Investigation of the conformational and self-aggregational processes of histones using hydrogen and carbon-13 nuclear magnetic resonance

Lilley, David M.J.; Howarth, Oliver W.; Clark, V. M.; Pardon, J. F.; Richards, B. M.

doi:10.1021/bi00692a006

Cited by 25 publications

(10 citation statements)

References 22 publications

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“…The spectra are simitar and most differences may be accounted for in terms of the signal-to-noise ratio. Furthermore, the general appearance of the spectra, with narrow resonances superimposed on a broad background, is very similar to that of previously recorded 13C N MR spectra from histones (Clark et al, 1974;Lilley et al, 1975Lilley et al, , 1976Lilley, 1977;Tancredi et al" 1976) showing that the general nature of histone structure is independent of the method used for their extraction. Histone !3C NMR line widths have been analyzed in some detail elsewhere (Lilley, 1977).…”

Section: Resultssupporting

confidence: 84%

Structural investigations of chromatin core protein by nuclear magnetic resonance

Lilley¹,

Pardon²,

Richards³

1977

Biochemistry

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A complex derived from chromatin containing one molecule of each of histones H2A, H2B, H3, and H4, termed core protein, was studied by 13C and 1H nuclear magnetic resonance. 13C line widths, when analyzed and compared with those of native and thermally unfolded representative globular proteins, showed that regions of the core protein possess considerable mobility. Studies of Calpha and Cbeta line widths, and Calpha spin-spin relaxation times, show that this mobility arises from sections of random-coil polypeptide. It is argued that these regions are N-terminal "tails", attached to C-terminal globular polypeptides. The 270-MHz 1H nuclear magnetic resonance spectrum shows numerous ring current shifted resonances, indicating that the C-terminal globular domain has a precise tertiary structure. The globular domain most likely forms the histone "core" of the chromatin monomer particle, whilst the basic tails probably wind around the grooves of the double helix, enabling the basic side chains to interact with the DNA phosphate groups. Some biological implications of this model are considered.

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Section: Resultssupporting

confidence: 84%

Structural investigations of chromatin core protein by nuclear magnetic resonance

Lilley¹,

Pardon²,

Richards³

1977

Biochemistry

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“…It is believed that most of the secondary structure of the histones is located in the more hydrophobic domains35,36 which are also the parts which interact with each other. 37 We therefore conclude that the CD transition at 223 nm actually monitors the destruction of the histone core at about 700C. Coupled with it is a relaxation of conformation constraints on the DNA.…”

Section: Discussionmentioning

confidence: 70%

Thermal denaturation of nucleosomal core particles

Weischet¹,

Tatchell²,

Holde³

et al. 1978

Nucl Acids Res

171

125

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Thermal denaturation of very homogeneous preparations of core particles from chicken erythrocyte chromatin is studied by several techniques. The change in absorbance, which is very closely paralleled by changes in heat capacity, is a biphasic process with inflexions at 600C and 740C. In contrast, isolated DNA of the same length denatures in a single transition around 440C. Monitoring the circular dichroism of the cores during thermal denaturation reveals biphasic changes in the secondary structure of the DNA, preceding the base unstacking by 100C in the first and 30C in the second phase. However, measurable alterations in the secondary structure of the histones are confined to the second phase with a melting temperature at 710C. Increase in the ionic strength of the buffer from 1 mM to 10 mM leads to almost monophasic melting curves as measured by absorbance and CD, while not causing any measurable conformational changes at room temperature. The melting of core particles is interpreted as a denaturation of about 40 base pairs in the first phase, followed by a massive breakdown of the native structure of a tight histone-DNA complex, which frees the remaining 100 base pairs for unstacking.

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“…It should be noted, however, that these DNA binding studies were carried out in the absence of a full complement of histones. More recent work supports the concept of a H2B structural core formed by residues 55-78 (Lilley et al, 1975;Tancredi et al, 1976). A similar study using proton magnetic resonance and circular dichroism to analyze the H2A-H2B complex indicates that residues 37-114 of H2B are involved in the stable tertiary structure that is formed (Moss et al, 1976).…”

Section: Hn-p-e-p-a-k-s-a-p---amentioning

confidence: 63%

Sequence of histone 2B of Drosophila melanogaster

Elgin¹,

Schilling²,

Hood³

1979

Biochemistry

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The complete sequence of histone 2B of Drosophila has been determined by using an improved Beckman sequenator. Comparing these data with those previously published by other investigators on the histone 2B of calf [Iwai, K., Hayashi, H., & Ishikawa, K. (1972) J. Biochem. (Tokyo) 72, 357--367], trout [Koostra, A., & Bailey, G. S. (1978) Biochemistry 17, 2504--2510], and Patella (a limpet) [van Helden, P. D., Strickland, W. N., Brandt, W. F., & von Holt, C. (1979) Eur. J. Biochem. 93, 71--78], it is possible to assess the evolutionary stability of this protein. There is little conservation of sequence in the N-terminal portion of the molecule (residues 1--26 numbering according to calf H2B), while the remainder of the protein, which we designate the C-terminal portion, is highly conserved. In the region of 27--125 residues, there are 9 substitutions in the composite data among the 98 positions, 8 of them conservative. These data indicate that very different selective pressures operate on the two different portions of the H2B molecule, implying the existence of two well-defined regions. Studies on the structure of the nucleosome by others have suggested that the C-terminal portion of H2B is involved in histone-histone interactions while the N-terminal portion is a relatively free "tail" binding to DNA. The sequence data indicate that the function of the C-terminal region of H2B requires considerable sequence specificity while that of the N-terminal region does not.

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Investigation of the conformational and self-aggregational processes of histones using hydrogen and carbon-13 nuclear magnetic resonance

Cited by 25 publications

References 22 publications

Structural investigations of chromatin core protein by nuclear magnetic resonance

Structural investigations of chromatin core protein by nuclear magnetic resonance

Thermal denaturation of nucleosomal core particles

Sequence of histone 2B of Drosophila melanogaster

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