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J Biol Chem, Vol. 274, Issue 28, 19973-19978, July 9, 1999

Regulation of A-crystallin Gene Expression
LENS SPECIFICITY ACHIEVED THROUGH THE DIFFERENTIAL PLACEMENT OF SIMILAR TRANSCRIPTIONAL CONTROL ELEMENTS IN MOUSE AND CHICKEN

From the Laboratory of Molecular and Developmental Biology, National Eye Institute, National Institutes of Health, Bethesda, Maryland 20892-2730

The lens-preferred mouse A-crystallin gene contains a conserved stretch (proximal element 2, +24/+43) in its 5'-noncoding region that we have previously shown binds nuclear proteins of lens and non-lens cells. The 5'-half of this sequence (PE2A, +25/+32) has consensus binding sites for AP-1 and other transcription factors. We show here by deletion experiments that PE2A is important for activity of the mouse A-crystallin promoter and mediates phorbol ester and c-Jun responsiveness of this promoter in transfected lens cells. In vitro protein binding studies suggest that AP-1 complexes are capable of binding to PE2A. Our findings suggest that PE2A plays a role in mouse A-crystallin gene expression through AP-1-mediated regulatory mechanisms. We propose that the mouse and chicken A-crystallin genes are expressed with lens specificity using a similar assortment of transcription factors but with a different physical arrangement of their respective cis-elements within the promoter region. A fundamental role for AP-1 in lens-preferred expression of crystallin genes is consistent with the idea that a redox-sensitive mechanism is a selective force for recruiting lens crystallins.

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