Literature DB >> 11881

Histone-histone interactions. II. Structural stability of the histone H3-H4 complex.

P N Lewis.   

Abstract

The stability of the histone H3-H4 complex toward urea, changes in pH and ionic strength, and certain chemical modifications have been examined by gel electrophoresis anc circular dichronism. When uncomplexed, the two cysteine residues of histone H3 become rapidly oxidized, forming an intramolecular disulfide bridge which apparently blocks complex formation on return to complexing conditions. The complex was found to be unstable toward low values of pH and ionic strength, concentrations of urea exceeding 1 M, modifications of the cysteine residues, and fragmention in which the C terminal portions of either H3 or H4 are removed. A possible structure for this complex is proposed.

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Year:  1976        PMID: 11881     DOI: 10.1139/o76-139

Source DB:  PubMed          Journal:  Can J Biochem        ISSN: 0008-4018


  2 in total

1.  Nucleosomal structure as probed by H3 histone thiol reactivity. Conformation of H3 histone variants is differently affected by thiol group reagents.

Authors:  N Ferrari; U Pfeffer; G Vidali
Journal:  Cell Biophys       Date:  1987-02

2.  Infrared spectroscopy and X-ray diffraction study of complexes of histones H3 and H4 in the condensed state.

Authors:  E J Wachtel; C Gilon; R Sperling
Journal:  Nucleic Acids Res       Date:  1981-08-11       Impact factor: 16.971

  2 in total

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