categories; TBP-associated factors (TAF), Nuclear Factor Y (NF-Y), Dr1/DrAp1 proteins and the chromatin accessibility complex (CHRAC). These proteins families are known to be involved in transcriptional regulation, co-activation and chromosome maintenance. Partner recognition through dimer formation remains a major conserved feature of these groups when compared with core histone sub-units.</p>

A compendium of the histone H1 family of somatic subtypes: An elusive cast of characters and their characteristics

2001 ◽  
Vol 79 (3) ◽  
pp. 289-304 ◽  
Author(s):  
Missag H Parseghian ◽  
Barbara A Hamkalo
Keyword(s):  
Historical Context ◽  
Histone H1 ◽  
General Function ◽  
Linker Histones ◽  
Chromatin Compaction ◽  
The Core ◽  
The Past ◽  
Current State ◽  
Core Histones

The last 35 years has seen a substantial amount of information collected about the somatic H1 subtypes, yet much of this work has been overshadowed by research into highly divergent isoforms of H1, such as H5. Reports from several laboratories in the past few years have begun to call into question some of the traditional views regarding the general function of linker histones and their heterogeneity. Hence, the impression in some circles is that less is known about these ubiquitous nuclear proteins as compared with the core histones. The goal of the following review is to acquaint the reader with the ubiquitous somatic H1s by categorizing them and their characteristics into several classes. The reasons for our current state of misunderstanding is put into a historical context along with recent controversies centering on the role of H1 in the nucleus. Finally, we propose a model that may explain the functional role of H1 heterogeneity in chromatin compaction.Key words: histone H1, linker histones, chromatin organization, chromatin compaction, heat shock.

Modulation of the relative trypsin sensitivities of the core histone ‘tails’

FEBS Letters ◽  
1983 ◽  
Vol 155 (1) ◽  
pp. 88-92 ◽  
Author(s):  
Nerina Harborne ◽  
James Allan
Keyword(s):  
Core Histone ◽  
Histone Tails ◽  
The Core

scholarly journals Preferential interaction of the core histone tail domains with linker DNA

2001 ◽  
Vol 98 (12) ◽  
pp. 6599-6604 ◽  
Author(s):  
D. Angelov ◽  
J. M. Vitolo ◽  
V. Mutskov ◽  
S. Dimitrov ◽  
J. J. Hayes
Keyword(s):  
Core Histone ◽  
Histone Tail ◽  
Preferential Interaction ◽  
The Core ◽  
Core Histone Tail

scholarly journals Hdac3, Setdb1, and Kap1 mark H3K9me3/H3K14ac bivalent regions in young and aged liver

2019 ◽  
Author(s):  
Andrew J. Price ◽  
Mohan C. Manjegowda ◽  
Irina M. Bochkis
Keyword(s):  
Gene Expression ◽  
Location Analysis ◽  
Histone Tails ◽  
Post Translational Modifications ◽  
The Core ◽  
Expression Of Genes ◽  
Genome Wide ◽  
Core Histones ◽  
Chromatin Profiling ◽  
Cholesterol Secretion

SummaryPost-translational modifications of histone tails play a crucial role in gene regulation. Here, we performed chromatin profiling by quantitative targeted mass spectrometry to assess all possible modifications of the core histones. We discovered a novel bivalent combination, a dually-marked H3K9me3/H3K14ac modification in the liver, that is significantly decreased in old hepatocytes. Subsequent genome-wide location analysis (ChIP-Seq) identified 1032 and 668 bivalent regions in young and old livers, respectively, with 280 in common. Histone H3K9 deacetylase Hdac3, as well as H3K9 methyltransferase Setdb1, found in complex Kap1, occupied bivalent regions in both young and old livers, correlating to presence of H3K9me3. Expression of genes associated with bivalent regions in young liver, including those regulating cholesterol secretion and triglyceride synthesis, is upregulated in old liver once the bivalency is lost. Hence, H3K9me3/H3K14ac dually-marked regions define a poised inactive state that is resolved with loss of one or both of the chromatin marks, which subsequently leads to change in gene expression.

scholarly journals Dynamic networks observed in the nucleosome core particles couple the histone globular domains with DNA

2020 ◽  
Vol 3 (1) ◽  
Author(s):  
Xiangyan Shi ◽  
Chinmayi Prasanna ◽  
Aghil Soman ◽  
Konstantin Pervushin ◽  
Lars Nordenskiöld
Keyword(s):  
Dynamic Networks ◽  
Structural Features ◽  
Epigenetic Changes ◽  
Internal Dynamics ◽  
Histone Tails ◽  
Multiple Timescales ◽  
Nucleosome Core ◽  
The Core ◽  
Nucleosome Core Particles ◽  
Core Particles

Abstract The dynamics of eukaryotic nucleosomes are essential in gene activity and well regulated by various factors. Here, we elucidated the internal dynamics at multiple timescales for the human histones hH3 and hH4 in the Widom 601 nucleosome core particles (NCP), suggesting that four dynamic networks are formed by the residues exhibiting larger-scale μs-ms motions that extend from the NCP core to the histone tails and DNA. Furthermore, despite possessing highly conserved structural features, histones in the telomeric NCP exhibit enhanced μs-ms dynamics in the globular sites residing at the identified dynamic networks and in a neighboring region. In addition, higher mobility was observed for the N-terminal tails of hH3 and hH4 in the telomeric NCP. The results demonstrate the existence of dynamic networks in nucleosomes, through which the center of the core regions could interactively communicate with histone tails and DNA to potentially propagate epigenetic changes.

Physical methods used to study core histone tail structures and interactions in solutionThis paper is one of a selection of papers published in this Special Issue, entitled 27th International West Coast Chromatin and Chromosome Conference, and has undergone the Journal's usual peer review process.

2006 ◽  
Vol 84 (4) ◽  
pp. 578-588 ◽  
Author(s):  
Xiaodong Wang ◽  
Jeffrey J. Hayes
Keyword(s):  
Peer Review Process ◽  
Regulatory Elements ◽  
Core Histone ◽  
Histone Tail ◽  
Tertiary Structures ◽  
Post Translational Modifications ◽  
Binding Behavior ◽  
The Core ◽  
Solution Methods ◽  
Core Histone Tail

The core histone tail domains are key regulatory elements in chromatin. The tails are essential for folding oligonucleosomal arrays into both secondary and tertiary structures, and post-translational modifications within these domains can directly alter DNA accessibility. Unfortunately, there is little understanding of the structures and interactions of the core histone tail domains or how post-translational modifications within the tails may alter these interactions. Here we review NMR, thermal denaturation, cross-linking, and other selected solution methods used to define the general structures and binding behavior of the tail domains in various chromatin environments. All of these methods indicate that the tail domains bind primarily electrostatically to sites within chromatin. The data also indicate that the tails adopt specific structures when bound to DNA and that tail structures and interactions are plastic, depending on the specific chromatin environment. In addition, post-translational modifications, such as acetylation, can directly alter histone tail structures and interactions.

scholarly journals Intra- and inter-nucleosome interactions of the core histone tail domains in higher-order chromatin structure

Chromosoma ◽  
2013 ◽  
Vol 123 (1-2) ◽  
pp. 3-13 ◽  
Author(s):  
Sharon Pepenella ◽  
Kevin J. Murphy ◽  
Jeffrey J. Hayes
Keyword(s):  
Chromatin Structure ◽  
Higher Order ◽  
Core Histone ◽  
Histone Tail ◽  
The Core ◽  
Core Histone Tail
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