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Pea histones H2A and H2B. Variable and conserved regions in the sequences
Journal of Biochemistry
|August 1, 1977
Summary
Pea histone H2A and H2B proteins show distinct amino-terminal regions compared to calf histones, suggesting evolutionary variability in these DNA-binding domains. Conserved hydrophobic regions are crucial for chromatin structure.
Area of Science:
- Molecular Biology
- Biochemistry
- Chromatin Biology
Background:
- Histones are fundamental proteins involved in DNA packaging and chromatin structure.
- Understanding histone variations across species provides insights into evolutionary conservation and functional divergence.
Purpose of the Study:
- To characterize and compare pea histone H2A and H2B with their calf counterparts.
- To investigate the structural and sequence differences, particularly in the amino-terminal regions.
Main Methods:
- Purification of pea histone II group (H2A and H2B) using ion-exchange, carboxymethylcellulose, and Bio-Gel P-60 chromatography.
- Analysis of chromatographic behavior and gel electrophoretic mobilities.
- Amino acid composition analysis and partial sequencing of pea H2B using BrCN cleavage and tryptic peptide mapping.
Main Results:
- Pea H2A and H2B exhibited distinct chromatographic and electrophoretic properties compared to calf histones.
- Amino acid compositions were similar overall but showed detailed differences.
- Pea H2B possesses a unique amino-terminal region with a blocked N-terminus and more residues, while hydrophobic regions show some divergence.
Conclusions:
- The amino-terminal regions of pea H2A and H2B histones are evolutionarily variable, likely maintaining basicity for DNA binding.
- Conserved hydrophobic regions in H2A, H2B, H3, and H4 are essential for stable histone core formation in chromatin.