Plant and Cell Physiology Advance Access published online on April 4, 2005
Plant and Cell Physiology, doi:10.1093/pcp/pci097
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1 Program in Biochemistry, Biophysics, and Molecular Biology, Department of Biology, Whitman College, Walla Walla, WA 99362
* To whom correspondence should be addressed. Leucine rich repeat proteins (LRRs) feature tandem leucine-rich motifs that form a protein-protein interaction domain. Plants contain diverse classes of LRRs, many of which take part in signal transduction. We have identified a novel family of nine Arabidopsis LRRs that, based on predicted intracellular location and LRR-motif consensus sequence, are related to Ras-binding LRRs found in signaling complexes in animal and yeast. This new class has been named Plant Intracellular Ras-group-related LRRs (PIRLs). We have characterized PIRL cDNAs, rigorously defined gene and protein annotations, investigated gene-family evolution, and surveyed mRNA expression. While LRR regions suggested a relationship to Ras-group LRRs, outside of their LRR domains PIRLs differed from Ras-group proteins, exhibiting N- and C-terminal regions containing low-complexity stretches and clusters of charged amino acids. PIRLs grouped into three sub-families based on sequence relationships and gene structures. Related gene pairs and dispersed chromosomal locations suggested family expansion by ancestral genomic or segmental duplications. Expression surveys revealed that all PIRL mRNAs are actively transcribed, with three expressed differentially in leaves, roots, or flowers. These results define PIRLs as a distinct, plant-specific class of intracellular LRRs that likely mediate protein interactions, possibly in the context of signal transduction. T-DNA knock-out mutants have been isolated as a starting point for systematic functional analysis of this intriguing family.
Received December 9, 2004
Accepted March 25, 2005
Regular Paper
PIRLs: A Novel Class of Plant Intracellular Leucine-Rich Repeat Proteins
Daniel M. Vernon, E-mail: vernondm{at}whitman.edu
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