Contributions of Histone Variants in Nucleosome Structure and Function

Nucleosome dynamics and properties are central to all forms of genomic activities. Among the core histones, H3 variants play a pivotal role in modulating nucleosome structure and function. Here, we focus on the impact of H3 variants on various facets of development. The deposition of the replicative H3 variant following DNA replication is essential for the transmission of the epigenomic information encoded in posttranscriptional modifications. Through this process, replicative H3 maintains cell fate while, in contrast, the replacement H3.3 variant opposes cell differentiation during early embryogenesis. In later steps of development, H3.3 and specialized H3 variants are emerging as new, important regulators of terminal cell differentiation, including neurons and gametes. The specific pathways that regulate the dynamics of the deposition of H3.3 are paramount during reprogramming events that drive zygotic activation and the initiation of a new cycle of development.

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Plant Histone HTB (H2B) Variants in Regulating Chromatin Structure and Function

Plants ◽

10.3390/plants9111435 ◽

2020 ◽

Vol 9 (11) ◽

pp. 1435

Author(s):

Janardan Khadka ◽

Anat Pesok ◽

Gideon Grafi

Keyword(s):

Arabidopsis Thaliana ◽

Chromatin Structure ◽

Developmental Stages ◽

Histone Variants ◽

Structure And Function ◽

Core Histone ◽

Histone H2b ◽

Histone Proteins ◽

Genes Encoding ◽

And Function

Besides chemical modification of histone proteins, chromatin dynamics can be modulated by histone variants. Most organisms possess multiple genes encoding for core histone proteins, which are highly similar in amino acid sequence. The Arabidopsis thaliana genome contains 11 genes encoding for histone H2B (HTBs), 13 for H2A (HTAs), 15 for H3 (HTRs), and 8 genes encoding for histone H4 (HFOs). The finding that histone variants may be expressed in specific tissues and/or during specific developmental stages, often displaying specific nuclear localization and involvement in specific nuclear processes suggests that histone variants have evolved to carry out specific functions in regulating chromatin structure and function and might be important for better understanding of growth and development and particularly the response to stress. In this review, we will elaborate on a group of core histone proteins in Arabidopsis, namely histone H2B, summarize existing data, and illuminate the potential function of H2B variants in regulating chromatin structure and function in Arabidopsis thaliana.

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2SDA-01 Structural basis of chromatin dynamics regulated by histone variants(2SDA Studies of dynamic chromatin structure and function to understand fundamentals of life,Symposium,The 52nd Annual Meeting of the Biophysical Society of Japan(BSJ2014))

Seibutsu Butsuri ◽

10.2142/biophys.54.s127_6 ◽

2014 ◽

Vol 54 (supplement1-2) ◽

pp. S127

Author(s):

Hitoshi Kurumizaka

Keyword(s):

Annual Meeting ◽

Chromatin Structure ◽

Histone Variants ◽

Structure And Function ◽

Structural Basis ◽

Chromatin Dynamics ◽

Biophysical Society ◽

And Function

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The Art of War: harnessing the epigenome against cancer

F1000Research ◽

10.12688/f1000research.12833.1 ◽

2018 ◽

Vol 7 ◽

pp. 141 ◽

Cited By ~ 5

Author(s):

Jonathan Nye ◽

Daniël P. Melters ◽

Yamini Dalal

Keyword(s):

Cancer Cells ◽

Chromatin Structure ◽

Histone Variants ◽

Structure And Function ◽

Histone Chaperones ◽

Growth And Survival ◽

Art Of War ◽

Chromatin Interactions ◽

And Function ◽

Target Cancer

Histone chaperones are indispensable regulators of chromatin structure and function. Recent work has shown that they are frequently mis-regulated in cancer, which can have profound consequences on tumor growth and survival. Here, we focus on chaperones for the essential H3 histone variants H3.3 and CENP-A, specifically HIRA, DAXX/ATRX, DEK, and HJURP. This review summarizes recent studies elucidating their roles in regulating chromatin and discusses how cancer-specific chromatin interactions can be exploited to target cancer cells.

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Nucleosome Structure and Function

Chemical Reviews ◽

10.1021/cr500373h ◽

2014 ◽

Vol 115 (6) ◽

pp. 2255-2273 ◽

Cited By ~ 187

Author(s):

Robert K. McGinty ◽

Song Tan

Keyword(s):

Structure And Function ◽

Nucleosome Structure ◽

And Function

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Nucleosome Structure and Function

The Histone Code and Beyond - Ernst Schering Research Foundation Workshop ◽

10.1007/3-540-37633-x_2 ◽

2006 ◽

pp. 29-46 ◽

Cited By ~ 12

Author(s):

J. V. Chodaparambil ◽

R. S. Edayathumangalam ◽

Y. Bao ◽

Y. -J. Park ◽

K. Luger

Keyword(s):

Structure And Function ◽

Nucleosome Structure ◽

And Function

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Structure and function of neural networks in the retina

Proceedings, annual meeting, Electron Microscopy Society of America ◽

10.1017/s0424820100102213 ◽

1988 ◽

Vol 46 ◽

pp. 26-27

Author(s):

Peter Sterling

Keyword(s):

Ganglion Cells ◽

Three Dimensional ◽

Structure And Function ◽

Synaptic Connections ◽

Visual Axis ◽

One Dimensional ◽

Cat Retina ◽

Ultrathin Sections ◽

And Function ◽

Insight Into

The synaptic connections in cat retina that link photoreceptors to ganglion cells have been analyzed quantitatively. Our approach has been to prepare serial, ultrathin sections and photograph en montage at low magnification (˜2000X) in the electron microscope. Six series, 100-300 sections long, have been prepared over the last decade. They derive from different cats but always from the same region of retina, about one degree from the center of the visual axis. The material has been analyzed by reconstructing adjacent neurons in each array and then identifying systematically the synaptic connections between arrays. Most reconstructions were done manually by tracing the outlines of processes in successive sections onto acetate sheets aligned on a cartoonist's jig. The tracings were then digitized, stacked by computer, and printed with the hidden lines removed. The results have provided rather than the usual one-dimensional account of pathways, a three-dimensional account of circuits. From this has emerged insight into the functional architecture.

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Osseointegration interface of calcified bone and endosseous implants

Proceedings, annual meeting, Electron Microscopy Society of America ◽

10.1017/s0424820100130110 ◽

1992 ◽

Vol 50 (2) ◽

pp. 1096-1097

Author(s):

K.E. Krizan ◽

J.E. Laffoon ◽

M.J. Buckley

Keyword(s):

Structure And Function ◽

Titanium Implants ◽

En Bloc ◽

Endosseous Implants ◽

Ultrastructural Studies ◽

The Past ◽

Cacodylate Buffer ◽

One Year ◽

And Function

With increase use of tissue-integrated prostheses in recent years it is a goal to understand what is happening at the interface between haversion bone and bulk metal. This study uses electron microscopy (EM) techniques to establish parameters for osseointegration (structure and function between bone and nonload-carrying implants) in an animal model. In the past the interface has been evaluated extensively with light microscopy methods. Today researchers are using the EM for ultrastructural studies of the bone tissue and implant responses to an in vivo environment. Under general anesthesia nine adult mongrel dogs received three Brånemark (Nobelpharma) 3.75 × 7 mm titanium implants surgical placed in their left zygomatic arch. After a one year healing period the animals were injected with a routine bone marker (oxytetracycline), euthanized and perfused via aortic cannulation with 3% glutaraldehyde in 0.1M cacodylate buffer pH 7.2. Implants were retrieved en bloc, harvest radiographs made (Fig. 1), and routinely embedded in plastic. Tissue and implants were cut into 300 micron thick wafers, longitudinally to the implant with an Isomet saw and diamond wafering blade [Beuhler] until the center of the implant was reached.

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Use of human autoantibodies and immunoelectron microscopy to study structure and function of the nucleolus and nuclear bodies

Proceedings, annual meeting, Electron Microscopy Society of America ◽

10.1017/s0424820100122939 ◽

1992 ◽

Vol 50 (1) ◽

pp. 506-507

Author(s):

Robert L. Ochs

Keyword(s):

Electron Microscopy ◽

Structure And Function ◽

Nuclear Bodies ◽

Nuclear Interior ◽

Coiled Bodies ◽

Interchromatin Granules ◽

And Function ◽

Conventional Electron Microscopy ◽

Perichromatin Granules ◽

Perichromatin Fibrils

By conventional electron microscopy, the formed elements of the nuclear interior include the nucleolus, chromatin, interchromatin granules, perichromatin granules, perichromatin fibrils, and various types of nuclear bodies (Figs. 1a-c). Of these structures, all have been reasonably well characterized structurally and functionally except for nuclear bodies. The most common types of nuclear bodies are simple nuclear bodies and coiled bodies (Figs. 1a,c). Since nuclear bodies are small in size (0.2-1.0 μm in diameter) and infrequent in number, they are often overlooked or simply not observed in any random thin section. The rat liver hepatocyte in Fig. 1b is a case in point. Historically, nuclear bodies are more prominent in hyperactive cells, they often occur in proximity to nucleoli (Fig. 1c), and sometimes they are observed to “bud off” from the nucleolar surface.

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Depletion and Reconstitution of Active E. Coli Ribosomes

Proceedings, annual meeting, Electron Microscopy Society of America ◽

10.1017/s0424820100116826 ◽

1975 ◽

Vol 33 ◽

pp. 640-641

Author(s):

M. Boublik ◽

W. Hellmann ◽

F. Jenkins

Keyword(s):

Protein Biosynthesis ◽

Large Subunit ◽

High Resolution Electron Microscopy ◽

Small Subunit ◽

Structure And Function ◽

Biologically Active ◽

Biological Macromolecules ◽

E Coli ◽

Resolution Electron ◽

And Function

Correlations between structure and function of biological macromolecules have been studied intensively for many years, mostly by indirect methods. High resolution electron microscopy is a unique tool which can provide such information directly by comparing the conformation of biopolymers in their biologically active and inactive state. We have correlated the structure and function of ribosomes, ribonucleoprotein particles which are the site of protein biosynthesis. 70S E. coli ribosomes, used in this experiment, are composed of two subunits - large (50S) and small (30S). The large subunit consists of 34 proteins and two different ribonucleic acid molecules. The small subunit contains 21 proteins and one RNA molecule. All proteins (with the exception of L7 and L12) are present in one copy per ribosome.This study deals with the changes in the fine structure of E. coli ribosomes depleted of proteins L7 and L12. These proteins are unique in many aspects.

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