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  • Title: Synthesis, acetylation, and phosphorylation of histone IV and its binding to DNA during spermatogenesis in trout.
    Author: Louie AJ, Dixon GH.
    Journal: Proc Natl Acad Sci U S A; 1972 Jul; 69(7):1975-9. PubMed ID: 4505675.
    Abstract:
    During spermatogenesis in trout testis, histone IV is extensively modified by acetylation and phosphorylation. To examine the relationship of synthesis of histone IV to its modification, histone IV labeled with [(3)H]aminoacids and inorganic [(32)P]phosphate was prepared from testis cells by acid extraction and column chromatography. Purified histone IV was resolved by starch gel electrophoresis into 10 bands, of which nine are modified by acetylation and/or phosphorylation. In the first 4 hr of labeling, the diacetyl-histone IV band showed the highest proportion of [(3)H]aminoacid label. After 12 hr of incorporation, more label was found in the triacetyl and tetraacetyl bands. A significant amount of amino-acid label in the two major bands (the unsubstituted and monoacetyl bands) of histone IV was not seen until 16 hr of incubation. From 1 to 12 days, the proportion of label in the unsubstituted and monoacetylated bands increased, while that in the tetra-, tri-, and monoacetyl bands decreased. Very little [(3)H]aminoacid was found in the phosphorylated bands of histone IV in the first 12 hr. However, after 16 hr about 20% of the total (3)H was found in the phosphorylated bands. The proportion increased to 33% and remained at this level between 1 and 8 days, but, by 16 days, had decreased to 12% of the total. These data suggest that an "obligatory" acetylation of recently synthesized histone IV is involved in the correct binding of newly synthesized histone IV to DNA. We propose that epsilon-amino acetylation of lysyl residues 5, 8, 12, and 16 neutralizes their positive charges and allows the NH(2)-terminal region of histone IV to assume the correct conformation (in this case, an alpha-helix), and fit into the major groove of DNA. Deacetylation then "locks" histone IV to DNA by ionic linkages. The biological significance of phosphorylation of histone IV is not known.
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