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The RNA-binding protein FCA is an abscisic acid receptor

A Retraction to this article was published on 11 December 2008

Abstract

The phytohormone abscisic acid (ABA) regulates various physiological processes in plants. The molecular mechanisms by which this is achieved are not fully understood. Genetic approaches have characterized several downstream components of ABA signalling, but a receptor for ABA has remained elusive. Although studies indicate that several ABA response genes encode RNA-binding or RNA-processing proteins, none has been found to be functional in binding ABA. Here we show that FCA, an RNA-binding protein involved in flowering, binds ABA with high affinity in an interaction that is stereospecific and follows receptor kinetics. The interaction between FCA and ABA has molecular effects on downstream events in the autonomous floral pathway and, consequently, on the ability of the plant to undergo transition to flowering. We further show that ABA binding exerts a direct control on the FCA-mediated processing of precursor messenger RNA. Our results indicate that FCA is an ABA receptor involved in RNA metabolism and in controlling flowering time.

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Figure 1: Binding of [ 3 H](+ )-ABA to purified recombinant FCA protein.
Figure 2: ABA affects FCA–FY interaction.
Figure 3: ABA affects FCA autoregulation.
Figure 4: ABA affects flowering.
Figure 5: FCA is involved in a distinct ABA response.

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Acknowledgements

We thank C. Dean and G. Simpson for clones and advice; M. Galka for an ABA affinity column; and K. Baron for help with microscopy. The financial support of the Natural Sciences and Engineering Council of Canada (to R.D.H.) and Genome Canada (to R.D.H. and S.R.A.) is gratefully acknowledged.

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Correspondence to Robert D. Hill.

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Reprints and permissions information is available at npg.nature.com/reprintsandpermissions. The authors declare no competing financial interests.

Supplementary information

Supplementary Figure 1.

Binding of 3H-(+)-ABA to purified recombinant FCA protein. (PDF 10 kb)

Supplementary Figure 2.

FCA protein purified on biotin-tagged (+)-ABA column. (PDF 53 kb)

Supplementary Figure 3.

ABA binding disrupts FCA/FY interaction. (PDF 7 kb)

Supplementary Figure 4.

ABA affects FCA autoregulation. (PDF 15 kb)

Supplementary Figure 5.

ABA delays flowering. (PDF 29 kb)

Supplementary Figure Legends

Text to accompany the above Supplementary Figures. (DOC 46 kb)

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Razem, F., El-Kereamy, A., Abrams, S. et al. The RNA-binding protein FCA is an abscisic acid receptor. Nature 439, 290–294 (2006). https://doi.org/10.1038/nature04373

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  • DOI: https://doi.org/10.1038/nature04373

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