Abstract
The promoter of the murine γE-crystallin (γE-Cry) encoding gene (γ( E-cry) was analyzed for specific interactions with lenticular proteins in a gel-retardation assay. A 21-bp fragment immediately downstream of the transcription initiation site ( DOTIS) is demonstrated to be responsible for specific interactions with lens extracts. The DOTIS-binding protein (s) accept only the sense DNA strand as target; anti-sense or double-stranded DNA do not interact with these proteins. The DOTIS sequence element is highly conserved among the murine γD-, γE- and γ F-cry and is present at comparable positions in the orthologous rat genes. Only a weak or even no protein-binding activity is observed if a few particular bases are changed, as in the rat γA-, γC- and γE-cry elements. DOTIS-binding proteins were found in commercially available bovine α-Cry preparations. The essential participation of α-Cry in the DNA-binding protein complex was confirmed using α-Cry-specific monoclonal antibody. The results reported here point to a novel function of α-Cry besides the structural properties in the lens.
Published Version
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