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Nucleic Acids Research 2006 34(6):1798-1806; doi:10.1093/nar/gkl101
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Published online 31 March 2006

© The Author 2006. Published by Oxford University Press. All rights reserved
The online version of this article has been published under an open access model. Users are entitled to use, reproduce, disseminate, or display the open access version of this article for non-commercial purposes provided that: the original authorship is properly and fully attributed; the Journal and Oxford University Press are attributed as the original place of publication with the correct citation details given; if an article is subsequently reproduced or disseminated not in its entirety but only in part or as a derivative work this must be clearly indicated. For commercial re-use, please contact journals.permissions@oxfordjournals.org

Article

Acetylation of UBF changes during the cell cycle and regulates the interaction of UBF with RNA polymerase I

Joachim Meraner, Markus Lechner, Adele Loidl, Maria Goralik-Schramel, Renate Voit1, Ingrid Grummt1 and Peter Loidl*

Division of Molecular Biology, Biocenter, Innsbruck Medical University A-6020 Innsbruck, Austria 1 Division of Molecular Biology of the Cell II, German Cancer Research Center D-69120 Heidelberg, Germany

*To whom correspondence should be addressed. +43 512 507 3600; Fax: +43 512 507 9880; Email: Peter.Loidl{at}i-med.ac.at

Received December 19, 2005. Revised January 16, 2006. Accepted March 8, 2006.

The upstream binding factor UBF, an activator of RNA polymerase I transcription, is posttranslationally modified by phosphorylation and acetylation. We found that in NIH3T3 cells, UBF is acetylated in S-phase but not in G1-phase. To assess the role of acetylation in regulation of UBF activity, we have established an NIH3T3 cell line that inducibly overexpresses HDAC1. Both in vivo and in vitro, HDAC1 efficiently hypoacetylates UBF. Immunoprecipitation with antibodies against the Pol I-associated factor PAF53 co-precipitated UBF in mock cells but not in cells overexpressing HDAC1. Pull-down experiments showed that acetylation of UBF augments the interaction with Pol I. Consistent with acetylation of UBF being important for association of PAF53 and recruitment of Pol I, the level of Pol I associated with rDNA and pre-rRNA synthesis were reduced in cells overexpressing HDAC1. The results suggest that acetylation and deacetylation of UBF regulate rRNA synthesis during cell cycle progression.

The authors wish it to be known that, in their opinion, the first two authors should be regarded as joint First Authors


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