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, 86 (18), 6930-4

A CACGTG Motif of the Antirrhinum Majus Chalcone Synthase Promoter Is Recognized by an Evolutionarily Conserved Nuclear Protein

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A CACGTG Motif of the Antirrhinum Majus Chalcone Synthase Promoter Is Recognized by an Evolutionarily Conserved Nuclear Protein

D Staiger et al. Proc Natl Acad Sci U S A.

Abstract

In the chalcone synthase gene of Antirrhinum majus (snapdragon), 150 base pairs of the 5' flanking region contain cis-acting signals for UV light-induced expression. A nuclear factor, designated CG-1, specifically recognizes a hexameric motif with internal dyad symmetry, CACGTG, located within this light-responsive sequence. Binding of CG-1 is influenced by C-methylation of the CpG dinucleotide in the recognition sequence. CG-1 is a factor found in a variety of dicotyledonous plant species including Nicotiana tabacum, A. majus, Petunia hybrida, Arabidopsis thaliana, and Glycine max. CACGTG motifs contained within trans-acting factor recognition sites in various other plant promoters can interact with CG-1. In addition, the binding site of the human adenovirus major late transcription factor USF can compete for CG-1 binding to the chalcone synthase promoter. This suggests an evolutionary conservation of trans-acting factor recognition sites involved in divergent mechanisms of gene control.

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