Home LiteratureArticle Details
PMID: 9211915 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S.

In vitro chromatin assembly of the HIV-1 promoter. ATP-dependent polar repositioning of nucleosomes by Sp1 and NFkappaB.

The Journal of biological chemistry ·Vol. 272 ·No. 28 ·1997-07-11 ·Pages 17654-61

Widlak P, Gaynor RB, Garrard WT

Abstract

Nuclease hypersensitive sites exist in vivo in the chromatin of the integrated human immunodeficiency virus (HIV)-1 proviral genome, in the 5'-long terminal repeat (LTR) within the promoter/enhancer region near Sp1 and NFkappaB binding sites. Previous studies from the Kadonaga and Jones laboratories have shown that Sp1 and NFkappaB can establish hypersensitive sites in a truncated form of this LTR when added before in vitro chromatin assembly with Drosophila extracts, thus facilitating subsequent transcriptional activation of a linked reporter gene upon the association of additional factors (Pazin, M. J., Sheridan, P. L., Cannon, K., Cao, Z., Keck, J. G., Kadanaga, J. T., and Jones, K. A. (1996) Genes & Dev. 10, 37-49). Here we assess the role of a full-length LTR and 1 kilobase pair of downstream flanking HIV sequences in chromatin remodeling when these transcription factors are added after chromatin assembly. Using Xenopus laevis oocyte extracts to assemble chromatin in vitro, we have confirmed that Sp1 and NFkappaB can indeed induce sites hypersensitive to DNase I, micrococcal nuclease, or restriction enzymes on either side of factor binding sites in chromatin but not naked DNA. We extend these earlier studies by demonstrating that the process is ATP-dependent when the factors are added after chromatin assembly and that histone H1, AP1, TBP, or Tat had no effect on hypersensitive site formation. Furthermore, we have found that nucleosomes upstream of NFkappaB sites are rotationally positioned prior to factor binding and that their translational frame is registered after binding NFkappaB. On the other hand, binding of Sp1 positions adjacent downstream nucleosome(s). We term this polar repositioning because each factor aligns nucleosomes only on one side of its binding sites. Mutational analysis and oligonucleotide competition each demonstrated that this remodeling required Sp1 and NFkappaB binding sites.

MeSH Terms
Adenosine Triphosphate/metabolism Animals Base Sequence Binding Sites Cell Polarity Chromatin/metabolism,virology DNA/metabolism DNA Footprinting DNA, Superhelical/metabolism HIV Long Terminal Repeat/genetics In Vitro Techniques Micrococcal Nuclease/metabolism Models, Molecular Molecular Sequence Data NF-kappa B/metabolism Nucleosomes/metabolism Oocytes/metabolism Sp1 Transcription Factor/metabolism Xenopus laevis
Chemicals
Chromatin DNA, Superhelical NF-kappa B Nucleosomes Sp1 Transcription Factor Adenosine Triphosphate DNA Micrococcal Nuclease
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Widlak P
Department of Molecular Biology and Oncology, University of Texas Southwestern Medical Center, Dallas, Texas 75235-9140, USA.
Gaynor R B
Garrard W T
Article Info
Journal
The Journal of biological chemistry
Abbr.
J Biol Chem
ISSN
0021-9258
Published
1997-07-11
Pages
17654-61
Language
English
Region
United States
NLM ID
2985121R
Subset
IM
Grants
NIAID NIH HHS · AI25288 · United States
Analysis Services
Analysis Services

Contact

No. 2 Wenbo Road, Zhangqiu District, Jinan, Shandong

Qilu Normal University · Genelibs Bioinformatics Lab

750 Shunhua Rd, Jinan

2F, Bldg F, University Science Park

Tel: 0531-88819269

WeChat Official Account

Follow our WeChat subscription account for real-time updates and the latest in medical and biological research.


Business Email

E-mail: [email protected]