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Binding of a pea nuclear protein to promoters of certain photoregulated genes is modulated by phosphorylation.

Binding of a pea nuclear protein to promoters of certain photoregulated genes is modulated by... Abstract There have been numerous recent reports documenting phosphorylation of DNA-binding proteins [Montminy and Bilezikjian (1987); Sorger, Lewis, and Pelham (1987); Hoeffler, Kovelman, and Roeder (1988); Jones et al. (1988); Prywes et al. (1988); Sorger and Pelham (1988); Yamamoto et al. (1988)], and the transcriptional regulatory activity of at least one of these proteins appears to be modulated by this modification [Montminy and Bilezikjian (1987); Yamamoto et al. (1988)]. We report here on a plant nuclear protein, the DNA-binding activity of which is strongly affected by phosphorylation. This protein, AT-1, binds to specific AT-rich elements (the AT-1 box) within promoters of certain nuclear genes encoding the small subunit of ribulose-1,5-bisphosphate carboxylase and the polypeptide components of the light-harvesting chlorophyll a/b protein complex. A consensus sequence of AATATTTTTATT was derived for the AT-1 box. We demonstrate that the DNA-binding ability of AT-1, from nuclear extracts of pea, can be reversibly modulated by phosphorylation. AT-1 is active in the nonphosphorylated form and loses all DNA-binding ability as a result of phosphorylation. The kinase that phosphorylates AT-1 uses both Mg-ATP and Mg-GTP as a substrate and is inhibited by heparin and spermine, indicative of an NII-type casein kinase. This content is only available as a PDF. © 1989 by American Society of Plant Biologists This article is published and distributed under the terms of the Oxford University Press, Standard Journals Publication Model (https://academic.oup.com/journals/pages/open_access/funder_policies/chorus/standard_publication_model) http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png The Plant Cell Oxford University Press

Binding of a pea nuclear protein to promoters of certain photoregulated genes is modulated by phosphorylation.

Datta, N; Cashmore, A R
The Plant Cell , Volume 1 (11) – Nov 1, 1989
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References (26)

Publisher
Oxford University Press
Copyright
Copyright © 2021 American Society of Plant Biologists
ISSN
1040-4651
eISSN
1532-298X
DOI
10.1105/tpc.1.11.1069
Publisher site
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Abstract

Abstract There have been numerous recent reports documenting phosphorylation of DNA-binding proteins [Montminy and Bilezikjian (1987); Sorger, Lewis, and Pelham (1987); Hoeffler, Kovelman, and Roeder (1988); Jones et al. (1988); Prywes et al. (1988); Sorger and Pelham (1988); Yamamoto et al. (1988)], and the transcriptional regulatory activity of at least one of these proteins appears to be modulated by this modification [Montminy and Bilezikjian (1987); Yamamoto et al. (1988)]. We report here on a plant nuclear protein, the DNA-binding activity of which is strongly affected by phosphorylation. This protein, AT-1, binds to specific AT-rich elements (the AT-1 box) within promoters of certain nuclear genes encoding the small subunit of ribulose-1,5-bisphosphate carboxylase and the polypeptide components of the light-harvesting chlorophyll a/b protein complex. A consensus sequence of AATATTTTTATT was derived for the AT-1 box. We demonstrate that the DNA-binding ability of AT-1, from nuclear extracts of pea, can be reversibly modulated by phosphorylation. AT-1 is active in the nonphosphorylated form and loses all DNA-binding ability as a result of phosphorylation. The kinase that phosphorylates AT-1 uses both Mg-ATP and Mg-GTP as a substrate and is inhibited by heparin and spermine, indicative of an NII-type casein kinase. This content is only available as a PDF. © 1989 by American Society of Plant Biologists This article is published and distributed under the terms of the Oxford University Press, Standard Journals Publication Model (https://academic.oup.com/journals/pages/open_access/funder_policies/chorus/standard_publication_model)

Journal

The Plant Cell – Oxford University Press

Published: Nov 1, 1989

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