Phosphorylation of the butyrate-enhanced protein, histone H1/sup 0/, in Chinese hamster cells. [Effects on H1 configuration and on H1-DNA interactions]
Although the model studies focus attention upon the ability of H1 phosphorylation to alter H1-DNA interactions, the molecular effects of H1 phosphorylation in chromatin remain unresolved. Part of the difficulty has been technical. For example, most H1 molecules become dephosphorylated during the isolation of chromatin and chromosomes; therefore, it has not been possible to compare the properties of fully phosphorylated chromatin or chromatin subunits with those of their unphosphorylated counterparts. Recent reports, however, suggest that it may be possible to replace unphosphorylated H1 with phosphorylated H1 in oligonucleosomes, nucleosomes, and chromatosomes. Hence, in the near future, we anticipate significant advances in this area.
- Research Organization:
- Los Alamos National Laboratory (LANL), Los Alamos, NM (United States); Oregon State Univ., Corvallis (USA). Dept. of Biochemistry and Biophysics; Mayo Clinic, Rochester, MN (USA)
- DOE Contract Number:
- W-7405-ENG-36
- OSTI ID:
- 5064221
- Report Number(s):
- LA-UR-80-2535; CONF-800984-1
- Resource Relation:
- Conference: Protein phosphorylation meeting, Cold Spring Harbor, NY, USA, Sep 1980
- Country of Publication:
- United States
- Language:
- English
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