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 Clade,

Author:

Baumberger Nicolas1,Doesseger Brigitte1,Guyot Romain1,Diet Anouck1,Parsons Ronald L.2,Clark Mark A.2,Simmons M.P.2,Bedinger Patricia2,Goff Stephen A.3,Ringli Christoph1,Keller Beat1

Affiliation:

1. Institute of Plant Biology, University of Zurich, CH–8008 Zurich, Switzerland (N.B., B.D., R.G., A.D., C.R., B.K.);

2. Department of Biology, Colorado State University, Fort Collins, Colorado 80523–1878 (R.L.P., M.A.C., M.P.S., P.B.); and

3. Torrey Mesa Institute, Syngenta, 3115 Meryfield Row, San Diego, California 92121 (S.A.G.)

Abstract

Abstract 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. TheLRX 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.

Publisher

Oxford University Press (OUP)

Subject

Plant Science,Genetics,Physiology

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