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 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 Higher-order structure of nucleosome oligomers from short-repeat chromatin.

1983 ◽  
Vol 2 (8) ◽  
pp. 1367-1372 ◽  
Author(s):  
E.C. Pearson ◽  
P.J. Butler ◽  
J.O. Thomas
Keyword(s):  
Higher Order ◽  
Order Structure ◽  
Short Repeat

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

scholarly journals Higher-order structure of the 30-nm chromatin fiber revealed by cryo-EM

IUBMB Life ◽  
2016 ◽  
Vol 68 (11) ◽  
pp. 873-878 ◽  
Author(s):  
Ping Zhu ◽  
Guohong Li
Keyword(s):  
Higher Order ◽  
Chromatin Fiber ◽  
Order Structure

Transitions between in situ and isolated chromatin

1993 ◽  
Vol 105 (2) ◽  
pp. 551-561 ◽  
Author(s):  
P.J. Giannasca ◽  
R.A. Horowitz ◽  
C.L. Woodcock
Keyword(s):  
Higher Order ◽  
Chromatin Fiber ◽  
Sperm Chromatin ◽  
Order Structure ◽  
Native State ◽  
Chromatin Fibers

We show that the mechanism by which chromatin displaying higher-order structure is usually isolated from nuclei involves a transition to an extended nucleosomal arrangement. After being released from nuclei, chromatin must refold in order to produce the typical chromatin fibers observed in solution. For starfish sperm chromatin with a long nucleosome repeat (222 bp), isolated fibers are significantly wider than those in the nucleus, indicating that the refolding process does not regenerate the native higher-order structure. We also propose that for typical eukaryotic nuclei, the concept that the native state of the (inactive) bulk of the genome is a chromatin fiber with defined architecture be reconsidered.

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 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.

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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