Studies on the role and mode of operation of the very-lysine-rich histone H1 (F1) in eukaryote chromatin. The conformation of histone H1.

@article{Bradbury1975StudiesOT,
  title={Studies on the role and mode of operation of the very-lysine-rich histone H1 (F1) in eukaryote chromatin. The conformation of histone H1.},
  author={E. Bradbury and P. Cary and G. E. Chapman and C. Crane-Robinson and S. Danby and H. Rattle and M. Boublik and J. Palau and F. J. Aviles},
  journal={European journal of biochemistry},
  year={1975},
  volume={52 3},
  pages={
          605-13
        }
}
Proton magnetic resonance, circular dichroism and other studies of whole and cleaved calf thymus histone H1 (formerly F1) reveal the presence of specific folded structures in the region approximately from residue 40--115. Ionic, hydrogen-bond and hydrophobic interactions all appear to contribute to the stability of the structure, which is predicted to contain alpha-helices in regions 42--55 and 58--75. No evidence was found for beta-structures, either inter or intramolecular, or for any… Expand
Studies on the role and mode of operation of the very-lysine-rich histone H1 in eukaryote chromatin. The three structural regions of the histone H1 molecule.
TLDR
Proton nuclear magnetic resonance (NMR) and ultracentrifugation studies show that the H1 histone molecule consists of three distinct structural domains under structuring conditions: a random coil 'nose' consisting of 35 to 40 residues from the N-terminal end; a globular 'head' involving the next approximately 80 residues; and a random-coil 'tail' of the remainder of the molecule. Expand
Studies on the role and mode of operation of the very-lysine-rich histones in eukaryote chromatin. Effect of A and B site phosphorylation on the conformation and interaction of histone H1.
TLDR
Phosphorylation at serine-105, which is located in the globular region of H1, was found to reduce the enthalpy of structure formation and the strength of binding of the histone to DNA considerably at some ionic strengths. Expand
Studies on the role and mode of operation of the very-lysine-rich histone H1 (F1) in eukaryote chromatin. The properties of the N-terminal and C-terminal halves of histone H1.
TLDR
Restricted chymotrypsin digestion of calf thymus H1 histone gives two fragments, residues 1--106 and 107--C-terminal, which were studied by proton magnetic resonance and circular dichroism and suggested that there may be a connection between these phenomena. Expand
Studies on the role and mode of operation of the very-lysine-rich histone H1 in eukaryote chromatin. The isolation of the globular and non-globular regions of the histone H1 molecule.
TLDR
It seems that the structure of the H1 histone in solution under physiological conditions consists of a globular head with a highly basic random coil tail. Expand
Studies on the role and mode of operation of the very-lysine-rich histones in eukaryote chromatin. The conformation of phi1 histones from marine invertebrate sperm.
TLDR
Both phi 1 proton magnetic resonance spectra have perturbed methyl resonances at chemical shifts close to those observed for calf thymus H1, suggesting analogies in tertiary structure. Expand
Studies on the role and mode of operation of the very-lysine-rich histones in eukaryote chromatin. Nuclear-magnetic-resonance studies on nucleoprotein and histone phi 1-DNA complexes from marine invertebrate sperm.
TLDR
The data overall show that phi 1 histones play a role in the contraction mechanism of sperm chromatin similar to that of H 1 histone in calf thymus chromatin. Expand
The central tryptic fragment of histones H1 and H5 is a fully compacted domain and is the only folded region in the polypeptide chain. A thermodynamic study.
TLDR
Calorimetric measurements on a central tryptic fragment from histones H1 and H5 show these fragments to have the same molar melting enthalpy as the parent histones, and the folded structures of H1and H5 are therefore located only within these fragments. Expand
Distinction and similarity in the structure of histones H1 and H5 as indicated by 13C nuclear-magnetic-resonance spectroscopy.
TLDR
No evidence for a specific interaction between acidic and basic residues has been found and it has been shown that the pH-effects of aliphatic and aromatic resonances are quite different between H1 and H5, suggesting that the globular domain of H5 is more stable than that of H1. Expand
Involvement of the histidine residues in the pH-induced conformational change of histone H5.
TLDR
It is concluded that His-25 and His-62, which are buried in the globular domain, play an important role in the conformational stability of histone H5. Expand
Physical studies by NMR and circular dichroism determining three structurally different domains in Physarum polycephalum histone H1.
TLDR
It is suggested that titration of the histidine residues is the most decisive step for the development of tertiary folding of the globular unit. Expand
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References

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Magnetic Resonance Studies of Deoxyribonucleoprotein
TLDR
Of the five major types of histone fraction normally associated with mammalian genetic material, the lysine-rich histone F1 (or histone I) has some properties which set it apart from the others, and a proposed scheme for this interaction, involving an antiparallel alignment of chain segments has been presented. Expand
Spectroscopic studies of the conformations of histones and protamine
Abstract Earlier optical rotatory dispersion studies on calf thymus histone fractions showed that increasing the salt molarity of aqueous solution caused an increase in the optical rotatoryExpand
Simple computer-aided approach for the analyses of the nuclear-magnetic-resonance spectra of histones. Fractions F1, Fsa1, F2B, cleaved halves of F2B and F2B-DNA.
TLDR
A simple method for the computer simulation of high-resolution nuclear magnetic resonance spectra is described and applied to the analyses of salt-induced changes in the spectra of histones, which allows the information contained in the spectral envelope to be used and has led to some modifications of the earlier proposals of the segments of histone involved in salt- induced conformational changes, interhistone interactions and interactions with DNA. Expand
Regions of high and low cationic charge in a lysine-rich histone.
TLDR
The results indicate that most of the lysine and proline residues are closely packed in the carboxyl-terminal half of the molecule, whereas the amino acid composition of the amino- terminal half is not unlike small enzymes such as ribonuclease and lysozyme. Expand
Conformational Investigations of Histones
WE have carried out some investigations into the conformations of whole histones and histone fractions under various conditions. The experiments on repression of DNA-dependent RNA synthesis withExpand
Conservative amino-acid replacement in the tyrosine region of the lysine-rich histones.
  • M. Bustin
  • Biology, Medicine
  • European journal of biochemistry
  • 1972
TLDR
The results indicate that the sequence of amino acids around the single tyrosine present in the lysine-rich molecule is constant from tissue to tissue, however, this sequence varies among the molecular species comprising the lynium-rich histone complement of a single tissue. Expand
Sedimentation equilibrium and other physicochemical studies on the lysine-rich fraction of calf thymus histones.
TLDR
Sedimentation-velocity measurements combined with the known molecular weight imply that lysine-rich histone has a high frictional ratio and an extended shape, which explains anomalies in reports of the molecular weight of this histone. Expand
Bisection of a lysine-rich histone by N-bromosuccinimide.
TLDR
Preliminary data suggest that the amino-terminal portion of these molecules is the location of most of the differences in primary structure from one subfraction to another. Expand
Phosphorylation of very-lysine-rich histone in Physarum polycephalum. Correlation with chromosome condensation.
TLDR
A dramatic increase in phosphate content of this histone occurred in late G2 phase with a peak where chromosome condensation is seen to be occurring in the phase contrast microscope, suggesting phosphate content is low during S phase and the peaks of RNA synthesis. Expand
Effect of electrostatic interactions on the prediction of helices in proteins: The histones
Abstract A helix prediction method, previously successfully applied to globular proteins, is modified to include the effect of electrostatic attractions and repulsions from neighbouring side chains.Expand
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