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First published online February 18, 2005; 10.1105/tpc.104.028118

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The Plant Cell 17:1000-1015 (2005)
© 2005 American Society of Plant Biologists

Structure–Function Analysis of Cf-9, a Receptor-Like Protein with Extracytoplasmic Leucine-Rich Repeats{boxw}

Renier A.L. van der Hoorna,1, Brande B.H. Wulffb,c,1, Susana Rivasb,d,1, Marcus C. Durrante, Anke van der Ploega, Pierre J.G.M. de Wita and Jonathan D.G. Jonesb,2

a Wageningen University, Laboratory of Phytopathology, 6709 PD, Wageningen, The Netherlands
b Sainsbury Laboratory, John Innes Centre, Norwich Research Park, Norwich NR4 7UH, United Kingdom
c Instituto de Biología Molecular y Celular de Plantas, Universidad Politécnica de Valencia, 46022 Valencia, Spain
d Laboratoire des Interactions Plantes-Microorganismes, Unité Mixte de Recherche, Centre National de la Recherche Scientifique/Institut National de la Recherche Agronomique 2594/441, 31326 Castanet-Tolosan Cedex, France
e Computational Biology Group, John Innes Centre, Norwich Research Park, Norwich NR4 7UH, United Kingdom

2 To whom correspondence should be addressed. E-mail jonathan.jones{at}sainsbury-laboratory.ac.uk; fax 44-01603-450011.

The tomato (Lycopersicon pimpinellifolium) resistance protein Cf-9 belongs to a large class of plant proteins with extracytoplasmic Leu-rich repeats (eLRRs). eLRR proteins play key roles in plant defense and development, mainly as receptor-like proteins or receptor-like kinases, conferring recognition of various pathogen molecules and plant hormones. We report here a large-scale structure–function analysis of an eLRR protein. A total of 66 site-directed mutants of Cf-9 were analyzed for activity in Avr9 recognition and for protein stability and the results interpreted with the help of a homology model of the Cf-9 structure. Conserved Trp and Cys pairs in the N-terminal LRR-flanking domain appear to be important for Cf-9 activity and are probably exposed at the putative concave inner surface of the Cf-9 protein, where recognition specificity also resides. Removal of each of the 22 putative N-linked glycosylation sites (PGS) revealed that many PGSs contribute to Cf-9 activity and that the PGSs in the putative {alpha}-helices of the LRR modules are essential. Immunoblot analysis and mass spectrometry showed that all but one of the PGSs are N-glycosylated. Introduction of glycosylation at the putative concave ß-sheet surface blocks Cf-9 activity, in some cases probably by disturbing specific recognition, and in another case by steric hindrance with existing N-glycans. The glycosylation pattern and several other features are conserved in other eLRR proteins, where similar mutations show similar phenotypes.




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