Proteolytic processing of h1-like histones in chromatin: a physiologically and developmentally regulated event in Tetrahymena micronuclei.
Micronuclei isolated from growing cells of Tetrahymena thermophila contain three H1-like polypeptides alpha, beta, and gamma. Micronuclei isolated from young conjugating cells (3-7 h) also contain a larger molecular weight polypeptide, X, which is being actively synthesized and deposited into these nuclei (Allis, C. D., and J. C. Wiggins, 1984, Dev. Biol., 101:282-294). Pulse-chase experiments (with growing and conjugating cells) suggested that X is a precursor to alpha and that alpha is further processed to gamma and a previously undescribed and relatively minor species, delta. These precursor-product relationships were supported by cross-reactivity with polyclonal antibodies raised against alpha and peptide mapping. While beta consistently became labeled under chase conditions (both in growing and mating cells), it was not clear whether it is part of the vivo processing event(s) which interrelates X, alpha, gamma, and delta. Beta was not recognized by alpha antibodies. Despite this uncertainty, these results suggest that proteolytic processing serves to generate significant changes in the complement of H1-like histones present in this nucleus.
D000818:Animals; D000918:Antibody Specificity; D002843:Chromatin / Q000378:metabolism*; D000939:Epitopes / Q000276:immunology; D006657:Histones / Q000276:immunology / Q000378:metabolism*; D007106:Immune Sera / Q000276:immunology; D008239:Lysine / Q000378:metabolism; D010446:Peptide Fragments / Q000276:immunology; D010447:Peptide Hydrolases; D011498:Protein Precursors / Q000378:metabolism*; D011499:Protein Processing, Post-Translational; D013768:Tetrahymena / Q000235:genetics / Q000254:growth & development / Q000378:metabolism*
D002843:Chromatin; D000939:Epitopes; D006657:Histones; D007106:Immune Sera; D010446:Peptide Fragments; D011498:Protein Precursors; D010447:Peptide Hydrolases; D008239:Lysine