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. 1982 Jun 1;203(3):577–582. doi: 10.1042/bj2030577

Precise elimination of the N-terminal domain of histone H1.

L Böhm, P Sautière, P D Cary, C Crane-Robinson
PMCID: PMC1158271  PMID: 7052061

Abstract

The proteinase from mouse submaxillary gland was used to cleave total calf thymus histone H1 between residues 32 and 33. The C-terminal peptide, comprising residues 33 to the C-terminus, was purified and identified by amino acids analysis and Edman degradation. Spectroscopic characterization by n.m.r. for tertiary structure and by c.d. for secondary structure shows the globular domain of the parent histone H1 to be preserved intact in the peptide. It has therefore lost only the N-terminal domain and is a fragment of histone H1 comprising the globular plus C-terminal domains only. Precise elimination of only the N-terminal domain makes the fragment suitable for testing domain function in histone H1.

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Selected References

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

  1. Allan J., Hartman P. G., Crane-Robinson C., Aviles F. X. The structure of histone H1 and its location in chromatin. Nature. 1980 Dec 25;288(5792):675–679. doi: 10.1038/288675a0. [DOI] [PubMed] [Google Scholar]
  2. Aviles F. J., Chapman G. E., Kneale G. G., Crane-Robinson C., Bradbury E. M. The conformation of histone H5. Isolation and characterisation of the globular segment. Eur J Biochem. 1978 Aug 1;88(2):363–371. doi: 10.1111/j.1432-1033.1978.tb12457.x. [DOI] [PubMed] [Google Scholar]
  3. Barbero J. L., Franco L., Montero F., Morán F. Structural studies on histones H1. Circular dichroism and difference spectroscopy of the histones H1 and their trypsin-resistant cores from calf thymus and from the fruit fly Ceratitis capitata. Biochemistry. 1980 Aug 19;19(17):4080–4087. doi: 10.1021/bi00558a027. [DOI] [PubMed] [Google Scholar]
  4. Bradbury E. M., Cary P. D., Chapman G. E., Crane-Robinson C., Danby S. E., Rattle H. W., Boublik M., Palau J., Aviles F. J. Studies on the role and mode of operation of the very-lysine-rich histone H1 (F1) in eukaryote chromatin. The conformation of histone H1. Eur J Biochem. 1975 Apr 1;52(3):605–613. doi: 10.1111/j.1432-1033.1975.tb04032.x. [DOI] [PubMed] [Google Scholar]
  5. Böhm E. L., Strickland W. N., Strickland M., Thwaits B. H., van der Westhuizen D. R., von Holt C. Purification of the five main calf thymus histone fractions by gel exclusion chromatography. FEBS Lett. 1973 Aug 15;34(2):217–221. doi: 10.1016/0014-5793(73)80797-5. [DOI] [PubMed] [Google Scholar]
  6. Chen Y. H., Yang J. T., Chau K. H. Determination of the helix and beta form of proteins in aqueous solution by circular dichroism. Biochemistry. 1974 Jul 30;13(16):3350–3359. doi: 10.1021/bi00713a027. [DOI] [PubMed] [Google Scholar]
  7. Giancotti V., Russo E., Cosimi S., Cary P. D., Crane-Robinson C. Secondary and tertiary structural differences between histone H1 molecules from calf thymus and sea-urchin (Sphaerechinus granularis) sperm. Biochem J. 1981 Sep 1;197(3):655–660. doi: 10.1042/bj1970655. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Hartman P. G., Chapman G. E., Moss T., Bradbury E. M. Studies on the role and mode of operation of the very-lysine-rich histone H1 in eukaryote chromatin. The three structural regions of the histone H1 molecule. Eur J Biochem. 1977 Jul 1;77(1):45–51. doi: 10.1111/j.1432-1033.1977.tb11639.x. [DOI] [PubMed] [Google Scholar]
  9. Laemmli U. K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 1970 Aug 15;227(5259):680–685. doi: 10.1038/227680a0. [DOI] [PubMed] [Google Scholar]
  10. Liao L. W., Cole R. D. The amino acid sequence of residues 1-104 of CTL-1, a bovine H1 histone. J Biol Chem. 1981 Mar 25;256(6):3024–3029. [PubMed] [Google Scholar]
  11. Macleod A. R., Wong N. C., Dixon G. H. The amino-acid sequence of trout-testis histone H1. Eur J Biochem. 1977 Aug 15;78(1):281–291. doi: 10.1111/j.1432-1033.1977.tb11739.x. [DOI] [PubMed] [Google Scholar]
  12. Moss T., Cary P. D., Abercrombie B. D., Crane-Robinson C., Bradbury E. M. A pH-dependent interaction between histones H2A and H2B involving secondary and tertiary folding. Eur J Biochem. 1976 Dec 11;71(2):337–350. doi: 10.1111/j.1432-1033.1976.tb11120.x. [DOI] [PubMed] [Google Scholar]
  13. Puigdomenech P., Palau J., Crane-Robinson C. The structure of sea-urchin-sperm histone phi 1 (H1) in chromatin and in free solution. Trypsin digestion and spectroscopic studies. Eur J Biochem. 1980 Feb;104(1):263–270. doi: 10.1111/j.1432-1033.1980.tb04424.x. [DOI] [PubMed] [Google Scholar]

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