Amino acid sequence of the N-terminal domain of calf thymus histone H2A.Z

Dorothy J. Ball, Clive A. Slaughter, Preston Hensley, William T. Garrard

Research output: Contribution to journalArticle

19 Citations (Scopus)

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 languageEnglish (US)
Pages (from-to)166-170
Number of pages5
JournalFEBS Letters
Volume154
Issue number1
DOIs
StatePublished - Apr 5 1983
Externally publishedYes

Fingerprint

Thymus
Histones
Thymus Gland
Amino Acid Sequence
Tissue
Amino Acids
Degradation

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

Cite this

Amino acid sequence of the N-terminal domain of calf thymus histone H2A.Z. / Ball, Dorothy J.; Slaughter, Clive A.; Hensley, Preston; Garrard, William T.

In: FEBS Letters, Vol. 154, No. 1, 05.04.1983, p. 166-170.

Research output: Contribution to journalArticle

Ball, Dorothy J. ; Slaughter, Clive A. ; Hensley, Preston ; Garrard, William T. / Amino acid sequence of the N-terminal domain of calf thymus histone H2A.Z. In: FEBS Letters. 1983 ; Vol. 154, No. 1. pp. 166-170.
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