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Abstract
Synthesis and enzymatic modification of histone V was 1 order of magnitude lower in mature gander erythrocytes as compared with immature enriched cells hwich were capable of DNA synthesis. Application of shallow, linear gradient chromatography was used to demonstrate qualitative changes as well. This technique permitted the separation of newly synthesized and phosphorylated histone V from older, less phosphorylated molecules but did not discriminate between acetylated species. The most easily eluted fractions were those most recently synthesized, acetylated, and phosphorylated. While lysine chased into the other subfractions of histone V, phosphate did not, indicating a dephosphorylation step in the immature cells. Acetylation of histone V which occurs at a very low level was closely related to its synthesis. No differences in molecular weights or amino acid compositions were apparent, and behavior on polyacrylamide gels was similar to whole histone V. It is proposed that phosphorylation of histone V may play an important role in the modulation of the effect of histone V in immature cells on condensation and template restriction of chromatin which occurs in the terminal stages of differentiation of the avian erythroid cells.
Highlights
In an attempt to better understand the significance of these modifications in histone V we examined the relationship between phosphorylation, acetylation, and synthesis of histone V from goose erythrocytes
The results of this study reported here suggest that much of the phosphorylation and most the acetylation of histone V can be accounted for by de novo synthesis and that newly synthesized, phosphorylated histone V can be partially purified by chromatography
Acetate uptake into the whole histone fraction was highest in the immature enriched cells
Summary
Synthesis and enzymatic modification of histone V was 1 order of magnitude lower in mature gander erythrocytes as compared with immature enriched cells which were capable of DNA synthesis. One possibility [2, 17,18,19] for which there is some evidence is that enzymatic modifications of histone V could mediate binding alterations to DNA or other proteins (or both) by reduction of key basic charges either by the addition of phosphoryl groups to serine residues or possibly addit.ion of acetyl residues, primarily to the e-amino of lysines These considerations are largely based upon an analogy drawn from the studies of Louie et al [20] on the binding of histones and protamine to chromatin-DNA in trout spermatids. Because of the differences in turnover of phosphate, acetate, and synthesis, more important than this molecule
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