Post-translational modifications of the endogenous and transgenic FLC protein in Arabidopsis thaliana

Robertson, M; Helliwell, CA; Dennis, ES

Post-translational modifications of the endogenous and transgenic FLC protein in Arabidopsis thaliana

Robertson, M Helliwell, CA Dennis, ES

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Publication Type:: Journal Article
Citation:: Plant and Cell Physiology, 2008, 49 (12), pp. 1859 - 1866
Issue Date:: 2008-12-01

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Field	Value	Language
dc.contributor.author	Robertson, M	en_US
dc.contributor.author	Helliwell, CA	en_US
dc.contributor.author	Dennis, ES https://orcid.org/0000-0002-7850-591X	en_US
dc.date.issued	2008-12-01	en_US
dc.identifier.citation	Plant and Cell Physiology, 2008, 49 (12), pp. 1859 - 1866	en_US
dc.identifier.issn	0032-0781	en_US
dc.identifier.uri	http://hdl.handle.net/10453/28226
dc.description.abstract	FLC is a MADS box transcription factor that acts as a dosage-dependent repressor of flowering. We carried out a 2D gel analysis and showed that the majority of endogenous FLC and overexpressed FLC-FLAG proteins are post-translationally modified. The endogenous and transgenic proteins have different floral repressor activities; however, they have similar, if not the same, profiles of post-translational modifications. The protein modification profile was also not changed by vernalization treatment. The activities of other MADS box proteins have been shown to be affected by phosphorylation and we found that both the endogenous FLC and the transgenic FLC-FLAG protein are phosphorylated. When eight potential serine kinase target sites in FLC were changed to mimic phosphorylated residues, expression of the mutant FLC-FLAG protein led to early flowering, suggesting that the repressive function was abolished. When the same eight serine residues were changed to non-phosphorylatable residues, expression of the resulting protein gave the same weak flowering repression as overexpressed unmodified FLC-FLAG. The non-phosphorylatable variant of FLC-FLAG showed a similar spectrum of post-translational modifications to unmodified FLC-FLAG, indicating that modifications other than the predicted phosphorylations occur. Our data provide evidence for a post-translational regulation of FLC function. © The Author 2008. Published by Oxford University Press on behalf of Japanese Society of Plant Physiologists. All rights reserved.	en_US
dc.relation.ispartof	Plant and Cell Physiology	en_US
dc.relation.isbasedon	10.1093/pcp/pcn167	en_US
dc.subject.classification	Plant Biology & Botany	en_US
dc.subject.mesh	Plants, Genetically Modified	en_US
dc.subject.mesh	Arabidopsis	en_US
dc.subject.mesh	Flowers	en_US
dc.subject.mesh	MADS Domain Proteins	en_US
dc.subject.mesh	Arabidopsis Proteins	en_US
dc.subject.mesh	Protein Processing, Post-Translational	en_US
dc.subject.mesh	Phosphorylation	en_US
dc.subject.mesh	Genes, Plant	en_US
dc.title	Post-translational modifications of the endogenous and transgenic FLC protein in Arabidopsis thaliana	en_US
dc.type	Journal Article
utslib.citation.volume	12	en_US
utslib.citation.volume	49	en_US
utslib.for	060702 Plant Cell and Molecular Biology	en_US
utslib.for	0601 Biochemistry and Cell Biology	en_US
utslib.for	0607 Plant Biology	en_US
pubs.embargo.period	Not known	en_US
pubs.organisational-group	/University of Technology Sydney
pubs.organisational-group	/University of Technology Sydney/Faculty of Science
pubs.organisational-group	/University of Technology Sydney/Faculty of Science/School of Life Sciences
utslib.copyright.status	closed_access
pubs.issue	12	en_US
pubs.publication-status	Published	en_US
pubs.volume	49	en_US

Abstract:

FLC is a MADS box transcription factor that acts as a dosage-dependent repressor of flowering. We carried out a 2D gel analysis and showed that the majority of endogenous FLC and overexpressed FLC-FLAG proteins are post-translationally modified. The endogenous and transgenic proteins have different floral repressor activities; however, they have similar, if not the same, profiles of post-translational modifications. The protein modification profile was also not changed by vernalization treatment. The activities of other MADS box proteins have been shown to be affected by phosphorylation and we found that both the endogenous FLC and the transgenic FLC-FLAG protein are phosphorylated. When eight potential serine kinase target sites in FLC were changed to mimic phosphorylated residues, expression of the mutant FLC-FLAG protein led to early flowering, suggesting that the repressive function was abolished. When the same eight serine residues were changed to non-phosphorylatable residues, expression of the resulting protein gave the same weak flowering repression as overexpressed unmodified FLC-FLAG. The non-phosphorylatable variant of FLC-FLAG showed a similar spectrum of post-translational modifications to unmodified FLC-FLAG, indicating that modifications other than the predicted phosphorylations occur. Our data provide evidence for a post-translational regulation of FLC function. © The Author 2008. Published by Oxford University Press on behalf of Japanese Society of Plant Physiologists. All rights reserved.

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http://hdl.handle.net/10453/28226