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

FEBS Letters

Slaughter, Clive A.³  Garrard, William T.²  Ball, Dorothy J.²  Hensley, Preston¹ 

[1] The Department of Biochemistry, Georgetown University Medical Center, Washington, DC 20007, USA;Division of Molecular Biology, The Department of Biochemistry, University of Texas Health Science Center at Dallas, 5323 Harry Hines Boulevard, Dallas, TX 75235, USA;The Department of Microbiology, The University of Texas Health Science Center at Dallas, 5323 Harry Hines Boulevard, Dallas, TX 75235, USA

关键词: Histone H2A.Z;    Nucleosome;    Evolution;    Histone variant;    Chromatin;    Amino acid sequence;   

DOI  :  10.1016/0014-5793(83)80896-5

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown