Staiger D et al. 1991
- Authors:
Staiger D. Becker F. Schell J. Koncz C. Palme K.
- Title:
Purification of tobacco nuclear proteins binding to a CACGTG motif of the
chalcone synthase promoter by DNA affinity chromatography.
- Reference location:
European Journal of Biochemistry. 199(3):519-27, 1991 Aug 1.
- Abstract:
The activity of various light-regulated and developmentally regulated
plant gene promoters critically depends upon the presence of a conserved
sequence with a central CACGTG motif. Using band-shift assays, we have
identified nuclear factor(s) from Nicotiana tabacum, termed CG-1, that
specifically recognize(s) this transcriptional element in the
ultraviolet-light-regulated Antirrhinum majus chalcone synthase promoter.
CG-1 activity is constitutively expressed in tobacco seedlings grown in
the absence of ultraviolet light as well as in seedlings induced for
chalcone synthase gene expression by ultraviolet light irradiation. CG-1
activity has also been detected in flower tissue. DNA-protein
cross-linking studies identified three polypeptides with apparent
molecular masses of 20, 32 and 42 kDa binding to the CACGTG motif.
Proteins interacting with the CACGTG motif were purified from N. tabacum
seedlings using differential sequence-specific DNA affinity chromatography
employing wild-type and mutated CG-1-binding sites. Denaturing
polyacrylamide gel electrophoresis revealed major polypeptides of
approximately 20, 30 and 40 kDa which are highly enriched in the
affinity-purified fractions binding specifically to the CACGTG motif.
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