Abstract
Calf-thymus histone III is a single polypeptide chain of 135 residues (combined molecular weight of 15,324) with alanine at both the amino and carboxyl ends. The NH2-terminal region (Residues 1-53) of histone III is strongly basic (net charge of +18) and contains lysines-14 and -23, which are ε-N-acetylated in a fraction of the molecules, as well as lysines-9 and -27, which are partially ε-N-methylated. The COOH-terminal region (Residues 54-135) is only slightly basic (net charge of +4), contains most of the hydrophobic residues, and has a 29-residue sequence that lacks a basic residue. The two cysteines are in the nonbasic region at positions 96 and 110. A few sequence similarities of calf-thymus histone III with other histones have been noted.
Keywords: acetyllysine, methyllysine, acetylation, methylation
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- DeLange R. J. Egg white avidin. I. Amino acid composition; sequence of the amino- and carboxyl-terminal cyanogen bromide peptides. J Biol Chem. 1970 Mar 10;245(5):907–916. [PubMed] [Google Scholar]
- DeLange R. J., Fambrough D. M., Smith E. L., Bonner J. Calf and pea histone IV. 3. Complete amino acid sequence of pea seedling histone IV; comparison with the homologous calf thymus histone. J Biol Chem. 1969 Oct 25;244(20):5669–5679. [PubMed] [Google Scholar]
- DeLange R. J., Fambrough D. M., Smith E. L., Bonner J. Calf and pea histone IV. I. Amino acid compositions and the identical COOH-terminal 19-residue sequence. J Biol Chem. 1968 Nov 25;243(22):5906–5913. [PubMed] [Google Scholar]
- DeLange R. J., Fambrough D. M., Smith E. L., Bonner J. Calf and pea histone IV. II. The complete amino acid sequence of calf thymus histone IV; presence of epsilon-N-acetyllysine. J Biol Chem. 1969 Jan 25;244(2):319–334. [PubMed] [Google Scholar]
- DeLange R. J., Smith E. L., Bonner J. Calf thymus histone 3: sequences of the amino-and carboxyl-terminal regions and of the regions containing lysyl residues modified by acetylation and methylation. Biochem Biophys Res Commun. 1970 Aug 24;40(4):989–993. doi: 10.1016/0006-291x(70)91001-6. [DOI] [PubMed] [Google Scholar]
- DeLange R. J., Smith E. L. Histones: structure and function. Annu Rev Biochem. 1971;40:279–314. doi: 10.1146/annurev.bi.40.070171.001431. [DOI] [PubMed] [Google Scholar]
- Fambrough D. M., Bonner J. Sequence homology and role of cysteine in plant and animal arginine-rich histones. J Biol Chem. 1968 Sep 10;243(17):4434–4439. [PubMed] [Google Scholar]
- Greenaway P. J., Murray K. Heterogeneity and polymorphism in chicken erythrocyte histone fraction V. Nat New Biol. 1971 Feb 24;229(8):233–238. doi: 10.1038/newbio229233a0. [DOI] [PubMed] [Google Scholar]
- Greenaway P. J. Studies on the primary structure of chicken erythrocyte histone fraction V. Biochem J. 1971 Sep;124(2):319–325. doi: 10.1042/bj1240319. [DOI] [PMC free article] [PubMed] [Google Scholar]
- HIRS C. H. The oxidation of ribonuclease with performic acid. J Biol Chem. 1956 Apr;219(2):611–621. [PubMed] [Google Scholar]
- Hayashi H., Iwai K. Calf thymus alanine-rich, leucine-rich histone: sequences of the tryptic peptides and characteristic distributions of the basic and other residues in the molecule. J Biochem. 1971 Sep;70(3):543–547. doi: 10.1093/oxfordjournals.jbchem.a129670. [DOI] [PubMed] [Google Scholar]
- Hnilica L. S., Kappler H. A., Jordan J. J. Assymetry in the distribution of basic amino acid residues in the moderately lysine-rich histone F2b from calf thymus. Experientia. 1970 Apr 15;26(4):353–355. doi: 10.1007/BF01896882. [DOI] [PubMed] [Google Scholar]
- Iwai K., Ishikawa K., Hayashi H. Amino-acid sequence of slightly lysine-rich histone. Nature. 1970 Jun 13;226(5250):1056–1058. doi: 10.1038/2261056b0. [DOI] [PubMed] [Google Scholar]
- Johns E. W. Studies on histones. 7. Preparative methods for histone fractions from calf thymus. Biochem J. 1964 Jul;92(1):55–59. doi: 10.1042/bj0920055. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Murray K. The acid extraction of histones from calf thymus deoxyribonucleoprotein. J Mol Biol. 1966 Feb;15(2):409–419. doi: 10.1016/s0022-2836(66)80116-x. [DOI] [PubMed] [Google Scholar]
- Ogawa Y., Quagliarotti G., Jordan J., Taylor C. W., Starbuck W. C., Busch H. Structural analysis of the glycine-rich, arginine-rich histone. 3. Sequence of the amino-terminal half of the molecule containing the modified lysine residues and the total sequence. J Biol Chem. 1969 Aug 25;244(16):4387–4392. [PubMed] [Google Scholar]
- Panyim S., Sommer K. R., Chalkley R. Oxidation of the cysteine-containing histone F3. Detection of an evolutionary mutation in a conservative histone. Biochemistry. 1971 Oct 12;10(21):3911–3917. doi: 10.1021/bi00797a018. [DOI] [PubMed] [Google Scholar]
- Rall S. C., Cole R. D. Amino acid sequence and sequence variability of the amino-terminal regions of lysine-rich histones. J Biol Chem. 1971 Dec 10;246(23):7175–7190. [PubMed] [Google Scholar]
- Sadgopal A., Bonner J. Proteins of interphase and metaphase chromosomes compared. Biochim Biophys Acta. 1970 Apr 28;207(1):227–239. doi: 10.1016/0005-2795(70)90154-6. [DOI] [PubMed] [Google Scholar]
- Sautiere P., Tyrou D., Moschetto Y., Biserte G. Structure primaire de l'histone riche en glycine et en arginine isolée de la tumeur de chloroleucémic du rat. Biochimie. 1971;53(4):479–483. doi: 10.1016/s0300-9084(71)80165-7. [DOI] [PubMed] [Google Scholar]
- Sautière P., Breynaert M. D., Moschetto Y., Biserte G. Séquence complète des acides aminés de l'histone riche en glycine et en arginine du thymus de porc. C R Acad Sci Hebd Seances Acad Sci D. 1970 Jul 20;271(3):364–365. [PubMed] [Google Scholar]
- Sung M. T., Dixon G. H. Modification of histones during spermiogenesis in trout: a molecular mechanism for altering histone binding to DNA. Proc Natl Acad Sci U S A. 1970 Nov;67(3):1616–1623. doi: 10.1073/pnas.67.3.1616. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Wilson R. K., Starbuck W. C., Taylor C. W., Jordan J., Busch H. Structure of the glycine-rich, arginine-rich histone of the Novikoff hepatoma. Cancer Res. 1970 Dec;30(12):2942–2951. [PubMed] [Google Scholar]