Temperature-dependent cleavage of chromatin by micrococcal nuclease near the nucleosome center

Sue Ying Huang, William T. Garrard

Research output: Contribution to journalArticlepeer-review

5 Scopus citations


Digestion of nuclei at 4°C with micrococcal nuclease results in significant intranucleosomal cleavage compared to digestion conducted at 37°C. Employing nucleoprotein gel electrophoresis in one dimension followed by DNA electrophoresis in a second dimension, we demonstrate that such temperature-sensitive, internal cleavage predominantly occurs about 20 bp from the nucleosome center. We suggest that lower temperatures reduce the stability of hydrophobic interactions within the histone octamer and lead to a conformational alteration in nucleosomes that is detected by micrococcal nuclease.

Original languageEnglish (US)
Pages (from-to)89-91
Number of pages3
JournalFEBS Letters
Issue number1
StatePublished - Apr 7 1986


  • Chromatin structure
  • Half-nucleosome
  • Histone octamer
  • Micrococcal nuclease
  • Nucleosome
  • Two-dimensional electrophoresis

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology


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