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First published online February 13, 2003; 10.1104/pp.102.014928

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Plant Physiol, March 2003, Vol. 131, pp. 1313-1326

Whole-Genome Comparison of Leucine-Rich Repeat Extensins in Arabidopsis and Rice. A Conserved Family of Cell Wall Proteins Form a Vegetative and a Reproductive Clade1,[w]

Nicolas Baumberger,2 Brigitte Doesseger, Romain Guyot, Anouck Diet, Ronald L. Parsons, Mark A. Clark, M.P. Simmons, Patricia Bedinger, Stephen A. Goff, Christoph Ringli, and Beat Keller*

Institute of Plant Biology, University of Zurich, CH-8008 Zurich, Switzerland (N.B., B.D., R.G., A.D., C.R., B.K.); Department of Biology, Colorado State University, Fort Collins, Colorado 80523-1878 (R.L.P., M.A.C., M.P.S., P.B.); and Torrey Mesa Institute, Syngenta, 3115 Meryfield Row, San Diego, California 92121 (S.A.G.)

We have searched the Arabidopsis and rice (Oryza sativa) genomes for homologs of LRX1, an Arabidopsis gene encoding a novel type of cell wall protein containing a leucine-rich repeat (LRR) and an extensin domain. Eleven and eight LRX (LRR/EXTENSIN) genes have been identified in these two plant species, respectively. The LRX gene family encodes proteins characterized by a short N-terminal domain, a domain with 10 LRRs, a cysteine-rich motif, and a variable C-terminal extensin-like domain. Phylogenetic analysis performed on the conserved domains indicates the existence of two major clades of LRX proteins that arose before the eudicot/monocot divergence and then diversified independently in each lineage. In Arabidopsis, gene expression studies by northern hybridization and promoter::uidA fusions showed that the two phylogenetic clades represent a specialization into "reproductive" and "vegetative" LRXs. The four Arabidopsis genes of the "reproductive" clade are specifically expressed in pollen, whereas the seven "vegetative" genes are predominantly expressed in various sporophytic tissues. This separation into two expression classes is also supported by previous studies on maize (Zea mays) and tomato (Lycopersicon esculentum) LRX homologs and by information on available rice ESTs. The strong conservation of the amino acids responsible for the putative recognition specificity of the LRR domain throughout the family suggests that the LRX proteins interact with similar ligands.


1 This work was supported by the Swiss National Science Foundation (grant nos. 31-51055.97 and 41-6 419.00) and by the National Science Foundation (grant no. 0091976 to P.A.B.).

2 Present address: Sainsbury Laboratory, John Innes Centre Colney, NR4 7UH Norwich, UK.

[w] The online version of this article contains Web-only data. The supplemental material is available at www.plantphysiol.org.

* Corresponding author; e-mail bkeller{at}botinst.unizh.ch; fax 41-1-6348204.

© 2003 American Society of Plant Biologists



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