Chromatin structure as probed by nucleases and proteases: Evidence for the central role of hitones H3 and H4 |
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Authors: | Barbara Sollner-Webb Rafael D Camerini-Otero Gary Felsenfeld |
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Institution: | Laboratory of Molecular Biology National Institute of Arthritis, Metabolism and Digestive Disease National Institutes of Health Bethesda, Maryland 20014 USA |
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Abstract: | We have examined the role played by each histone in forming the structure of the ν-body. When DNAase I, DNAase II, trypsin, and chymotrypsin attack chromatin, characteristic discrete DNA and protein digest fragments are produced. Using this restriction of accessibility as diagnostic for chromatin structure, we have examined complexes of DNA with virtually all possible combinations of histones. The results strongly support our previous conclusion (Camerini-Otero, Sollner-Webb, and Felsenfeld, 1976) that the arginine-rich histones are unique in their ability to create, with DNA, a structure with many features of native chromatin. Acting together, slightly lysine-rich histones then modify this complex into one very similar to native chromatin. An analysis of the rate constants of staphylococcal nuclease digestion also confirms that the complex of H3, H4, and DNA is crucial to the structure of the ν-body. |
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