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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

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Calmodulin isoforms differentially enhance the binding of cauliflower nuclear proteins and recombinant TGA3 to a region derived from the Arabidopsis Cam-3 promoter.

Many stimuli increase cytoplasmic Ca2+ concentrations as an early signal transduction event and alter the patterns of nuclear gene transcription, but the mechanisms by which Ca2+ signals are transduced to the nucleus are not known. This article shows that at least four DNA binding proteins from cauliflower nuclear extracts are also calmodulin ( CaM) binding proteins. CaM enhances the binding of these proteins to a C/G-box sequence element in the Arabidopsis Cam-3 promoter. Binding to the C/G-box is enhanced preferentially by the CaM isoform encoded by Cam-3. However, it is not clear whether the effect is mediated directly by CaM or indirectly through the activity of a CaM- regulated protein phosphatase. CaM also binds recombinant TGA3 and enhances its binding to the same Cam-3 promoter element. These results are consistent with the idea that a Ca(2+)-mediated signalling pathway eliciting some changes in gene expression may consist of CaM, or a structurally related Ca2+ binding protein, and transcription factors.[1]

References

  1. Calmodulin isoforms differentially enhance the binding of cauliflower nuclear proteins and recombinant TGA3 to a region derived from the Arabidopsis Cam-3 promoter. Szymanski, D.B., Liao, B., Zielinski, R.E. Plant Cell (1996) [Pubmed]
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