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Hen oviduct nuclei were subjected to pancreatic DNase I treatment under conditions known to preferentially degrade transcriptionally active genes (Weintraub, H., and Groudine, M. (1976) Science (Wash. D. C.) 93, 848-856). The ovalbumin gene, its structurally related genes, X and Y, and the spacer and flanking DNA were all found to exist in a DNase I-sensitive configuration. The DNase I-sensitive region was extended more than 20 kilobases beyond the 5' end of the X gene and approximately an equal distance beyond the 3' end of the ovalbumin gene before it became DNase I-resistant. The transition from a DNase I-sensitive to a -resistant conformation in oviduct chromatin occurred in a gradient fashion with 10 kilobases of DNA. Thus, ovalbumin and its related genes, X and Y, exist in a 100-kilobase DNase-sensitive domain in the oviduct tissue. In contrast, the entire domain was resistant to DNase I in spleen, liver, and erythrocyte nuclei. When the transcription of ovalbumin, X, and Y genes was eliminated by the withdrawal of hormone from estrogen-stimulated chicks, the entire domain remained in a DNase I-sensitive configuration. We conclude that DNase I-sensitive domains may provide the structural capability for gene expression and appear to be a result of the differentiation process since they are cell-specific and contain potentially expressible genes of that cell type. Repetitive sequences within this domain have been mapped and the possible relationship of these repetitive sequences to the DNase I-sensitive structure is discussed.
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Lawson et al. (1982) studied this question.
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