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Nucleic Acids Research 2005 33(11):3465-3478; doi:10.1093/nar/gki653
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Published online 21 June 2005

© The Author 2005. 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{at}oupjournals.org

Article

The 5'-AT-rich half-site of Maf recognition element: a functional target for bZIP transcription factor Maf

Tomonori Yoshida1,2,*, Tsuyoshi Ohkumo1,3, Shoko Ishibashi1,4 and Kunio Yasuda1

1Graduate School of Biological Sciences, Nara Institute of Science and Technology Takayama 8916-5, Ikoma, Nara, 630-0101, Japan 2Regulatory Biology Laboratory, The Salk Institute for Biological Studies La Jolla, CA 92037, USA 3Graduate School of Frontier Biosciences, Osaka University Suita, Osaka, 565-0871, Japan 4Wellcome Trust/Cancer Research UK Gurdon Institute, University of Cambridge Tennis Court Road, Cambridge CB2 1QN, UK

*To whom correspondence should be addressed. Tel: +1 858 453 4100, ext. 1851; Fax: +1 858 535 8194; Email: yoshida{at}salk.edu

Received March 15, 2005. Accepted May 23, 2005.

The Maf family of proteins are a subgroup of basic region-leucine zipper (bZIP) transcription factors, which recognize a long palindromic DNA sequence [TGCTGAC(G)TCAGCA] known as the Maf recognition element (MARE). Interestingly, the functional target enhancer sequences present in the {alpha}A-crystallin gene contain a well-conserved half-site of MARE rather than the entire palindromic sequence. To resolve how Maf proteins bind to target sequences containing only MARE half-sites, we examined their binding activities using electrophoretic gel mobility shift assays as well as in vitro and in vivo reporter assays. Our results indicate that the 5'-flanking region of the MARE half-site is required for Maf proteins to bind both in vitro and in vivo. The critical 5'-flanking sequences for c-Maf were determined by a selection and amplification binding assay and show a preference for AT-rich nucleotides. Furthermore, sequence analysis of the regulatory regions of several target genes also suggests that AT-rich sequences are important. We conclude that Maf can bind to at least two types of target sequences, the classical MARE (palindrome type) and a 5'-AT-rich MARE half-site (half-site type). Our results provide important new insights into the DNA binding and site selection by bZIP transcription factors.


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