Self-association of Chaetopterus variopedatus sperm histone H1-like. Relevance of arginine content and possible physiological role.

2008 ◽  
Vol 55 (4) ◽  
pp. 701-706 ◽  
Author(s):  
Daniela Salvati ◽  
Salvatore Conforti ◽  
Mariachiara Conte ◽  
Danilo Swann Matassa ◽  
Laura Fucci ◽  
...  
Keyword(s):  
Physiological Role ◽  
Histone H1 ◽  
Native Page ◽  
High Tendency ◽  
Phosphate Ions ◽  
R Ratio ◽  
Chaetopterus Variopedatus ◽  
Calf Thymus ◽  
Similar Content ◽  
Self Association

Self-association of histones H1 from calf thymus and from sperm of the marine worm Chaetopterus variopedatus was studied on native and glutaraldehyde cross-linked molecules by PAGE and by salt-induced turbidity measurements. Multiple polymers were generated by native sperm histone H1-like after glutaraldehyde cross-linking while the same treatment on its lysine- or arginine-modified derivatives and on somatic histone H1 failed to induce polymerization. This result suggests the relevance of arginine content in the formation of histone H1-like polymers particularly because Chaetopterus variopedatus and calf thymus histones H1 have similar content of lysine but different K/R ratio (2 and 15, respectively). Salt-induced turbidity experiments confirmed the high tendency of sperm histone H1-like to form oligomers, particularly in the presence of phosphate ions. Native PAGE analysis in the presence of phosphate supported this hypothesis. The reported results suggest that phosphate ions connecting lysine and arginine side chain groups contribute to the interaction of sperm histone H1-like with DNA in chromatin and play a key role in organization and stabilization of the chromatin higher order structures.

scholarly journals The binding of adenosine(5′)tetraphospho(5′)adenosine to calf thymus histones measured by non-equilibrium dialysis

1987 ◽  
Vol 246 (3) ◽  
pp. 681-686 ◽  
Author(s):  
G Just ◽  
E Holler
Keyword(s):  
Ionic Strength ◽  
Dissociation Constants ◽  
Equilibrium Dialysis ◽  
Physiological Saline ◽  
Histone H1 ◽  
The Other ◽  
Competition Assay ◽  
Calf Thymus ◽  
Non Equilibrium

Binding of adenosine(5′)tetraphospho(5′)adenosine (Ap4A) to histones of calf thymus was investigated by non-equilibrium dialysis. Histone H1 interacts with the dinucleotide via two strong sites and competes with Mg2+ ions. Intrinsic dissociation constants were 1.6 +/- 0.1 microM and 11 +/- 1 microM for zero and 0.4 mm-Mg2+ concentration respectively. Binding of poly(dT) and of other nucleotides to histone H1 was measured in an [3H]Ap4A-competition assay. The tendency to form complexes among nucleotides was highest for bisnucleoside tetraphosphates and decreased in the order poly(dT) greater than or equal to Ap4A approximately Gp4G greater than Ap4 much greater than Ap3A approximately Ap5A greater than or equal to ATP, GTP and dTTP. The co-ordination complex derived from Ap4A and cis-diammine-dichloroplatinum(II) was not reactive. The other histones of calf thymus also bound Ap4A with affinities decreasing in the order H4 approximately H3 greater than H1 greater than H2b greater than H2a. Ap4A stimulated the exchange of histone H1 between nucleosomes, but this effect was referred to ionic strength. It did not bind to assembled nucleosomes. Binding of Ap4A to histone H1 was decreased by salt (NaCl). At physiological saline concentration the value of the dissociation constant is commensurable with the value of the Ap4A concentration in the nucleus and thus indicative of complex-formation in vivo.

The selective extraction of histones from rye chromatin

1976 ◽  
Vol 54 (9) ◽  
pp. 765-771 ◽  
Author(s):  
Hélène LaRue ◽  
Dominick Pallotta
Keyword(s):  
Selective Extraction ◽  
Histone H1 ◽  
The Other ◽  
Calf Thymus

The selective extraction of histones from rye chromatin was studied using three different methods. Extractions with NaCl–phosphate buffers atpH 5.5 gave results similar to those already obtained with other types of chromatin. Histone H1 was selectively extracted with 0.6 M NaCl –0.001 M PO4, while the selectivity of dissociation of the other fractions was reduced at higher NaCl concentrations. The use of phosphate–urea buffers at pH 5.5 also revealed that the histones were dissociated at the same concentrations as were calf thymus histones. Histone H1 was extracted with 0.5 M PO4 – 1 M urea; H1, H2A, and H2B were extracted with 0.8 M PO4 – 2 M urea; and all histones were removed with 0.8 M PO4 –5.3 M urea. It was, however, observed that the dissociated rye histones H2A and H2B were unstable in these buffers. This instability was maximum in the presence of 3 M urea, where both histones were absent from the extracted proteins and the residual nucleoproteins. Finally, a solution of 30% ethanol −0.35 M NaCl – 6 M urea produced a rye nucleoprotein fraction containing only histone H1.

Kinetics of chemical modification of arginine and lysine residues in calf thymus histone H1

Biopolymers ◽  
1981 ◽  
Vol 20 (6) ◽  
pp. 1103-1112 ◽  
Author(s):  
Kazuei Mita ◽  
Sachiko Ichimura ◽  
Mitsuo Zama ◽  
Koei Hamana
Keyword(s):  
Chemical Modification ◽  
Histone H1 ◽  
Calf Thymus ◽  
Lysine Residues ◽  
Kinetics Of

scholarly journals Preparation and characterization of histone H1 from the sperm of the sea-urchin Sphaerechinus granularis

1981 ◽  
Vol 195 (1) ◽  
pp. 171-176 ◽  
Author(s):  
V Giancotti ◽  
S Cosimi ◽  
P D Cary ◽  
C Crane-Robinson ◽  
G Geraci
Keyword(s):  
Secondary Structure ◽  
Sea Urchin ◽  
Fluorescence Spectra ◽  
Tertiary Structure ◽  
Histone H1 ◽  
Separation And Purification ◽  
Tertiary Structures ◽  
Calf Thymus ◽  
Sea Urchin Sperm

The separation and purification of histone H1 from the sperm of the sea-urchin Sphaerechinus granularis is described. Physical studies were used to compare this histone H1 molecule with H1 histones from other species. C.d. and 270 MHz n.m.r. spectroscopy indicate that, despite significant compositional differences from other sea-urchin sperm H1 histones, their secondary and tertiary structures are very similar. A large difference in helicity was, however, found between S. granularis histone H1 and calf thymus histone H1, and their n.m.r. and fluorescence spectra also differ considerably. It is concluded that secondary structure and tertiary structure have not been conserved in the evolution of the H1 histone family.

Changes in binding affinity between ofloxacin and calf thymus DNA in the presence of histone H1: Spectroscopic and molecular modeling investigations

2018 ◽  
Vol 203 ◽  
pp. 599-608 ◽  
Author(s):  
Farzad Dehghani Sani ◽  
Niloufar Shakibapour ◽  
Sima Beigoli ◽  
Hamid Sadeghian ◽  
Maral Hosainzadeh ◽  
...  
Keyword(s):  
Molecular Modeling ◽  
Binding Affinity ◽  
Histone H1 ◽  
Calf Thymus Dna ◽  
Calf Thymus

Probing the binding of lomefloxacin to a calf thymus DNA-histone H1 complex by multi-spectroscopic and molecular modeling techniques

2018 ◽  
Vol 256 ◽  
pp. 127-138 ◽  
Author(s):  
Tahmineh Sohrabi ◽  
Maral Hosseinzadeh ◽  
Sima Beigoli ◽  
Mohammad Reza Saberi ◽  
Jamshidkhan Chamani
Keyword(s):  
Molecular Modeling ◽  
Histone H1 ◽  
Calf Thymus Dna ◽  
Calf Thymus ◽  
Modeling Techniques

Histone H1 and chromatin higher order structure does histone H1 exhibit specific self-association?

1983 ◽  
Vol 15 (4) ◽  
pp. 487-493 ◽  
Author(s):  
E. Russo ◽  
V. Giancotti ◽  
C. Crane-Robinson ◽  
G. Geraci
Keyword(s):  
Histone H1 ◽  
Higher Order ◽  
Order Structure ◽  
Self Association

Exogenous histone H1 injection into mitotic cells disrupts synchronous progression of mitotic events by delaying chromosome decondensation

1994 ◽  
Vol 107 (3) ◽  
pp. 693-701 ◽  
Author(s):  
Y. Matsuoka ◽  
S. Takechi ◽  
T. Nakayama ◽  
Y. Yoneda
Keyword(s):  
Mitotic Spindle ◽  
Protein Transport ◽  
Type A ◽  
Histone H1 ◽  
Type B ◽  
Lamin B ◽  
Calf Thymus ◽  
Exogenous Histone ◽  
Chromosome Decondensation

At the end of open mitosis, chromosome decondensation, nuclear envelope re-formation and reassembly of interphase microtubules following mitotic spindle dissociation occur coordinately. To determine whether these events progress only synchronously in vivo, we delayed chromosome decondensation by injecting of exogenous proteins into the mitotic rat kangaroo kidney epithelium (PtK2) cells. When histone H1 purified from calf thymus was injected at prometaphase, chromosome condensation was prolonged for several hours, and sister chromatid separation and cytokinesis did not occur. However, interphase microtubules reassembled and lamin B-positive structures re-formed around the condensed chromosomes. Exactly the same results were obtained on injection of bacterially expressed H1. Kinetic experiments showed that there were two types of lamin B-positive structures. One type (type A) was stained uniformly with anti-lamin B antibodies. The other (type B) showed peripheral lamin B staining; that is, the normal interphase staining pattern, and was found to be competent for nuclear protein transport. As the chromosomes decondensed, the amount of type A decreased and that of type B increased. However, even cells containing highly condensed chromosomes had both type A and type B. From these results, we conclude that the re-formation of microtubules and reassembly of a nuclear transport-competent envelope do not depend on chromosome decondensation.

Sign in / Sign up

Export Citation Format

Share Document