Abstract
The minor histone H2A subtype, H2A.Z, has been purified to homogeneity from calf thymus and subjected to automated Edman degradation. The sequence of the first 30 amino acids possesses only 60% homology with major H2A subtypes of the same tissue. This sequence difference is more extreme than that exhibited between evolutionarily distant major H2A subtypes. However, an analysis of secondary structure reveals that H2A.Z and major H2A subtypes exhibit the same general topographical features within their N-terminal domains.
Original language | English (US) |
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Pages (from-to) | 166-170 |
Number of pages | 5 |
Journal | FEBS Letters |
Volume | 154 |
Issue number | 1 |
DOIs | |
State | Published - Apr 5 1983 |
Keywords
- Amino acid sequence
- Chromatin
- Evolution
- Histone H2A.Z
- Histone variant
- Nucleosome
ASJC Scopus subject areas
- Biophysics
- Structural Biology
- Biochemistry
- Molecular Biology
- Genetics
- Cell Biology