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Nucleic Acids Research Advance Access published online on August 24, 2007
Nucleic Acids Research, doi:10.1093/nar/gkm620
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© 2007 The Author(s)
This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/2.0/uk/) which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.

Molecular Biology

Nucleosome and transcription activator antagonism at human ß-globin locus control region DNase I hypersensitive sites

AeRi Kim1,*, Sang-hyun Song3, Marjorie Brand2 and Ann Dean3

1Department of Molecular Biology, College of Natural Sciences, Pusan National University, Pusan 609-735, Korea, 2Sprott Center for Stem Cell Research, Ottawa Health Research Institute, Ottawa, ON K1H 8LC, Canada and 3Laboratory of Cellular and Developmental Biology, NIDDK, NIH, Bethesda, MD 20892, USA

*To whom correspondence should be addressed. Tel: +82 51 510 3683; Fax: +82 51 513 9258; Email: kimaeri{at}pusan.ac.kr

Received April 21, 2007. Revised July 7, 2007. Accepted July 30, 2007.

Locus control regions are regulatory elements that activate distant genes and typically consist of several DNase I hypersensitive sites coincident with clusters of transcription activator binding sites. To what extent nucleosomes and activators occupy these sites together or exclusively has not been extensively studied in vivo. We analyzed the chromatin structure of human ß-globin locus control region hypersensitive sites in erythroid cells expressing embryonic and fetal globin genes. Nucleosomes were variably depleted at hypersensitive sites HS1-HS4 and at HS5 which flanks the 5' of the locus. In lieu of nucleosomes, activators were differentially associated with these sites. Erythroid–specific GATA-1 resided at HS1, HS2 and HS4 but the NF-E2 hetero-dimer was limited to HS2 where nucleosomes were most severely depleted. Histones H3 and H4 were hyperacetylated and H3 was di-methylated at K4 across the LCR, however, the H3 K4 MLL methyltransferase component Ash2L and histone acetyltransferases CBP and p300 occupied essentially only HS2 and the NF-E2 motif in HS2 was required for Ash2L recruitment. Our results indicate that each hypersensitive site in the human ß-globin LCR has distinct structural features and suggest that HS2 plays a pivotal role in LCR organization at embryonic and fetal stages of globin gene expression.


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