Skip to main content
NCBI home page
Proceedings of the National Academy of Sciences of the United States of America logoLink to Proceedings of the National Academy of Sciences of the United States of America
. 1972 Aug;69(8):2015–2019. doi: 10.1073/pnas.69.8.2015

Amino-Terminal Sequences and Sites of In Vivo Acetylation of Trout-Testis Histones III and IIb2

E Peter M Candido 1, Gordon H Dixon 1
PMCID: PMC426858  PMID: 4506069

Abstract

The sequences of the first 25 residues of histone III, and the first 22 residues of histone IIb2, from trout testis have been determined on an automatic protein sequencer. The amino-terminal sequence of trout-testis histone III is identical to the corresponding region of calfthymus histone III, whereas the trout-testis histone IIb2 sequence differs from that of calf-thymus histone IIb2 at several positions in the amino-terminal region. Several in vivo sites of acetylation of these trout-testis histones have also been determined, by the same automated procedure. In addition to the two main sites at lysyl residues 14 and 23 acetylated in calf-thymus histone III, a lower degree of acetylation at two other sites, lysyl residues 9 and 18, has been detected. Four sites of acetylation have also been detected in trout-testis histone IIb2, at lysyl residues 5, 10, 13, and 18. When the amino-acid sequences around the acetylated lysyl residues of different histones are compared, striking similarities are seen. The methods used in these studies should prove useful in elucidation of the locations of chemically stable modifications in other proteins.

Keywords: protein sequencer, [14C]acetate, sequence homology

Full text

PDF
2015

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Africa B., Carpenter F. H. Alkaline hydrolysis of phenylthiohydantoins of amino acids. Biochem Biophys Res Commun. 1966 Jul 6;24(1):113–119. doi: 10.1016/0006-291x(66)90418-9. [DOI] [PubMed] [Google Scholar]
  2. Candido E. P., Dixon G. H. Sites of in vivo acetylation in trout testis histone IV. J Biol Chem. 1971 May 25;246(10):3182–3188. [PubMed] [Google Scholar]
  3. Capra J. D., Kehoe J. M., Kotelchuck D., Walter R., Breslow E. Evolution of neurophysin proteins: the partial sequence of bovine neurophysin-I (vasopressin-oxytocin-carrier proteins-automated amino-acid-sequence analysis-homology-protein evolution). Proc Natl Acad Sci U S A. 1972 Feb;69(2):431–434. doi: 10.1073/pnas.69.2.431. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. 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]
  5. DeLange R. J., Hooper J. A., Smith E. L. Complete amino-acid sequence of calf-thymus histone 3. Proc Natl Acad Sci U S A. 1972 Apr;69(4):882–884. doi: 10.1073/pnas.69.4.882. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. 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]
  7. 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]
  8. Edman P., Begg G. A protein sequenator. Eur J Biochem. 1967 Mar;1(1):80–91. doi: 10.1007/978-3-662-25813-2_14. [DOI] [PubMed] [Google Scholar]
  9. Gallwitz D. Organ specificity of histone Acetyltransferases. FEBS Lett. 1971 Mar 22;13(5):306–308. doi: 10.1016/0014-5793(71)80247-8. [DOI] [PubMed] [Google Scholar]
  10. 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]
  11. 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]
  12. Olson M. O., Jordan J., Busch H. The amino terminal sequence of calf thymus histone 3. Biochem Biophys Res Commun. 1972 Jan 14;46(1):50–55. doi: 10.1016/0006-291x(72)90628-6. [DOI] [PubMed] [Google Scholar]
  13. Sung M., Smithies O. Differential elution of histones from gel-trapped nuclei. Biopolymers. 1969;7(1):39–58. doi: 10.1002/bip.1969.360070105. [DOI] [PubMed] [Google Scholar]
  14. Van Orden H. O., Carpenter F. H. Hydrolysis of phenylthiohydantoins of amino acids. Biochem Biophys Res Commun. 1964;14:399–403. doi: 10.1016/0006-291x(64)90075-0. [DOI] [PubMed] [Google Scholar]
  15. Vidali G., Gershey E. L., Allfrey V. G. Chemical studies of histone acetylation. The distribution of epsilon-N-acetyllysine in calf thymus histones. J Biol Chem. 1968 Dec 25;243(24):6361–6366. [PubMed] [Google Scholar]

Articles from Proceedings of the National Academy of Sciences of the United States of America are provided here courtesy of National Academy of Sciences

RESOURCES