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Molecular and Cellular Biology, May 2007, p. 3557-3568, Vol. 27, No. 10
0270-7306/07/$08.00+0     doi:10.1128/MCB.01106-06
Copyright © 2007, American Society for Microbiology. All Rights Reserved.

The Nucleosome Assembly Activity of NAP1 Is Enhanced by Alien{triangledown}

Maren Eckey,1,{dagger} Wei Hong,1,2 Maria Papaioannou,1 and Aria Baniahmad1,2*

Institute of Human Genetics and Anthropology, Friedrich Schiller University, 07740 Jena, Germany,1 Institute for Biochemistry, University of Kuopio, Kuopio, Finland2

Received 20 June 2006/ Returned for modification 28 July 2006/ Accepted 19 February 2007

The assembly of nucleosomes into chromatin is essential for the compaction of DNA and inactivation of the DNA template to modulate and repress gene expression. The nucleosome assembly protein 1, NAP1, assembles nucleosomes independent of DNA synthesis and was shown to enhance coactivator-mediated gene expression, suggesting a role for NAP1 in transcriptional regulation. Here, we show that Alien, known to harbor characteristics of a corepressor of nuclear hormone receptors such as of the vitamin D receptor (VDR), binds in vivo and in vitro to NAP1 and modulates its activity by enhancing NAP1-mediated nucleosome assembly on DNA. Furthermore, Alien reduces the accessibility of the histones H3 and H4 for NAP1-promoted assembly reaction. This indicates that Alien sustains and reinforces the formation of nucleosomes. Employing deletion mutants of Alien suggests that different regions of Alien are involved in enhancement of NAP1-mediated nucleosome assembly and in inhibiting the accessibility of the histones H3 and H4. In addition, we provide evidence that Alien is associated with chromatin and with micrococcus nuclease-prepared nucleosome fractions and interacts with the histones H3 and H4. Furthermore, chromatin immunoprecipitation and reimmunoprecipitation experiments suggest that NAP1 and Alien localize to the endogenous CYP24 promoter in vivo, a VDR target gene. Based on these findings, we present here a novel pathway linking corepressor function with nucleosome assembly activity.

* Corresponding author. Mailing address: Institute of Human Genetics and Anthropology, Friedrich Schiller University, 07740 Jena, Germany. Phone: 49 3641 935524. Fax: 49 3641 934706. E-mail: aban{at}mti.uni-jena.de

{triangledown} Published ahead of print on 5 March 2007.

{dagger} Present address: Adolf Butenandt Institut, Ludwig Maximilians University, 80336 Munich, Germany.

Molecular and Cellular Biology, May 2007, p. 3557-3568, Vol. 27, No. 10
0270-7306/07/$08.00+0     doi:10.1128/MCB.01106-06
Copyright © 2007, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • Tachiwana, H., Osakabe, A., Kimura, H., Kurumizaka, H. (2008). Nucleosome formation with the testis-specific histone H3 variant, H3t, by human nucleosome assembly proteins in vitro. Nucleic Acids Res 36: 2208-2218 [Abstract] [Full Text]  


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