Skip Navigation

This Article
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Add to My Personal Archive
Right arrow Download to citation manager
Right arrow Request Permissions
Google Scholar
Right arrow Articles by HAYASHI, T.
Right arrow Articles by IWAI, K.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by HAYASHI, T.
Right arrow Articles by IWAI, K.
Social Bookmarking
Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

J. Biochem, 1984, Vol. 95, No. 6 1741-1749
© 1984 Japanese Biochemical Society

research-article

Tetrahymena Histone H3. Purification and Two Variant Sequences1

Tomoko HAYASHI, Hiroaki HAYASHI, Yukihiro FUSAUCHI and Koichi IWAI

Department of Protein Chemistry, Institute of Endocrinology, Gunma University Maebashi, Gunma 371

The H3 histone of the protozoan Tetrahymena pyriformis was obtained as described previously (Fusauchi, Y. & Iwai, K. (1983) J. Biochem. 93, 1487–1497) and further purified by Sephadex G-50 chromatography after reduction and carboxymethylation. The purified H3 was shown to comprise two variants, 75 mol% of H3(1) and 25 mol% of H3(2). The H3 mixture was directly sequenced by Edman degradation from the N-terminal through residue 104. Sequence determination was further performed with tryptic peptides and cyanogen bromide fragments derived from the H3 mixture. Thus, the total sequences of H3(1) and H3(2) were completely determined; both consist of a total of 135 amino acid residues (the molecular weights in the unmodified form are 15,336 for H3(1) and 15,424 for H3(2)), and both are partially acetylated or methylated at the same six lysine residues to similar extents. The H3(1) and H3(2) sequences differ in 14 positions from each other, and in 17 and 21 positions from those of human spleen H3 (Ohe, Y. & Iwai, K. (1981) J. Biochem. 90, 1205–1211). The implications of these results for the structure-function relationship of this histone species and also for the phylogeny of protozoa are discussed.

1This study was supported in part by a Grant-in-Aid for Scientific Research from the Ministry of Education, Science and Culture of Japan.


Add to CiteULike CiteULike   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us    What's this?


This article has been cited by other articles:


Home page
 Proc. Natl. Acad. Sci. USAHome page
B. D. Strahl, R. Ohba, R. G. Cook, and C. D. Allis
Methylation of histone H3 at lysine 4 is highly conserved and correlates with transcriptionally active nuclei in Tetrahymena
PNAS, December 21, 1999; 96(26): 14967 - 14972.
[Abstract] [Full Text] [PDF]


Disclaimer: Please note that abstracts for content published before 1996 were created through digital scanning and may therefore not exactly replicate the text of the original print issues. All efforts have been made to ensure accuracy, but the Publisher will not be held responsible for any remaining inaccuracies. If you require any further clarification, please contact our Customer Services Department.