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J. Biol. Chem., Vol. 279, Issue 45, 47233-47241, November 5, 2004

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The Minimal Transactivation Domain of the Basic Motif-Leucine Zipper Transcription Factor NRL Interacts with TATA-binding Protein^*

From the Departments of ^aOphthalmology and Visual Sciences, ^fNeuroscience, and ⁱHuman Genetics, W. K. Kellogg Eye Center, University of Michigan, Ann Arbor, Michigan 48105, the ^eLaboratoire de Physiopathologie Cellulaire et Moléculaire de la Rétine, INSERM U.592, Clinique Médicale A, Centre Hospitalier Universitaire Régional, 67091 Strasbourg, France, and ^hSBI Science, Ann Arbor, Michigan 48103

The basic motif-leucine zipper (bZIP) transcription factor NRL controls the expression of rhodopsin and other phototransduction genes and is a key mediator of photoreceptor differentiation. To delineate the molecular mechanisms underlying transcriptional initiation of rod-specific genes, we characterized different regions of the NRL protein using yeast-based autoactivation assays. We identified 35 amino acid residues in the proline- and serine-rich N-terminal region (called minimal transactivation domain, MTD), which, when combined with LexA or Gal4 DNA binding domains, exhibited activation of target promoters. Because this domain is conserved in all proteins of the large Maf family, we hypothesized that NRL-MTD played an important role in assembling the transcription initiation complex. Our studies showed that the NRL protein, including the MTD, interacted with full-length or the C-terminal domain of TATA-binding protein (TBP) in vitro. NRL and TBP could be co-immunoprecipitated from bovine retinal nuclear extract. TBP was also part of c-Maf and MafA (two other large Maf proteins)-containing complex(es) in vivo. Our data suggest that the function of NRL-MTD is to activate transcription by recruiting or stabilizing TBP (and consequently other components of the general transcription complex) at the promoter of target genes, and a similar function may be attributed to other bZIP proteins of the large Maf family.

Received for publication, July 22, 2004 , and in revised form, August 23, 2004.

^* This work was supported in part by grants from the National Institutes of Health (Grants EY11115 and EY07003), The Foundation Fighting Blindness (FFB), and Research to Prevent Blindness (RPB). The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

^b Both authors contributed equally to this work.

^c Recipient of an FFB-Canada post-doctoral fellowship.

^d Current address: National Brain Research Center, Gurgaon, India.

^g Current address: Oakland University Eye Research Institute, Rochester, MI.

^j To whom correspondence should be addressed: Dept. of Ophthalmology and Visual Sciences, W. K. Kellogg Eye Center, University of Michigan, 1000 Wall St., Ann Arbor, MI 48105. Tel.: 734-763-3731; Fax: 734-647-0228; E-mail: swaroop{at}umich.edu.

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