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- W2137779221 abstract "The floral meristem identity gene LEAFY (LFY) of Arabidopsis thaliana is essential for the formation of fertile flowers and has roles in the control of several aspects of floral development, which include phyllotaxy and organ number and identity. This gene encodes a land plant-specific transcription factor and regulates expression of a number of genes that include other floral meristem identity genes and floral homeotic genes. Although the LFY DNA-binding domain has a structure that resembles that of helix–turn–helix proteins, LFY and its orthologs represent a novel family of transcription factors that are characterized by a conserved N-terminus domain of unknown function and a C-terminus DNA-binding domain. Many transcription factors act as dimers. These dimers are essential for the biological activity of the proteins. We demonstrate that LFY forms homodimers or oligomers in solution. This association is mediated through the N-terminus conserved region of the LFY protein. Although mutant LFY proteins that cannot dimerize in solution can bind DNA, the binding is weaker than that of wild type LFY protein. LFY–LFY interactions mediated by the N-terminus domain are essential for the biological activity of this protein, as mutations that abolish the ability to self-associate cannot complement an lfy null allele. Our data indicate: (i) that LFY, and probably its orthologs in other plants, must act in complexes that contain at least two LFY molecules; and (ii) that the N-terminus is essential for stabilization of LFY complexes. This situation is integral to the ability of LFY to regulate gene expression." @default.
- W2137779221 created "2016-06-24" @default.
- W2137779221 creator A5026564493 @default.
- W2137779221 creator A5063499733 @default.
- W2137779221 date "2012-06-12" @default.
- W2137779221 modified "2023-10-18" @default.
- W2137779221 title "A conserved domain in the N-terminus is important for LEAFY dimerization and function in Arabidopsis thaliana" @default.
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- W2137779221 doi "https://doi.org/10.1111/j.1365-313x.2012.05026.x" @default.
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