Core histone hyperacetylation co-maps with generalized DNase I sensitivity in the chicken beta-globin chromosomal domain. (original) (raw)

• Journal List
• EMBO J
• v.13(8); 1994 Apr 15
• PMC395022

EMBO J. 1994 Apr 15; 13(8): 1823–1830.

Biophysics Laboratories, University of Portsmouth, UK.

Abstract

The distribution of core histone acetylation across the chicken beta-globin locus has been mapped in 15 day chicken embryo erythrocytes by immunoprecipitation of mononucleosomes with an antibody recognizing acetylated histones, followed by hybridization probing at several points in the locus. A continuum of acetylation was observed, covering both genes and intergenic regions. Using the same probes, the generalized sensitivity to DNase I was mapped by monitoring the disappearance of intact genomic restriction fragments from Southern transfers. Close correspondence between the 33 kb of sensitive chromatin and the extent of acetylation indicates that one role of the modification could be the generation and/or maintenance of the open conformation. The precision of acetylation mapping makes it a possible approach to the definition of chromosomal domain boundaries.

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• Allan J, Harborne N, Rau DC, Gould H. Participation of core histone "tails" in the stabilization of the chromatin solenoid. J Cell Biol. 1982 May;93(2):285–297. [PMC free article] [PubMed] [Google Scholar]
• ALLFREY VG, FAULKNER R, MIRSKY AE. ACETYLATION AND METHYLATION OF HISTONES AND THEIR POSSIBLE ROLE IN THE REGULATION OF RNA SYNTHESIS. Proc Natl Acad Sci U S A. 1964 May;51:786–794. [PMC free article] [PubMed] [Google Scholar]
• Bonner WM, West MH, Stedman JD. Two-dimensional gel analysis of histones in acid extracts of nuclei, cells, and tissues. Eur J Biochem. 1980 Aug;109(1):17–23. [PubMed] [Google Scholar]
• Braunstein M, Rose AB, Holmes SG, Allis CD, Broach JR. Transcriptional silencing in yeast is associated with reduced nucleosome acetylation. Genes Dev. 1993 Apr;7(4):592–604. [PubMed] [Google Scholar]
• Chung JH, Whiteley M, Felsenfeld G. A 5' element of the chicken beta-globin domain serves as an insulator in human erythroid cells and protects against position effect in Drosophila. Cell. 1993 Aug 13;74(3):505–514. [PubMed] [Google Scholar]
• Clayton AL, Hebbes TR, Thorne AW, Crane-Robinson C. Histone acetylation and gene induction in human cells. FEBS Lett. 1993 Dec 20;336(1):23–26. [PubMed] [Google Scholar]
• Csordas A. On the biological role of histone acetylation. Biochem J. 1990 Jan 1;265(1):23–38. [PMC free article] [PubMed] [Google Scholar]
• Durrin LK, Mann RK, Kayne PS, Grunstein M. Yeast histone H4 N-terminal sequence is required for promoter activation in vivo. Cell. 1991 Jun 14;65(6):1023–1031. [PubMed] [Google Scholar]
• Felsenfeld G. Chromatin as an essential part of the transcriptional mechanism. Nature. 1992 Jan 16;355(6357):219–224. [PubMed] [Google Scholar]
• Grunstein M. Histone function in transcription. Annu Rev Cell Biol. 1990;6:643–678. [PubMed] [Google Scholar]
• Hebbes TR, Thorne AW, Crane-Robinson C. A direct link between core histone acetylation and transcriptionally active chromatin. EMBO J. 1988 May;7(5):1395–1402. [PMC free article] [PubMed] [Google Scholar]
• Hebbes TR, Turner CH, Thorne AW, Crane-Robinson C. A "minimal epitope" anti-protein antibody that recognises a single modified amino acid. Mol Immunol. 1989 Sep;26(9):865–873. [PubMed] [Google Scholar]
• Hebbes TR, Thorne AW, Clayton AL, Crane-Robinson C. Histone acetylation and globin gene switching. Nucleic Acids Res. 1992 Mar 11;20(5):1017–1022. [PMC free article] [PubMed] [Google Scholar]
• Jantzen K, Fritton HP, Igo-Kemenes T. The DNase I sensitive domain of the chicken lysozyme gene spans 24 kb. Nucleic Acids Res. 1986 Aug 11;14(15):6085–6099. [PMC free article] [PubMed] [Google Scholar]
• Jeppesen P, Turner BM. The inactive X chromosome in female mammals is distinguished by a lack of histone H4 acetylation, a cytogenetic marker for gene expression. Cell. 1993 Jul 30;74(2):281–289. [PubMed] [Google Scholar]
• Kamakaka RT, Thomas JO. Chromatin structure of transcriptionally competent and repressed genes. EMBO J. 1990 Dec;9(12):3997–4006. [PMC free article] [PubMed] [Google Scholar]
• Kellum R, Schedl P. A position-effect assay for boundaries of higher order chromosomal domains. Cell. 1991 Mar 8;64(5):941–950. [PubMed] [Google Scholar]
• Kornberg RD, Lorch Y. Chromatin structure and transcription. Annu Rev Cell Biol. 1992;8:563–587. [PubMed] [Google Scholar]
• Lawson GM, Knoll BJ, March CJ, Woo SL, Tsai MJ, O'Malley BW. Definition of 5' and 3' structural boundaries of the chromatin domain containing the ovalbumin multigene family. J Biol Chem. 1982 Feb 10;257(3):1501–1507. [PubMed] [Google Scholar]
• Lee DY, Hayes JJ, Pruss D, Wolffe AP. A positive role for histone acetylation in transcription factor access to nucleosomal DNA. Cell. 1993 Jan 15;72(1):73–84. [PubMed] [Google Scholar]
• Levy-Wilson B, Fortier C. The limits of the DNase I-sensitive domain of the human apolipoprotein B gene coincide with the locations of chromosomal anchorage loops and define the 5' and 3' boundaries of the gene. J Biol Chem. 1989 Dec 15;264(35):21196–21204. [PubMed] [Google Scholar]
• Mann RK, Grunstein M. Histone H3 N-terminal mutations allow hyperactivation of the yeast GAL1 gene in vivo. EMBO J. 1992 Sep;11(9):3297–3306. [PMC free article] [PubMed] [Google Scholar]
• Miller SA, Dykes DD, Polesky HF. A simple salting out procedure for extracting DNA from human nucleated cells. Nucleic Acids Res. 1988 Feb 11;16(3):1215–1215. [PMC free article] [PubMed] [Google Scholar]
• Loc PV, Strätling WH. The matrix attachment regions of the chicken lysozyme gene co-map with the boundaries of the chromatin domain. EMBO J. 1988 Mar;7(3):655–664. [PMC free article] [PubMed] [Google Scholar]
• Reitman M, Felsenfeld G. Developmental regulation of topoisomerase II sites and DNase I-hypersensitive sites in the chicken beta-globin locus. Mol Cell Biol. 1990 Jun;10(6):2774–2786. [PMC free article] [PubMed] [Google Scholar]
• Stalder J, Larsen A, Engel JD, Dolan M, Groudine M, Weintraub H. Tissue-specific DNA cleavages in the globin chromatin domain introduced by DNAase I. Cell. 1980 Jun;20(2):451–460. [PubMed] [Google Scholar]
• Strätling WH, Dölle A, Sippel AE. Chromatin structure of the chicken lysozyme gene domain as determined by chromatin fractionation and micrococcal nuclease digestion. Biochemistry. 1986 Jan 28;25(2):495–502. [PubMed] [Google Scholar]
• Tazi J, Bird A. Alternative chromatin structure at CpG islands. Cell. 1990 Mar 23;60(6):909–920. [PubMed] [Google Scholar]
• Turner BM. Histone acetylation and control of gene expression. J Cell Sci. 1991 May;99(Pt 1):13–20. [PubMed] [Google Scholar]
• Turner BM, Birley AJ, Lavender J. Histone H4 isoforms acetylated at specific lysine residues define individual chromosomes and chromatin domains in Drosophila polytene nuclei. Cell. 1992 Apr 17;69(2):375–384. [PubMed] [Google Scholar]
• Villeponteau B, Landes GM, Pankratz MJ, Martinson HG. The chicken beta globin gene region. Delineation of transcription units and developmental regulation of interspersed DNA repeats. J Biol Chem. 1982 Sep 25;257(18):11015–11023. [PubMed] [Google Scholar]
• Weintraub H, Groudine M. Chromosomal subunits in active genes have an altered conformation. Science. 1976 Sep 3;193(4256):848–856. [PubMed] [Google Scholar]
• Wood WI, Felsenfeld G. Chromatin structure of the chicken beta-globin gene region. Sensitivity to DNase I, micrococcal nuclease, and DNase II. J Biol Chem. 1982 Jul 10;257(13):7730–7736. [PubMed] [Google Scholar]

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