Abstract
THE structural functions of four of the five histones are now partially understood1 and the nucleosome structure of chromatin well established2–4. However, superimposed on this basic nucleosome structure is some heterogeneity with respect to the other chromosomal proteins, since although it has been shown that isolated nucleosomes contain non-histone chromosomal proteins5,6, there are insufficient of some classes for one per nucleosome. These nucleosomal non-histone chromosomal proteins have been designated the high-mobility group (HMG) proteins. They have been fractionated, and the main components, HMG 1, HMG 2, HMG 14 and HMG 17 have been isolated in a pure form7–9. The complete amino acid sequence of one of these proteins, HMG 17, has been determined10. We report here that the C-terminal region of protein HMG 1 contains an extremely unusual sequence of amino acids—41 aspartic and glutamic acid residues.
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WALKER, J., HASTINGS, J. & JOHNS, E. A novel continuous sequence of 41 aspartic and glutamic residues in a non-histone chromosomal protein. Nature 271, 281–282 (1978). https://doi.org/10.1038/271281a0
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DOI: https://doi.org/10.1038/271281a0
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