Research article summary (published 29 Sep 2009):

The major specificity-determining amino acids of the tomato Cf-9 disease resistance protein are at hypervariable solvent-exposed positions in the central leucine-rich repeats.

Full Abstract

The interaction between tomato and the leaf mold pathogen Cladosporium fulvum is controlled in a gene-for-gene manner by plant Cf genes that encode membrane-anchored extracytoplasmic leucine-rich repeat (LRR) glycoproteins, which confer recognition of their cognate fungal avirulence (Avr) proteins. Cf-9 and Cf-4 are two such proteins that are 91% identical yet recognize the sequence-unrelated fungal avirulence determinants Avr9 and Avr4, respectively. As shown previously, Cf-4 specificity is determined by three putative solvent-exposed residues in the central LRR and a deletion of two LRR relative to Cf-9. In this study, we focused on identifying the specificity determinants of Cf-9. We generated chimeras between Cf-9 and its close homologue Cf-9B and identified five amino acid residues that constitute major specificity determinants of Cf-9. Introduction of these residues into Cf-9B allowed recognition of Avr9. Consistent with a role in recognition specificity, the identified residues are putatively solvent exposed in the central LRR and occupy hypervariable positions in the global Cf alignment. One of the specificity residues is not found in any other known Cf protein, suggesting the importance of diversifying selection rather than sequence exchange between homologues. Interestingly, there is an overlap between the Cf-4 and Cf-9 specificity-determining residues, precluding a protein with dual specificity.

Author information

Author/s: Wulff, Brande B H (BB); Heese, Antje (A); Tomlinson-Buhot, Laurence (L); Jones, David A (DA); de la Peña, Marcos (M); Jones, Jonathan D G (JD);

Affiliation: The Sainsbury Laboratory, John Innes Centre, Norwich Research Park, Colney Lane, Norwich NR4 7UH, UK.

Journal and publication information

Publication Type: Journal Article; Research Support, Non-U.S. Gov't

Journal: Molecular plant-microbe interactions : MPMI (Mol Plant Microbe Interact), published in United States. (Language: eng)

Reference: 2009-Oct; vol 22 (issue 10) : pp 1203-13

Dates: Created 2009/09/09; Completed 2009/11/09;

PMID: 19737094, status: MEDLINE (last retrieved date: 11/9/2009)

Sourced from the National Library of Medicine. Abstract text and other information may be subject to copyright.

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MeSH headings (categories)

This article was linked to the MeSH Headings (categories) shown below.

Amino Acid Sequence Amino Acids - chemistry Cladosporium - pathogenicity Fungal Proteins - genetics; physiology Genes, Plant Host-Pathogen Interactions - genetics; physiology Lycopersicon esculentum - genetics; microbiology; physiology Membrane Glycoproteins - chemistry; genetics; physiology Models, Molecular

Models, Molecular Molecular Sequence Data Mutagenesis, Site-Directed Plant Diseases - genetics; microbiology Plant Proteins - chemistry; genetics; physiology Proteins - chemistry; genetics; physiology Recombinant Fusion Proteins - chemistry; genetics Sequence Homology, Amino Acid Solvents

Note: Bold headings indicate primary MeSH headings or qualifiers.

Associated Chemicals: Amino Acids (0) ; Cf protein, Lycopersicon esculentum (0) ; Fungal Proteins (0) ; Membrane Glycoproteins (0) ; Plant Proteins (0) ; Proteins (0) ; Recombinant Fusion Proteins (0) ; Solvents (0) ; leucine-rich repeat proteins (0) ; AVR9 protein, Cladosporium fulvum (138880-27-0)

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