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  • Title: Role of the protein alpha helixes in histone-DNA interactions studied by vibrational spectroscopy.
    Author: Taillandier E, Fort L, Liquier J, Couppez M, Sautiere P.
    Journal: Biochemistry; 1984 Jun 05; 23(12):2644-50. PubMed ID: 6466603.
    Abstract:
    The localization of structurally important histone-DNA interactions has been investigated by vibrational spectroscopy. Histones H2A, H2B, and H4 and their fragments (H2A, 1-56, 1-89, 73-129; H2B, 1-59, 1-83; H4, 1-53, 1-67, 1-84, 69-84, 85-102) have been prepared, characterized, and used to reconstitute protein-DNA complexes. Evidence is given for the existence of a direct relationship between the presence of ordered alpha-helical structures in the histones and a stabilization of the DNA in a B geometry. Infrared linear and ultraviolet dichroism measurements indicate that the N-terminal fragments, rich in basic residues and mostly in a random conformation, remain without any influence on the secondary structure of the nucleic acid, leaving it free in the complexes to undergo a total B----A conformational transition. On the contrary, histone fragments that involve some alpha-helical parts of the protein partially stabilize the DNA in a B geometry. Histone fragments that contain all of the alpha helixes of the protein block the DNA in the same way as the whole corresponding histone. A model for histone-DNA interactions in the core particle is discussed.
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