Nucleic Acids Research, 1989, Vol. 17, No. 9 3563-3582
© 1989
MOLECULAR BIOLOGY |
Multiple regulatory elements of the murine
2-crystallin promoter
1Department of Genetics, Research Institute, The Hospital for Sick Children 555 University Avenue, Toronto, Ontario M5G 1X8 2Department of Medical Genetics, University of Toronto Toronto, Ontario M5S 1A8 3Division of Cancer and Cell Biology, Mount Sinai Hospital Toronto, Ontario M5G 1X5, Canada
*To whom correspondence should be addresse
Received November 16, 1988. Revised March 31, 1989. Accepted March 31, 1989.
Crystallins are the major water-soluble proteins of the vertebrate eye lens. These lens-specific proteins are encoded by several multi-gene families whose expression is differentially regulated during development. Our previous studies showed that the mouse
2-crystallin promoter is active on transfection into lens-explant cultures derived from 14-day-old chick embryos but not on transfection into a variety of non-lens cells. In this study, transient expression data show that a sequence of 226 nucleotides upstream from the transcription start site is sufficient for activity of this promoter in the chicken lens cells. This sequence can be further divided into two domains, A and B, both of which are required for promoter function. Domain A (nucleotide 68 to 18) contains the TATA box and sequence motifs that are conserved in all
-crystallin promoters. Domain B (226 to 120) consists of three regions. One of these regions contains an element with dyad symmetry and a sequence similar to the octamer motif. The second region contains an enhancer core consensus sequence. Two "enhancer-like" activities have been detected, one in Domain B and a second in a more distal region (392 to 278) that does not appear to be required for promoter activity in transfection assays.
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