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Histones H1/sup 0/a and H1/sup 0/b are the same as CHO histones H1(III) and H1(IV):new features of H1/sup 0/ phosphorylation during the cell cycle

Journal Article · · Biochemistry; (United States)
OSTI ID:5245797
Two histone H1 fractions (H1(I) and H1(II) and two histone H1/sup 0/ fractions (H1/sup 0/a and H1/sup 0/b) have been isolated from butyrate-treated Chinese hamster (line CHO) cells by guanidine hydrochloride gradient chromatography on Bio-Rex 70 ion-exchange resin. The fractions have been identified by electrophoresis and amino acid analyses. Electrophoretic analysis of cyanogen bromide treated H1/sup 0/ in long acid-urea-polyacrylamide gels suggests that H1/sup 0/a and H1/sup 0/b differ, at least, within the 20-30 residue fragment(s) removed by the cyanogen bromide clevage. Shallow-gradient Bio-Rex 70 chromatography indicates that histones H1/sup 0/a and H1/sup 0/b are the same as the respective CHO histones, H1(III) and H1(IV). This identification and the phosphate incorporation data of Gurley et al. (1975) reveal new features about H1/sup 0/ phosphorylation: (1) following release from G/sub 1/ arrest, H1/sup 0/a and H1/sup 0/b become phosphorylated in late G/sub 1/ prior to DNA synthesis; (2) H1/sup 0/a and H1/sup 0/b are phosphorylated at similar rates throughout the cell cycle. These and other data demonstrate that histone H1/sup 0/ is phosphorylated in a cell cycle dependent fashion which mimics that of histone H1.
OSTI ID:
5245797
Journal Information:
Biochemistry; (United States), Journal Name: Biochemistry; (United States) Vol. 20:15; ISSN BICHA
Country of Publication:
United States
Language:
English