Skip Navigation

Nucleic Acids Research 2006 34(11):3288-3298; doi:10.1093/nar/gkl401
This Article
Right arrow Full Text Freely available
Right arrow Print PDF (2507K) Freely available
Right arrow Screen PDF (2517K) Freely available
Right arrow Supplementary Material
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in ISI Web of Science
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Add to My Personal Archive
Right arrow Download to citation manager
Right arrow Search for citing articles in:
ISI Web of Science (4)
Right arrow Commercial Re-use Guidelines
for Open Access NAR Content
Google Scholar
Right arrow Articles by Viiri, K. M.
Right arrow Articles by Lohi, O.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Viiri, K. M.
Right arrow Articles by Lohi, O.
Social Bookmarking
Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

Published online 4 July 2006

© 2006 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-commerical use, distribution, and reproduction in any medium, provided the original work is properly cited.

Article

SAP30L interacts with members of the Sin3A corepressor complex and targets Sin3A to the nucleolus

K. M. Viiri1, H. Korkeamäki1, M. K. Kukkonen1, L. K. Nieminen1, K. Lindfors1, P. Peterson2, M. Mäki1, H. Kainulainen3,4 and O. Lohi1,*

1 Paediatric Research Centre, University of Tampere Medical School and Tampere University Hospital Tampere, Finland 2 Molecular Pathology, University of Tartu Tartu, Estonia 3 Institute of Medical Technology and Tampere University Hospital Tampere, Finland 4 Department of Biology of Physical Activity, University of Jyväskylä Finland

To whom correspondence should be addressed. Tel: +358 3 355 184 05; Fax: +358 3 355 184 02; Email: olli.lohi{at}uta.fi

Received January 19, 2006. Revised March 24, 2006. Accepted May 11, 2006.

Histone acetylation plays a key role in the regulation of gene expression. The chromatin structure and accessibility of genes to transcription factors is regulated by enzymes that acetylate and deacetylate histones. The Sin3A corepressor complex recruits histone deacetylases and in many cases represses transcription. Here, we report that SAP30L, a close homolog of Sin3-associated protein 30 (SAP30), interacts with several components of the Sin3A corepressor complex. We show that it binds to the PAH3/HID (Paired Amphipathic Helix 3/Histone deacetylase Interacting Domain) region of mouse Sin3A with residues 120–140 in the C-terminal part of the protein. We provide evidence that SAP30L induces transcriptional repression, possibly via recruitment of Sin3A and histone deacetylases. Finally, we characterize a functional nucleolar localization signal in SAP30L and show that SAP30L and SAP30 are able to target Sin3A to the nucleolus.


Add to CiteULike CiteULike   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us    What's this?


This article has been cited by other articles:


Home page
 Genes Dev.Home page
L. A. Puto and J. C. Reed
Daxx represses RelB target promoters via DNA methyltransferase recruitment and DNA hypermethylation
Genes & Dev., April 15, 2008; 22(8): 998 - 1010.
[Abstract] [Full Text] [PDF]


Disclaimer:
Please note that abstracts for content published before 1996 were created through digital scanning and may therefore not exactly replicate the text of the original print issues. All efforts have been made to ensure accuracy, but the Publisher will not be held responsible for any remaining inaccuracies. If you require any further clarification, please contact our Customer Services Department.