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Human spleen histone H3. Isolation and amino acid sequence
Journal of Biochemistry
|October 1, 1981
Summary
Researchers sequenced human spleen histone H3, finding it nearly identical to calf thymus H3. This study provides insights into histone evolution and identifies variations suggesting multiple human H3 variants.
Area of Science:
- Biochemistry
- Molecular Biology
- Evolutionary Biology
Background:
- Histone H3 is a core component of eukaryotic chromatin.
- Previous studies characterized human spleen histone H2B and H2A.
- Understanding histone H3 sequence variations is crucial for evolutionary studies.
Purpose of the Study:
- To determine the amino acid sequence of human spleen histone H3.
- To compare human H3 with other eukaryotic H3 sequences.
- To investigate histone evolution through sequence analysis.
Main Methods:
- Purification of histone H3 fraction using Bio-Gel P-10 chromatography.
- Enzymatic digestion of histone H3 with Clostripain, trypsin, and chymotrypsin.
- Peptide sequencing via Edman degradation.
Main Results:
- The human spleen histone H3 sequence consists of 135 amino acid residues.
- It is nearly identical to calf thymus H3, with five substitutions identified.
- Three methylated lysines and two acetylated lysines were detected, indicating post-translational modifications.
- Sequence variations suggest the presence of at least two human H3 variants.
Conclusions:
- Human spleen histone H3 exhibits high conservation across eukaryotes.
- Identified substitutions and modifications offer insights into histone H3 evolution.
- The findings support the presence of multiple histone H3 variants in humans.