Skip Navigation


Nucleic Acids Research Advance Access originally published online on August 12, 2006
Nucleic Acids Research 2006 34(14):3929-3937; doi:10.1093/nar/gkl537
This Article
Right arrow Full Text Freely available
Right arrow Print PDF (745K) Freely available
Right arrow Screen PDF (304K) Freely available
Right arrowOA All Versions of this Article:
34/14/3929    most recent
gkl537v1
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 (5)
Right arrow Commercial Re-use Guidelines
for Open Access NAR Content
Google Scholar
Right arrow Articles by Le Guezennec, X.
Right arrow Articles by Stunnenberg, H. G.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Le Guezennec, X.
Right arrow Articles by Stunnenberg, H. G.
Social Bookmarking
Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

Nucleic Acids Research, 2006, Vol. 34, No. 14 3929-3937
© 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-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.

Molecular Biology

Molecular characterization of Sin3 PAH-domain interactor specificity and identification of PAH partners

Xavier Le Guezennec, Michiel Vermeulen and Hendrik G. Stunnenberg*

Department of Molecular Biology, NCMLS, Radboud University Nijmegen PO Box 9101, 6500 HB Nijmegen, The Netherlands

*To whom correspondence should be addressed. Tel: +31 3610524; Fax: +31 3610520; Email: h.stunnenberg{at}ncmls.ru.nl

Received December 21, 2005. Revised June 19, 2006. Accepted July 13, 2006.

Sin3 is the central component of a multisubunit co-repressor complex. A number of DNA-binding proteins are targeted by the Sin3 complex to chromatin through association with its paired amphipathic helix (PAH) domains. Here, we performed a yeast two-hybrid screening using a peptide aptamer library and identified peptides that interact with either PAH1 or PAH2. Analysis of PAH2 interacting peptides uncovered motifs similar to previously characterized PAH2 interacting proteins, Mad, Ume6 and kruppel-like members, while analysis of PAH1 interacting peptides revealed an LXXLL motif. In addition, a tandem affinity purification (TAP)-tagging approach of Sin3b resulted in the isolation of known and novel interactors amongst which neural retina leucine (NRL) zipper. Strikingly, one of the identified PAH2 interacting peptide showed strong resemblance to the NRL region amino acids 125–150. Direct association between PAH2 and NRL was shown and NRL(125–150) mediated transcriptional repression in reporter assays. Finally, we reveal that PAH1 and PAH2 amino acids 7, 14 and 39 shown previously to be important for Mad–PAH2 interaction, also play an important role in the specificity of interaction between PAH1, PAH2 and identified aptamers. Our results provide novel insights into the molecular determinant of the specificity of PAH1 and PAH2 for their interacting partners.


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
 J. Biol. Chem.Home page
D. R. Hurst, Y. Xie, K. S. Vaidya, A. Mehta, B. P. Moore, M. A. Accavitti-Loper, R. S. Samant, R. Saxena, A. C. Silveira, and D. R. Welch
Alterations of BRMS1-ARID4A Interaction Modify Gene Expression but Still Suppress Metastasis in Human Breast Cancer Cells
J. Biol. Chem., March 21, 2008; 283(12): 7438 - 7444.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
L. Y. Zhao, A. Santiago, J. Liu, and D. Liao
Repression of p53-mediated Transcription by Adenovirus E1B 55-kDa Does Not Require Corepressor mSin3A and Histone Deacetylases
J. Biol. Chem., March 9, 2007; 282(10): 7001 - 7010.
[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.