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Biomedical subjects

A Klug

Publications and source records attributed to A Klug.

At least 91 records · Page 5Linked to original sources
PubMed1982

Stabilization of the tertiary structure of yeast phenylalanine tRNA by [Co(NH3)6]3+. X-ray evidence for hydrogen bonding to pairs of guanine bases in the major groove.

The sites of three [Co(NH3)6]3+ ions bound to the phenylalanine tRNA of yeast have been determined by X-ray diffraction analysis. [Co(NH3)6]3+ binds to purine-purine sequences in yeast tRNA Phe. It is different from the binding fo Co2+, which binds to the base and phosphate of residue G15. There are no direct metal-nucleotide bonds, although hydrogen bonding of the coordinated ammines to double-helical guanylguanosine sequences in the major groove and to phosphate oxygen in neighboring polynucleotide strands increases the stability of the structure. Hydrogen-bonding appears to be via cis ammine ligands to N(7) and O(6) positions of adjacent purine bases.

Amino Acyl-tRNA Synthetases↗
PubMed1981

The helical periodicity of DNA on the nucleosome.

The precise number of base pairs per turn of the DNA double helix in the nucleosome core particle has been the subject of controversy. In this paper the positions of nuclease cutting sites are analysed in three dimensions. Using this midpoint of the DNA on the nucleosome dyad as origin, the cutting site locations measured along a strand of DNA are mapped onto models of the nucleosome core containing DNA of different helical periodicities. It is found that a helical periodicity of 10.5 base pairs per turn leads to cutting site positions which are sterically inaccessible. In contrast, a periodicity of 10.0 base pairs per turn leads to cutting site positions which are not only sterically sound, but which fall into a pattern such as would be expected when the access of the nuclease to the DNA is restricted by the presence of the histone core on one side and of the adjacent superhelical turn of DNA on the other. As proposed earlier by us (1), a value for the helical periodicity close to 10 base pairs per turn on the nucleosome, taken together with a periodicity close to 10.5 for DNA in solution - a value now established - resolves the so-called linkage number paradox.

Chemical Phenomena↗
PubMed1981

The nucleosome.

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Animals↗
PubMed1980

A low resolution structure for the histone core of the nucleosome.

Image reconstruction to 22 A resolution of the histone octamer (H3)2(H4)2(H2A)2(H2B)2 shows it to have a 2-fold axis of symmetry, and the overall shape of the left-handed helical spool on which to wind about two turns of a flat superhelix of DNA in the nucleosome. From this structure and the results of various cross-linking studies, we have deduced the arrangement of the individual histones. We propose that the (H3)2(H4)2 tetramer forms a dislocated disk which defines the central turn of DNA, while the two H2A-H2B dimers lie one on each face, each associated with about one half a turn.

Animals↗
PubMed1980

Helical periodicity of DNA determined by enzyme digestion.

The periodicity of DNA has been determined by binding short, stiff pieces of DNA to a flat surface and using DNase I to probe the accessibility of the phosphodiester bonds. We have found that the distance between successive DNase I cutting sites is 10.6 +/- 0.1 bases for the DNA immobilized on three different surfaces. We identify this value with the number of base pairs per turn of the DNA double helix in solution.

Binding Sites↗
PubMed1979

Periodicity of deoxyribonuclease I digestion of chromatin.

Two methods have been used to measure the single-strand lengths of the DNA fragments produced by deoxyribonuclease I digestion of chromatin. The average lengths obtained are muliples of about 10.4 bases, significantly different from the value of 10 previously reported. This periodicity in fragment lengths is closely related to the periodicity of the DNA double helix in chromatin, but the two values need not be exactly the same.

Animals↗
PubMed1979

Involvement of histone H1 in the organization of the nucleosome and of the salt-dependent superstructures of chromatin.

We describe the results of a systematic study, using electron microscopy, of the effects of ionic strength on the morphology of chromatin and of H1-depleted chromatin. With increasing ionic strength, chromatin folds up progressively from a filament of nucleosomes at approximately 1 mM monovalent salt through some intermediate higher-order helical structures (Thoma, F., and T. Koller, 1977, Cell 12:101-107) with a fairly constant pitch but increasing numbers of nucleosomes per turn, until finally at 60 mM (or else in approximately 0.3 mM Mg++) a thick fiber of 250 A diameter is formed, corresponding to a structurally well-organized but not perfectly regular superhelix or solenoid of pitch approximately 110 A as described by Finch and Klug (1976, Proc. Natl. Acad. Sci. U.S.A. 73:1897-1901). The numbers of nucleosomes per turn of the helical structures agree well with those which can be calculated from the light-scattering data of Campbell et al. (1978, Nucleic Acids Res. 5:1571-1580). H1-depleted chromatin also condenses with increasing ionic strength but not so densely as chromatin and not into a definite structure with a well-defined fiber direction. At very low ionic strengths, nucleosomes are present in chromatin but not in H1-depleted chromatin which has the form of an unravelled filament. At somewhat higher ionic strengths (greater than 5 mM triethanolamine chloride), nucleosomes are visible in both types of specimen but the fine details are different. In chromatin containing H1, the DNA enters and leaves the nucleosome on the same side but in chromatin depleted of H1 the entrance and exit points are much more random and more or less on opposite sides of the nucleosome. We conclude that H1 stabilizes the nucleosome and is located in the region of the exit and entry points of the DNA. This result is correlated with biochemical and x-ray crystallographic results on the internal structure of the nucleosome core to give a picture of a nucleosome in which H1 is bound to the unique region on a complete two-turn, 166 base pair particle (Fig. 15). In the formation of higher-order structures, these regions on neighboring nucleosomes come closer together so that an H1 polymer may be formed in the center of the superhelical structures.

Chromatin↗