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Nuclear type II [3H]estradiol binding sites: a histone H3-H4 complex
Kevin Shoulars1, Mary Ann Rodrigues, Jan R Crowley
1Department of Molecular and Cellular Biology, Baylor College of Medicine, One Baylor Plaza, Houston, TX 77030-3498, USA.
Summary
[(3)H]luteolin binds to histone H4 and a 35kDa H3-H4 dimer in rat uterine nuclei. This suggests bioflavonoids may modulate histone function, impacting gene transcription and cell proliferation.
Area of Science:
- Biochemistry
- Molecular Biology
- Endocrinology
Background:
- Type II binding sites in rat uterine nuclear extracts were previously labeled by [(3)H]luteolin.
- An 11kDa protein was identified as histone H4, while a 35kDa protein was recognized by anti-histone H4 antibodies.
Purpose of the Study:
- To identify the 35kDa protein labeled by [(3)H]luteolin.
- To investigate the role of histone dimers in [(3)H]luteolin binding.
- To explore the potential of bioflavonoids in modulating histone function.
Main Methods:
- Purification of calf thymus core histones retaining [(3)H]luteolin binding activity.
- Recombination studies using purified histone H3 and H4.
- Analysis of [(3)H]luteolin binding to histone complexes.
Main Results:
- Purified calf thymus core histones retained [(3)H]luteolin binding activity.
- Mixing experiments generated a 35kDa H3-H4 dimer that binds [(3)H]luteolin.
- This 35kDa dimer is equivalent to the protein found in rat uterine nuclear extracts.
Conclusions:
- The 35kDa [(3)H]luteolin binding protein is likely an H3-H4 dimer.
- Type II site ligands like luteolin may modulate histone function.
- This interaction could influence histone-dependent gene transcription and cellular proliferation.