Amino acid sequence of the N-terminal domain of calf thymus histone H2A.Z
- Dorothy J. Ball(corresponding author),
- ,
- Preston Hensley,
- William T. Garrard
- University of Texas Southwestern Medical Center,
- Georgetown University
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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.
Publication Information
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Scholary Output:
Contribution to journal
Article
Peer-reviewOriginal language
English (US)Pages from-to (Number of pages)
Pages 166-170 (5 pages)Journal (Volume, Issue Number)
FEBS Letters (Volume 154, Issue 1)Publication milestones
- Published - 04/05/1983
Publication status
Published - 04/05/1983
ISSN
0014-5793Publication IDs
- Scopus: 0021095306
- PubMed: 6832364
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Funding Details
We thank Dr Brent Reed and Messrs Lonnie Sorrells and Melvin Dews for performing the amino acid analysis. We are indebted to Dr J. Donald Capra in whosel aboratoryt he automated sequencingw as performed and to Dr Michael Karels for making availablet o us the secondary structure prediction routine. This researchw as supported by grants from NIH (GM22201 and GM29935)a nd The Robert A. Welch Foundation (I-823) to W.G., by NIH grant AI12127 to J. Donald Capra, and by NIH grant GM28731 to R.H.; C.S. was supportedb y an NIH postdoctoral fellowship (GM07710).
FundersFunding numbers
Robert A. Welch Foundation
GM28731, GM07710, AI12127, I-823
NIH
GM22201
NIGMS
R01GM029935