The higher order structure of chicken erythrocyte chromosomes in vivo

Nature ◽  
1980 ◽  
Vol 288 (5791) ◽  
pp. 620-622 ◽  
Author(s):  
J. P. Langmore ◽  
C. Schutt
Keyword(s):  
Higher Order ◽  
Order Structure ◽  
Chicken Erythrocyte

scholarly journals Natural chromatin is heterogeneous and self-associates in vitro

2018 ◽  
Vol 29 (13) ◽  
pp. 1652-1663 ◽  
Author(s):  
Shujun Cai ◽  
Yajiao Song ◽  
Chen Chen ◽  
Jian Shi ◽  
Lu Gan
Keyword(s):  
Divalent Cations ◽  
Large Mass ◽  
Higher Order ◽  
Linker Histone ◽  
Order Structure ◽  
Face To Face ◽  
Chromatin Packing ◽  
Electron Cryotomography

The 30-nm fiber is commonly formed by oligonucleosome arrays in vitro but rarely found inside cells. To determine how chromatin higher-order structure is controlled, we used electron cryotomography (cryo-ET) to study the undigested natural chromatin released from two single-celled organisms in which 30-nm fibers have not been observed in vivo: picoplankton and yeast. In the presence of divalent cations, most of the chromatin from both organisms is condensed into a large mass in vitro. Rare irregular 30-nm fibers, some of which include face-to-face nucleosome interactions, do form at the periphery of this mass. In the absence of divalent cations, picoplankton chromatin decondenses into open zigzags. By contrast, yeast chromatin mostly remains condensed, with very few open motifs. Yeast chromatin packing is largely unchanged in the absence of linker histone and mildly decondensed when histones are more acetylated. Natural chromatin is therefore generally nonpermissive of regular motifs, even at the level of oligonucleosomes.

scholarly journals Regulation of the higher-order structure of chromatin by histones H1 and H5.

1981 ◽  
Vol 90 (2) ◽  
pp. 279-288 ◽  
Author(s):  
J Allan ◽  
G J Cowling ◽  
N Harborne ◽  
P Cattini ◽  
R Craigie ◽  
...  
Keyword(s):  
Spatial Organization ◽  
Single Species ◽  
Histone H1 ◽  
Higher Order ◽  
Linker Histone ◽  
Micrococcal Nuclease ◽  
Order Structure ◽  
Chicken Erythrocyte ◽  
Base Pairs ◽  
Native Chicken

Chicken erythrocyte chromatins containing a single species of linker histone, H1 or H5, have been prepared, using reassembly techniques developed previously. The reconstituted complexes possess the conformation of native chicken erythrocyte chromatin, as judged by chemical and structural criteria; saturation is reached when two molecules of linker histone are bound per nucleosome, as in native erythrocyte chromatin, which the resulting material resembles in its appearance in the electron microscope and quantitatively in its linear condensation factor relative to free DNA. The periodicity of micrococcal nuclease-sensitive sites in the linker regions associated with histone H1 or H5 is 10.4 base pairs, suggesting that the spatial organization of the linker region in the higher-order structure of chromatin is similar to that in isolated nucleosomes. The susceptible sites are cut at differing frequencies, as previously found for the nucleosome cores, leading to a characteristic distribution of intensities in the digests. The scission frequency of sites in the linker DNA depends additionally on the identity of the linker histone, suggesting that the higher-order structure is subject to secondary modulation by the associated histones.

scholarly journals Stability of the Higher-Order Structure of Chicken-Erythrocyte Chromatin in Solution

1981 ◽  
Vol 119 (3) ◽  
pp. 469-476 ◽  
Author(s):  
David L. BATES ◽  
P. Jonathan G. BUTLER ◽  
Edwin C. PEARSON ◽  
Jean O. THOMAS
Keyword(s):  
Higher Order ◽  
Order Structure ◽  
Chicken Erythrocyte

Aged and post-mitotic cells share a very stable higher-order structure in the cell nucleus in vivo

2010 ◽  
Vol 11 (6) ◽  
pp. 703-716 ◽  
Author(s):  
Janeth Alva-Medina ◽  
Myrna A. R. Dent ◽  
Armando Aranda-Anzaldo
Keyword(s):  
Cell Nucleus ◽  
Higher Order ◽  
Order Structure ◽  
Mitotic Cells

scholarly journals Higher order structure in a short repeat length chromatin.

1984 ◽  
Vol 98 (4) ◽  
pp. 1320-1327 ◽  
Author(s):  
J Allan ◽  
D C Rau ◽  
N Harborne ◽  
H Gould
Keyword(s):  
Higher Order ◽  
Chromatin Fiber ◽  
Repeat Length ◽  
Order Structure ◽  
Dependent Manner ◽  
Chicken Erythrocyte ◽  
Base Pairs ◽  
Short Repeat ◽  
Cortical Neurone

Polynucleosomes from calf brain cortical neurone nuclei have an average repeat length of less than 168 base pairs. The ability of this material to adopt higher order structure has been assessed by various physical techniques. Although containing on average less DNA per nucleosome than is required to form a chromatosome, this short repeat length chromatin folded in an H1 dependent manner to a structure with properties similar to those observed for longer repeat length chromatins such as that of chicken erythrocyte (McGhee, J.D., D.C. Rau, E. Charney, and G. Felsenfeld, 1980, Cell, 22:87-96). These observations are discussed in the context of H1 location in the higher order chromatin fiber.

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 Formation of membrane ridges and scallops by the F-BAR protein Nervous Wreck

2013 ◽  
Vol 24 (15) ◽  
pp. 2406-2418 ◽  
Author(s):  
Agata N. Becalska ◽  
Charlotte F. Kelley ◽  
Cristina Berciu ◽  
Tatiana B. Stanishneva-Konovalova ◽  
Xiaofeng Fu ◽  
...  
Keyword(s):  
Electrostatic Interactions ◽  
Higher Order ◽  
Order Structure ◽  
Structural Determinants ◽  
Dynamic Membrane ◽  
Bar Domain ◽  
Neuronal Protein ◽  
Positively Curved

Eukaryotic cells are defined by extensive intracellular compartmentalization, which requires dynamic membrane remodeling. FER/Cip4 homology-Bin/amphiphysin/Rvs (F-BAR) domain family proteins form crescent-shaped dimers, which can bend membranes into buds and tubules of defined geometry and lipid composition. However, these proteins exhibit an unexplained wide diversity of membrane-deforming activities in vitro and functions in vivo. We find that the F-BAR domain of the neuronal protein Nervous Wreck (Nwk) has a novel higher-order structure and membrane-deforming activity that distinguishes it from previously described F-BAR proteins. The Nwk F-BAR domain assembles into zigzags, creating ridges and periodic scallops on membranes in vitro. This activity depends on structural determinants at the tips of the F-BAR dimer and on electrostatic interactions of the membrane with the F-BAR concave surface. In cells, Nwk-induced scallops can be extended by cytoskeletal forces to produce protrusions at the plasma membrane. Our results define a new F-BAR membrane-deforming activity and illustrate a molecular mechanism by which positively curved F-BAR domains can produce a variety of membrane curvatures. These findings expand the repertoire of F-BAR domain mediated membrane deformation and suggest that unique modes of higher-order assembly can define how these proteins sculpt the membrane.

scholarly journals Continued Stabilization of the Nuclear Higher-Order Structure of Post-Mitotic Neurons In Vivo

PLoS ONE ◽  
2011 ◽  
Vol 6 (6) ◽  
pp. e21360 ◽  
Author(s):  
Janeth Alva-Medina ◽  
Apolinar Maya-Mendoza ◽  
Myrna A. R. Dent ◽  
Armando Aranda-Anzaldo
Keyword(s):  
Higher Order ◽  
Order Structure

Chromatin structure of eukaryotic promoters: a changing perspective

2002 ◽  
Vol 80 (3) ◽  
pp. 295-300 ◽  
Author(s):  
Philippe T Georgel
Keyword(s):  
Transcriptional Activation ◽  
Structural Changes ◽  
Current Knowledge ◽  
Higher Order ◽  
Current View ◽  
Order Structure ◽  
Chromatin Dynamics ◽  
Technical Developments ◽  
Agarose Electrophoresis

Over the past few years, many studies have attempted to determine the role of nucleosomes as both positive and negative transcription regulators. The emphasis has mostly centered on chromatin remodeling activities and histone modifications, leaving the question of the influence of the higher-order structure out of the spotlight. Recent technical developments allowing direct measurements of size and mechanical properties of in vivo assembled chromatin may shed light on this poorly understood area. This article presents a brief summary of the current knowledge on transcription-dependent chromatin dynamics and how a rather simple agarose electrophoresis method may change the current view on structural changes linked to transcriptional activation of chromatin.Key words: chromatin, higher-order structure, quantitative agarose gel electrophoresis.

Increased stability of the higher order structure of chicken erythrocyte chromatin: nanosecond anisotropy studies of intercalated ethidium

Biochemistry ◽  
1985 ◽  
Vol 24 (6) ◽  
pp. 1291-1297 ◽  
Author(s):  
Ikuo Ashikawa ◽  
Kazuhiko Kinosita ◽  
Akira Ikegami ◽  
Yoshifumi Nishimura ◽  
Masamichi Tsuboi
Keyword(s):  
Higher Order ◽  
Order Structure ◽  
Chicken Erythrocyte
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