The WD-repeat protein superfamily in Arabidopsis: conservation and divergence in structure and function.
BACKGROUND
The WD motif (also known as the Trp-Asp or WD40 motif) is found in a multitude of eukaryotic proteins involved in a variety of cellular processes. Where studied, repeated WD motifs act as a site for protein-protein interaction, and proteins containing WD repeats (WDRs) are known to serve as platforms for the assembly of protein complexes or mediators of transient interplay among other proteins. In the model plant Arabidopsis thaliana, members of this superfamily are increasingly being recognized as key regulators of plant-specific developmental events.


RESULTS
We analyzed the predicted complement of WDR proteins from Arabidopsis, and compared this to those from budding yeast, fruit fly and human to illustrate both conservation and divergence in structure and function. This analysis identified 237 potential Arabidopsis proteins containing four or more recognizable copies of the motif. These were classified into 143 distinct families, 49 of which contained more than one Arabidopsis member. Approximately 113 of these families or individual proteins showed clear homology with WDR proteins from the other eukaryotes analyzed. Where conservation was found, it often extended across all of these organisms, suggesting that many of these proteins are linked to basic cellular mechanisms. The functional characterization of conserved WDR proteins in Arabidopsis reveals that these proteins help adapt basic mechanisms for plant-specific processes.


CONCLUSIONS
Our results show that most Arabidopsis WDR proteins are strongly conserved across eukaryotes, including those that have been found to play key roles in plant-specific processes, with diversity in function conferred at least in part by divergence in upstream signaling pathways, downstream regulatory targets and /or structure outside of the WDR regions.
van Nocker
Steven
S
Cell and Molecular Biology Program and Department of Horticulture, 390 Plant and Soil Sciences Building, Michigan State University, East Lansing, MI 48824, USA. vannocke@msu.edu
Ludwig
Philip
P
D000818:Animals; D029681:Arabidopsis Proteins / Q000235:genetics* / Q000502:physiology; D001224:Aspartic Acid / Q000235:genetics; D004331:Drosophila melanogaster / Q000235:genetics; D005796:Genes / Q000235:genetics; D014644:Genetic Variation; D006801:Humans; D005810:Multigene Family / Q000235:genetics*; D020449:Repetitive Sequences, Amino Acid / Q000235:genetics*; D012441:Saccharomyces cerevisiae / Q000235:genetics; D014364:Tryptophan / Q000235:genetics
D029681:Arabidopsis Proteins; D001224:Aspartic Acid; D014364:Tryptophan