Change in the pattern of histone binding to DNA upon transcriptional activation
- PMID: 2502314
- DOI: 10.1016/0092-8674(89)90399-1
Change in the pattern of histone binding to DNA upon transcriptional activation
Abstract
Patterns of histone binding to DNA of transcriptionally active D. melanogaster hsp70 genes within the nuclei have been analyzed by two methods of histone-DNA chemical cross-linking. When cross-linking is restricted to the central, "globular" regions of histones, it drops most for H1, to an intermediate extent for H2A and H2B, and least for H3 and H4 in transcriptionally active versus transcriptionally silent chromatin. When it occurs via histone terminal regions as well, cross-linking is quantitatively similar for active and inactive chromatin. Neither cross-linking method detects histones on the hsp70 promoter region. It appears that chromatin activation decreases histone binding to DNA via the "globular" regions, known to be essential for the folding of nucleosomes and the 30 nm chromatin fibril, but does not significantly affect the interaction of flexible and loosely bound histone "tails" with DNA. The role of these histone-DNA interaction changes in the unfolding of active chromatin and RNA polymerase reading through histone-bound DNA is discussed.
Similar articles
-
Effects of histone acetylation, ubiquitination and variants on nucleosome stability.Biochem J. 1993 Dec 15;296 ( Pt 3)(Pt 3):737-44. doi: 10.1042/bj2960737. Biochem J. 1993. PMID: 8280071 Free PMC article.
-
Factors affecting nucleosome structure in transcriptionally active chromatin. Histone acetylation, nascent RNA and inhibitors of RNA synthesis.Eur J Biochem. 1990 Dec 27;194(3):811-23. doi: 10.1111/j.1432-1033.1990.tb19474.x. Eur J Biochem. 1990. PMID: 1702716
-
Histone release during transcription: NAP1 forms a complex with H2A and H2B and facilitates a topologically dependent release of H3 and H4 from the nucleosome.Biochemistry. 2004 Mar 9;43(9):2359-72. doi: 10.1021/bi035737q. Biochemistry. 2004. PMID: 14992573
-
Chromatin structures condensed by linker histones.Essays Biochem. 2019 Apr 23;63(1):75-87. doi: 10.1042/EBC20180056. Print 2019 Apr 23. Essays Biochem. 2019. PMID: 31015384 Review.
-
Transcription: in tune with the histones.Cell. 1994 Apr 8;77(1):13-6. doi: 10.1016/0092-8674(94)90229-1. Cell. 1994. PMID: 8156588 Review.
Cited by
-
Nucleosomal histones of transcriptionally active/competent chromatin preferentially exchange with newly synthesized histones in quiescent chicken erythrocytes.Biochem J. 1990 Oct 1;271(1):67-73. doi: 10.1042/bj2710067. Biochem J. 1990. PMID: 2171504 Free PMC article.
-
The transcriptionally-active MMTV promoter is depleted of histone H1.Nucleic Acids Res. 1992 Jan 25;20(2):273-8. doi: 10.1093/nar/20.2.273. Nucleic Acids Res. 1992. PMID: 1311071 Free PMC article.
-
Transcriptional repression by nucleosomes but not H1 in reconstituted preblastoderm Drosophila chromatin.EMBO J. 1994 Jan 15;13(2):373-9. doi: 10.1002/j.1460-2075.1994.tb06271.x. EMBO J. 1994. PMID: 8313882 Free PMC article.
-
Disruption of higher-order folding by core histone acetylation dramatically enhances transcription of nucleosomal arrays by RNA polymerase III.Mol Cell Biol. 1998 Aug;18(8):4629-38. doi: 10.1128/MCB.18.8.4629. Mol Cell Biol. 1998. PMID: 9671473 Free PMC article.
-
Stably maintained microdomain of localized unrestrained supercoiling at a Drosophila heat shock gene locus.EMBO J. 1993 Mar;12(3):1067-75. doi: 10.1002/j.1460-2075.1993.tb05748.x. EMBO J. 1993. PMID: 8458324 Free PMC article.
MeSH terms
Substances
LinkOut - more resources
Full Text Sources
Molecular Biology Databases