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5. Observed biochemical modifications of histone H4 residues. , 1969). , 1975). polypeptide chain has also been established (Sung and Dixon, 1970; Candido and Dixon, 1971; Dixon et al, 1975; Thwaits et al, 1976b) (Fig. 5). B. HISTONE ACETYLATION AND DNA CONFORMATION It should be noted that the distribution of e-N-acetyllysine in histones is not random; all the modifiable lysine residues in H4 occur in the aminoterminal portion of the polypeptide chain, which by virtue of its clustering of the basic amino acids—arginine, lysine, and histidine—carries a high net positive charge.
1975). Once incorporated into the nucleosome, histone H4—together with the other histones of the nucleosome "core"—becomes subject to a controlled series of acetylation and deacetylation reactions. The structural basis of many of these reactions will now be considered. 3. , 1973; DeLange and Smith, 1975; Dixon et al, 1975). , 1973; Berkovic and Mauritzen, 1977), but acetylation in vivo is coordinate with HI synthesis (Ruiz-Carrilloet al, 1976) and results in the formation of iV-acetylserine at the amino terminus (Fig.
1976). , 1977) and certain higher eukaryotes (Thomas and Thompson, 1977). In Physarum, repeat lengths varying from 190 to 173 base pairs could be detected upon treatment of nuclei with staphylococcal nuclease for different lengths of time. , 1977). Despite significant evolutionary variability in sequences of certain his tones, little variability has been detected in DNA lengths of nucleosome monomers containing these histones. A minimum monomer DNA length of 140 base pairs may be characteristic of most, if not all, chromatin.