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