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Molecular Biology Reports

, Volume 10, Issue 3, pp 147–151 | Cite as

Modification of the lysine residues of histones H1 and H5: Effects on structure and on the binding to chromatin

  • J. Jordano
  • J. L. Barbero
  • F. Montero
  • E. Palacián
Article

Abstract

The extensive modification of histone H1 from calf thymus with the amino-group reagent dimethylmaleic anhydride (over 35 lysine residues modified per molecule) produces no effect on its secondary structure detectable by circular dichroism (far UV). Fluorescence and circular dichroism (near-UV) of the modified histone show variations in the local environment of its sole tyrosine residue. These changes are reversed on regeneration of the modified amino groups. While histone H1 is easily dissociated with this reagent from calf thymus or chicken erythrocyte chromatin, a much stronger treatment is needed to liberate histone H5 from erythrocyte chromatin. This difference appears to be related to the higher arginine content of histone H5.

Keywords

Tyrosine Secondary Structure Arginine Anhydride Circular Dichroism 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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Copyright information

© Dr W. Junk Publishers 1985

Authors and Affiliations

  • J. Jordano
    • 1
    • 2
  • J. L. Barbero
    • 3
  • F. Montero
    • 3
  • E. Palacián
    • 1
    • 2
  1. 1.Consejo Superior de Investigaciones CientíficasCentro de Biología MolecularMadrid-34Spain
  2. 2.Universidad Autónoma de MadridMadrid-34Spain
  3. 3.Departamento de Bioquímica, Facultad de Ciencias QuímicasUniversidad ComplutenseMadrid-3Spain

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