Two protein-binding sites in chromatin implicated in the activation of heat-shock genes
- 1 May 1984
- journal article
- research article
- Published by Springer Science and Business Media LLC in Nature
- Vol. 309 (5965), 229-234
- https://doi.org/10.1038/309229a0
Abstract
The resistance to exonuclease digestion of 2 regions of chromatin at the 5'' end of heat-shock genes in Drosophila implies they have protein bound to them. The pattern of resistance before and after induction of gene expression suggests that heat-shock genes are activated by the sequential binding of at least 2 protein factors.Keywords
This publication has 45 references indexed in Scilit:
- Active chromatinNature, 1982
- Evolutionary implications of a complex pattern of DNA sequence homology extending far upstream of the hsp70 genes at loci 87A7 and 87C1 in Drosophila melanogasterJournal of Molecular Biology, 1982
- DNAase I-hypersensitive sites of chromatinCell, 1981
- The 5′ ends of Drosophila heat shock genes in chromatin are hypersensitive to DNase INature, 1980
- The chromatin structure of specific genes: I. Evidence for higher order domains of defined DNA sequenceCell, 1979
- A stretch of “late” SV40 viral DNA about 400 bp long which includes the origin of replication is specifically exposed in SV40 minichromosomesCell, 1979
- Sites in simian virus 40 chromatin which are preferentially cleaved by endonucleasesCell, 1978
- Origin of DNA replication in papovavirus chromatin is recognized by endogenous endonuclease.Proceedings of the National Academy of Sciences of the United States of America, 1978
- SV40 viral minichromosome: preferential exposure of the origin of replication as probed by restriction endonucleasesNucleic Acids Research, 1978
- Relation of Nucleosomes to DNA SequencesCold Spring Harbor Symposia on Quantitative Biology, 1978