A CACGTG motif of the Antirrhinum majus chalcone synthase promoter is recognized by an evolutionarily conserved nuclear protein

Staiger D, Kaulen H, Schell J (1989)
Proceedings of the National Academy of Sciences 86(18): 6930-6934.

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DOI
Autor*in
Staiger, DorotheeUniBi; Kaulen, Hildegard; Schell, Jeff
Einrichtung
Fakultät für Biologie > RNA Biologie und Molekulare Physiologie
Abstract / Bemerkung
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.
Erscheinungsjahr
1989
Zeitschriftentitel
Proceedings of the National Academy of Sciences
Band
86
Ausgabe
18
Seite(n)
6930-6934
ISSN
0027-8424
eISSN
1091-6490
Page URI
https://pub.uni-bielefeld.de/record/2439207

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Staiger D, Kaulen H, Schell J. A CACGTG motif of the Antirrhinum majus chalcone synthase promoter is recognized by an evolutionarily conserved nuclear protein. Proceedings of the National Academy of Sciences. 1989;86(18):6930-6934.
Staiger, D., Kaulen, H., & Schell, J. (1989). A CACGTG motif of the Antirrhinum majus chalcone synthase promoter is recognized by an evolutionarily conserved nuclear protein. Proceedings of the National Academy of Sciences, 86(18), 6930-6934. https://doi.org/10.1073/pnas.86.18.6930
Staiger, Dorothee, Kaulen, Hildegard, and Schell, Jeff. 1989. “A CACGTG motif of the Antirrhinum majus chalcone synthase promoter is recognized by an evolutionarily conserved nuclear protein”. Proceedings of the National Academy of Sciences 86 (18): 6930-6934.
Staiger, D., Kaulen, H., and Schell, J. (1989). A CACGTG motif of the Antirrhinum majus chalcone synthase promoter is recognized by an evolutionarily conserved nuclear protein. Proceedings of the National Academy of Sciences 86, 6930-6934.
Staiger, D., Kaulen, H., & Schell, J., 1989. A CACGTG motif of the Antirrhinum majus chalcone synthase promoter is recognized by an evolutionarily conserved nuclear protein. Proceedings of the National Academy of Sciences, 86(18), p 6930-6934.
D. Staiger, H. Kaulen, and J. Schell, “A CACGTG motif of the Antirrhinum majus chalcone synthase promoter is recognized by an evolutionarily conserved nuclear protein”, Proceedings of the National Academy of Sciences, vol. 86, 1989, pp. 6930-6934.
Staiger, D., Kaulen, H., Schell, J.: A CACGTG motif of the Antirrhinum majus chalcone synthase promoter is recognized by an evolutionarily conserved nuclear protein. Proceedings of the National Academy of Sciences. 86, 6930-6934 (1989).
Staiger, Dorothee, Kaulen, Hildegard, and Schell, Jeff. “A CACGTG motif of the Antirrhinum majus chalcone synthase promoter is recognized by an evolutionarily conserved nuclear protein”. Proceedings of the National Academy of Sciences 86.18 (1989): 6930-6934.

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http://www.pnas.org/content/86/18/6930.full.pdf+html
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Restricted Closed Access

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