scholarly journals Changes in chromatin structure induced by EDTA treatment and partial removal of histone H1

1977 ◽  
Vol 4 (9) ◽  
pp. 3017-3028 ◽  
Author(s):  
Yu. Yu. Vengerov ◽  
V. I. Popenko
Keyword(s):  
Chromatin Structure ◽  
Histone H1 ◽  
Partial Removal ◽  
Edta Treatment

scholarly journals Integrase-Specific Enhancement and Suppression of Retroviral DNA Integration by Compacted Chromatin Structure In Vitro

2004 ◽  
Vol 78 (11) ◽  
pp. 5848-5855 ◽  
Author(s):  
Konstantin D. Taganov ◽  
Isabel Cuesta ◽  
René Daniel ◽  
Lisa Ann Cirillo ◽  
Richard A. Katz ◽  
...  
Keyword(s):  
Transcription Factors ◽  
Chromatin Structure ◽  
Site Selection ◽  
Integration Site ◽  
Histone H1 ◽  
Detectable Effect ◽  
Host Chromosome ◽  
Dna Integration ◽  
Hiv 1

ABSTRACT Integration of viral DNA into the host chromosome is an obligatory step in retroviral replication and is dependent on the activity of the viral enzyme integrase. To examine the influence of chromatin structure on retroviral DNA integration in vitro, we used a model target comprising a 13-nucleosome extended array that includes binding sites for specific transcription factors and can be compacted into a higher-ordered structure. We found that the efficiency of in vitro integration catalyzed by human immunodeficiency virus type 1 (HIV-1) integrase was decreased after compaction of this target with histone H1. In contrast, integration by avian sarcoma virus (ASV) integrase was more efficient after compaction by either histone H1 or a high salt concentration, suggesting that the compacted structure enhances this reaction. Furthermore, although site-specific binding of transcription factors HNF3 and GATA4 blocked ASV DNA integration in extended nucleosome arrays, local opening of H1-compacted chromatin by HNF3 had no detectable effect on integration, underscoring the preference of ASV for compacted chromatin. Our results indicate that chromatin structure affects integration site selection of the HIV-1 and ASV integrases in opposite ways. These distinct properties of integrases may also affect target site selection in vivo, resulting in an important bias against or in favor of integration into actively transcribed host DNA.

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 Pin1 promotes histone H1 dephosphorylation and stabilizes its binding to chromatin

2013 ◽  
Vol 203 (1) ◽  
pp. 57-71 ◽  
Author(s):  
Nikhil Raghuram ◽  
Hilmar Strickfaden ◽  
Darin McDonald ◽  
Kylie Williams ◽  
He Fang ◽  
...  
Keyword(s):  
Rna Polymerase Ii ◽  
Chromatin Structure ◽  
Transcriptional Activation ◽  
Binding Sites ◽  
Histone H1 ◽  
Dependent Manner ◽  
Prolyl Isomerase ◽  
Proline Isomerization ◽  
The Stability

Histone H1 plays a crucial role in stabilizing higher order chromatin structure. Transcriptional activation, DNA replication, and chromosome condensation all require changes in chromatin structure and are correlated with the phosphorylation of histone H1. In this study, we describe a novel interaction between Pin1, a phosphorylation-specific prolyl isomerase, and phosphorylated histone H1. A sub-stoichiometric amount of Pin1 stimulated the dephosphorylation of H1 in vitro and modulated the structure of the C-terminal domain of H1 in a phosphorylation-dependent manner. Depletion of Pin1 destabilized H1 binding to chromatin only when Pin1 binding sites on H1 were present. Pin1 recruitment and localized histone H1 phosphorylation were associated with transcriptional activation independent of RNA polymerase II. We thus identify a novel form of histone H1 regulation through phosphorylation-dependent proline isomerization, which has consequences on overall H1 phosphorylation levels and the stability of H1 binding to chromatin.

Influence of histone H1 on chromatin structure

1980 ◽  
Vol 94 (2) ◽  
pp. 535-541 ◽  
Author(s):  
Christian Marion ◽  
Bernard Roux
Keyword(s):  
Chromatin Structure ◽  
Histone H1

Poly(ADP-ribosyl)ation of chromatin: kinetics of relaxation and its effect on chromatin solubility

1985 ◽  
Vol 63 (7) ◽  
pp. 764-773 ◽  
Author(s):  
André Frechette ◽  
Ann Huletsky ◽  
Rémy J. Aubin ◽  
Gilbert de Murcia ◽  
Paul Mandel ◽  
...  
Keyword(s):  
Electron Microscopy ◽  
Enzyme Activity ◽  
Chromatin Structure ◽  
Microscopic Examination ◽  
Electron Microscopic Examination ◽  
Histone H1 ◽  
Electrophoretic Separation ◽  
Electron Microscopic ◽  
Kinetics Of ◽  
Modified Forms

We have studied the kinetics of relaxation of poly(ADP-ribosyl)ated polynucleosomes produced by endogenous enzyme activity by comparing the generation of hyper(ADP-ribosyl)ated histone H1 and its effect on the chromatin structure as revealed by electron microscopy. A correlation can be established between the appearance of histone H1 modified forms and the localized relaxation of the chromatin. We have also noticed, in parallel, that poly(ADP-ribosyl)ated chromatin showed increased solubility in the presence of Mg2+ and 0.2 M NaCl. Electron microscopic examination of the solubilized chromatin produced by poly(ADP-ribosyl)ation shows polynucleosomes exhibiting more relaxed conformation, whereas an increasing amount of hyper(ADP-ribosyl)ated histone H1 is found in the pellet, as shown by acid–urea–polyacrylamide electrophoretic separation of histone extracts.

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

Spectroscopic analysis of the interaction of valproic acid with histone H1 in solution and in chromatin structure

2017 ◽  
Vol 99 ◽  
pp. 427-432 ◽  
Author(s):  
Javad Sargolzaei ◽  
Azra Rabbani-Chadegani ◽  
Hossein Mollaei ◽  
Abdolkhalegh Deezagi
Keyword(s):  
Valproic Acid ◽  
Chromatin Structure ◽  
Spectroscopic Analysis ◽  
Histone H1
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