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Biomedical subjects

J Palau

Publications and source records attributed to J Palau.

At least 73 records · Page 4Linked to original sources
PubMed1977

The interaction of histone H3 with histone H4 and with other histones studied by 19F nuclear magnetic resonance.

The behaviour, upon variations in ionic strength, pH and temperature of 19F nuclear nuclear magnetic resonance signals of the trifluoroacetonylated derivative of histone H3 is compared with those of the H3-H4 complex and of the Hv fraction (an equimolar mixture of H2A, H2B, H3 and h4). The line width of the 19F-labelled histone H3 signals increases with ionic strength or pH, an effect consistent with aggregation of the protein. In the case of H3-H4 complex or Hv the line width decreases at intermediate ionic strengths (0.1-0.25 M NaCl). This effect is interpreted as the consequence of the formation of a well defined structure with ionic strength. At high salt concentrations the line width increases as a consequence of the final rigid quaternary structure or of the formation of higher aggregates.

Animals↗
PubMed1977

Interactions of histones and histone peptides with DNA Thermal denaturation and solubility studies.

The interactions of DNA with the five histone components (H1, H2B, H2A, H3 and H4) and with a number of histone fragments (N-H1 (1--72), C-H1 (73--216), N-H2B (l--59), C-H2B, (63--125), N-H2A (1-39), C-H2A (58--129), N-H4 (1--84) and C-H4 (85--102) have been studied by using the techniques of thermal denaturation and solubility behaviour. Complexes in 10(-3) M phosphate buffer, 2 - 10(-5) M Na(2)-EDTA, pH 7.0 were prepared by the direct mixing method. For lysine-rich histones (H1 and H2B) it has been found that the main characteristics which governs the interaction with DNA are located in the very lysine-rich part of the molecules, i.e. in the C-H1 and N-H2B segments. These regions are also responsible for a cooperative distribution of the histone along the DNA molecules in the artificial complexes. It appears from our studies that the tertiary structure of the moderately, arginine-rich histone (H2A) is an essential feature for its interaction with DNA. The two arginine-rich histones (H3 and H4) complexed with DNA behave in a similar way, both in thermal denaturation and in DNA precipitation. In the case of C-H4, a marked shift of the melting profile has been observed which is correlated with the presence in the peptide of the hydrophilic cluster Lys-Arg-Gln-Gly-Arg-Thr. Our results suggest that large segments rich in lysine and basic clustering within histones give rise to different modes of electrostatic interaction with DNA.

Animals↗
PubMed1976

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.

Proton magnetic resonance and other measurements have been carried out in order to study the behaviour of the lysine-rich histones phi 1 in the sperm chromatin of certain marine invertebrates. Well defined particles (12 S) have been obtained from this chromatin by nuclease treatment. Chromatin solubility as a function of ionic strength shows a relaxation at salt concentrations higher than in the case of calf thymus nucleoprotein. Nuclear magnetic resonance (NMR) studies show that the release of histone from DNA occurs both in chromatin and in the reconstituted complexes at practically the same ionic strength as solubility relaxation. The higher the arginine content of a given phi 1, the higher the ionic strength at which both effects take place. The NMR results demonstrate that arginine residues are bound more strongly than lysine residues. 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. The highly contracted state of sperm chromatin is directly related to the increased arginine content of the phi 1 histone.

Animals↗
PubMed1975

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.

Proton magnetic resonance, circular dichroism and infrared spectroscopy are used to investigate the secondary and tertiary structure of three very lysine-rich histones from marine invertebrate sperm. At high ionic strength both Arbacia lixula and Holothuria tubulosa histone phi 1 are observed to contain 25-30% alpha-helix, no beta-structure and to form specific folded structures. 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. Mytilus edulis histone phi 1 however, shows no spectroscopic evidence of secondary and tertiary structure on salt addition.

Amino Acids↗
PubMed1975

Behaviour of tyrosyl residues of calf-thymus histone F3. Difference-spectroscopy studies.

We have studied the behaviour of microenvironments containing tyrosine of calf thymus histone F3 (or histone H3) by using the difference spectroscopy techniques of thermal and solvent perturbation. By comparison of the parameters found for the models L-tyrosine methyl ester and N-acetyl-L-tyrosine ethyl ester with those for the protein at various conditions, several aspects of the tertiary structure of histone F3 become apparent. The raising of ionic strength produces a general burial of tyrosyl residues of the histone, whereas low pH or urea treatment causes a complete exposure of tyrosyl groups with respect to the solvent. Anomalously high values can also be observed of accessibility of the perturbants sucrose and ethylene glycol at low concentrations of phosphate buffer. The relevance of these findings towards a better understanding of the tertiary structure of histone F3 and of its interactions with DNA is discussed.

Animals↗
PubMed1975

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

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 structure formation outside the region 40--115. At 18 degrees C and a protein concentration of 2 mM the first-order exchange rate between random-coil and structured forms is slower than 80 s-1; at 40 degrees C the exchange rate is faster than 330 s-1.

Animals↗
PubMed1967

Countercurrent-distribution studies on histones.

1. The possibilities of fractionating histones and histone fractions by means of countercurrent distribution between two phases formed by water and butan-2-ol, in the presence of various concentrations of trichloroacetic acid, have been examined. 2. Although the principal histone fractions differ considerably in their partition ratios, a satisfactory resolution of the principal histone fractions from the whole histone has not been achieved. 3. The histone fractions obtained by other methods can be resolved with suitable concentrations of trichloroacetic acid. Besides the main peak several subsidiary peaks are obtained in most cases, the composition of which corresponds with others of the main fractions. 4. The method is therefore capable of removing from the principal fractions as previously prepared contamination by other fractions. 5. Except in one case, no fraction with composition unlike other fractions has been obtained. In several cases the material isolated from the principal peak behaves as a single component on running again. In two cases fractions with similar compositions were distinguished by countercurrent distribution.

Acids↗
PubMed1966

Trout-liver histones.

1. The histones of trout liver were examined and four main fractions (f1, f2b, f2a and f3) were isolated and characterized. 2. The amino acid analyses, N-terminal group analyses and starch-gel electrophoresis patterns are remarkably similar to the corresponding fractions of calf thymus. 3. The group f2a was also separated into two subfractions, f2al and f2a2, which are similar to those of calf thymus.

Amino Acids↗