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Published on March 2, 2006; 10.1104/pp.105.075382

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Received December 14, 2005
Returned for revision January 15, 2006
Accepted February 14, 2006

Characterization of the plant-specific BRX gene family reveals limited genetic redundancy despite high sequence conservation

Georgette C. Briggs , Céline F. Mouchel , and Christian S. Hardtke *

Department of Plant Molecular Biology, University of Lausanne, Biophore Building, CH-1015 Lausanne, Switzerland, and Biology Department, McGill University, 1205 Dr. Penfield Avenue, Montréal, Québec H3A 1B1, Canada

* Corresponding author; email: christian.hardtke{at}unil.ch.

To date, the function of most genes in the Arabidopsis genome is unknown. Here we present the first analysis of the novel, plant-specific BRX gene family. BRX has been identified as a modulator of root growth through a naturally occurring loss-of-function allele. The biochemical function of BRX is enigmatic, however several domains in BRX are conserved in the proteins encoded by the related BRX-like (BRXL) genes. The similarity between Arabidopsis BRXL proteins within these domains ranges from 84-93%. Nevertheless, analysis of brx brx-like multiple mutants indicates that functional redundancy of BRXLs is limited. This results mainly from differences in protein activity, as demonstrated by assaying the propensity of constitutively expressed BRXL cDNAs to rescue the brx phenotype. Among the genes tested, only BRXL1 can replace BRX in this assay. Nevertheless, BRXL1 does not act redundantly with BRX in vivo, presumably because it is expressed at much lower level than BRX. BRX and BRXL1 similarity is most pronounced in a characteristic tandem repeat domain, which we named "BRX domain". One copy of this domain is also present in the PRAF-like family proteins. The BRX domain mediates homo- and heterotypic interactions within and between the BRX and PRAF protein families in yeast, and therefore likely represents a novel protein-protein interaction domain. The importance of this domain for BRX activity in planta is underscored by our finding that expression of the C-terminal fragment of BRX, comprising the two BRX domains, is largely sufficient to rescue the brx phenotype.




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