JBC Transcription and Nuclear Factor Monoclonals

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Papers In Press, published online ahead of print April 9, 2002
J. Biol. Chem, 10.1074/jbc.M201407200
Submitted on February 11, 2002
Revised on April 9, 2002
Accepted on April 9, 2002

The rod cGMP-phosphodiesterase beta -subunit promoter is a specific target for Sp4 and is not activated by other Sp proteins or CRX

Leonid E. Lerner, Yekaterina E. Gribanova, Leigh Whitaker, Barry E. Knox, and Debora B. Farber

Department of Opthhalmology, University of California at Los Angeles, Los Angeles, CA 90095-7000

Corresponding Author: farber{at}jsei.ucla.edu

The beta -subunit of cGMP-phosphodiesterase (beta -PDE) is a key protein in phototransduction expressed exclusively in rod photoreceptors. It is necessary for visual function and for structural integrity of the retina. beta -PDE promoter deletions showed that the -45/-23 region containing a consensus Crx response element (CRE) was necessary for low-level transcriptional activity. Overexpressed Crx modestly transactivated this promoter in 293 human embryonic kidney cells, however, mutation of CRE had no significant effect on transcription either in transfected Y79 retinoblastoma cells or Xenopus embryonic heads. Thus, Crx is unlikely to be a critical beta -PDE transcriptional regulator in vivo. Interestingly, although the beta /GC element (-59/-49) binds multiple Sp transcription factors in vitro, only Sp4, but not Sp1 or Sp3, significantly enhanced beta -PDE promoter activity. Thus, the Sp4-mediated differential activation of the beta -PDE transcription defines the first specific Sp4 target gene reported to date and implies the importance of Sp4 for retinal function. Further extensive mutagenesis of the beta -PDE upstream sequences showed no additional regulatory elements. Although this promoter lacks a canonical TATA box or Inr element, it has the T/A-rich beta /TA sequence located within the –45/-23 region. We found that it binds purified TBP and TFIIB in gel mobility shift assays with cooperative enhancement of binding affinity.


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