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Published on November 6, 2009; 10.1104/pp.109.148197

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Received September 28, 2009
Accepted November 5, 2009

Functional analyses of the CLV2-like proteins and their domains that contribute to CLV2 specificity

Guodong Wang , Yuchen Long , Bart P.H.J. Thomma , P.J.G.M. de Wit , Gerco C. Angenent , and Martijn Fiers *

Plant Research International, Business Unit Bioscience, Droevendaalsesteeg 1, 6708 PB, Wageningen, The Netherlands; Laboratory of Phytopathology, Wageningen University, Droevendaalsesteeg 1, 6708 PB, Wageningen, The Netherlands; Centre for BioSystems Genomics (CBSG), Droevendaalsesteeg 1, 6708 PB, Wageningen, The Netherlands

* Corresponding author; email: martijn.fiers{at}wur.nl.

The Arabidopsis thaliana CLAVATA2 (CLV2) gene encodes a leucine-rich repeat receptor-like protein (LRR-RLP) that is involved in controlling the stem cell population size in the shoot apical meristem. Our previous genome-wide functional analysis of 57 Arabidopsis RLP (AtRLP) genes revealed only a few phenotypes for mutant alleles, despite screening a wide range of growth and developmental stages, and assaying sensitivity to various stress responses including susceptibility toward pathogens. To gain further insight into the biological role of AtRLPs, in particular of CLV2-related AtRLP genes, we tested their ability to complement the clv2 mutant phenotype. We found that out of four close CLV2 homologues tested, AtRLP2 and AtRLP12 could functionally complement the clv2 mutant when expressed under the control of the CLV2 promoter. This indicates that the functional specificity of these three genes is determined at the level of their transcriptional regulation. Single and double mutant combinations with impaired AtRLP2 and/or AtRLP12 did not show an aberrant phenotype, suggesting that other genes are redundant with these CLV2-like genes. To understand which protein domains are essential for CLV2 function and which parts are interchangeable between related CLV2-like proteins, we performed domain-deletion and domain-swap experiments. These experiments revealed that CLV2 remains functional without the island domain, whereas the C1 and C3 region of the LRR domain are essential for functionality. Analysis of domain-swap constructs showed that the C3-G region of CLV2 can be replaced by that of AtRLP38, although it could not complement the clv2 mutant under control of the CLV2 promoter. This suggests that the C3-G region is conserved among related AtRLP members, whereas the C1 domain may determine the functional specificity of CLV2.






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