DNase I sensitivity of ribosomal genes in isolated nucleosome core particles
Author(s) -
Chandrakant P. Giri,
Martin A. Gorovsky
Publication year - 1980
Publication title -
nucleic acids research
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 9.008
H-Index - 537
eISSN - 1362-4954
pISSN - 0305-1048
DOI - 10.1093/nar/8.1.197-e
Subject(s) - biology , nucleosome , tetrahymena , chromatin , deoxyribonuclease i , dnase i hypersensitive site , microbiology and biotechnology , ribosomal rna , dna , nuclease , hypersensitive site , micrococcal nuclease , gene , ribosomal dna , tetrahymena pyriformis , 30s , biochemistry , ribosome , rna , base sequence , phylogenetics
The level of chromatin structure at which DNase I recognizes conformational differences between inert and activated genes has been investigated. Bulk and ribosomal DNA's of Tetrahymena pyriformis were differentially labeled in vivo with [14C]- and [3H]-thymidine, respectively, utilizing a defined starvation-refeeding protocol. The 3H-labeled ribosomal genes were shown to be preferentially digested by DNase I in isolated nuclei. Staphylococcal nuclease digested the ribosomal genes more slowly than bulk DNA, probably owing to the higher GC content of rDNA. DNase I and staphylococcal nuclease digestions of purified nucleosomes and of nucleosome core particles isolated from dual-labeled, starved-refed nuclei were indistinguishable from those of intact nuclei. We conclude from these studies that DNase I recognizes an alteration in the internal nucleosome core structure of activated ribosomal genes.
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