Open AccessTransient Unfolding of Trypsin‐Digested Chromatin Core Particles
Author(s) -
GRIGORYEV Sergei A.,
KRASHENINNIKOV Igor A.
Publication year - 1982
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1982.tb07029.x
Subject(s) - nucleosome , histone , trypsin , chromatin , biophysics , circular dichroism , cleavage (geology) , nucleoprotein , chemistry , linker dna , crystallography , dna , biochemistry , biology , enzyme , fracture (geology) , paleontology
Limited digestion of nucleosome core particles with trypsin caused cleavage and removal of N‐terminal histone sequences of 10–30 amino acids. The proteolyzed core particles exhibited salt‐dependent structural transitions revealed by sedimentation, circular dichroism and nuclease‐cutting assays, while the intact nucleosome cores were not affected under the experimental conditions. The results obtained indicate that the observed transitions correspond to the transient unfolding of terminal segments of core particle nucleoprotein caused by the increase of its net negative charge. The excision of the N‐terminal histone domains therefore leads to partial destabilization but not to irreversible disruption of the compact nucleosome structure.