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Structure / Function analysis of RLPs


Plants have evolved mechanisms to defend themselves. Defence mechanisms are often triggered after the direct or indirect interaction of a disease resistance (R) gene from the plant and an avirulence (Avr) gene from the pathogen. In the absence of the R gene or the Avr gene, disease ensues. Such "gene-for- gene" interactions are known for many different pathogens and plants. R proteins can be divided into five classes based on their structure. The focus of my work will be on the Receptor-like Protein (RLP) class, of which Cf-9 is the founding member.

RLPs are membrane-anchored glycoproteins with extra-cytoplasmic Leucine Rich Repeat (LRRs, a protein-protein interaction motif), a transmembrane domain and a short cytoplasmic tail lacking any obvious signalling domain. The Cf-9 protein has 27 LRRs, which are divided in two blocks. Domain Cl comprises 23 LRRs, and the second, domain C3, has 4 LRRs. In between there is a putative "hinge" region, which does not have any LRRs, called domain C2. Sequence alignments of C2 between Cf-9 and Arabidopsis RLPs (AtRLPs) reveal conserved amino acids. Amino-acids surrounding the C2 region are also well conserved.

The aim of the proposed project is to:
(i) investigate the functional significance of amino acids conserved between Cf-9 and Arabidopsis RLPs, using transient assays of mutated Cf-9 alleles in Nicotiana benthamiana and
(ii) to make chimeras of Cf- proteins and Arabidopsis proteins, that can be transiently assessed in transient assays in turnip, to try establish a Cf-9/Avr9 response in Arabidopsis that can be used for genetic studies on Cf-9 signal transduction.

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Norwich Research Park, Colney
United Kingdom

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