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Edinburgh, Scotland, United Kingdom - TAIR

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New classes of proteins forming complexes<br />

with resistance proteins<br />

Resistance (R) proteins directly or indirectly recognize cognate pathogen<br />

effectors, thereby activating effector-triggered immunity (ETI). Two types of<br />

proteins have been reported to form complexes with the NB-LRR class of R<br />

proteins before R proteins are activated by the effectors: chaperone-type<br />

proteins such as RAR1 and SGT1; and protein targets (or decoys) of the<br />

effectors, such as RIN4. We used a biotin affinity-purification tag to purify R<br />

protein complexes (Qi and Katagiri, Plant J. 57, 932 (2009)) and identified new<br />

classes of candidate proteins forming complexes with the NB-LRR proteins<br />

RPS2 and/or RPM1 before R protein activation. One class consists of the<br />

hypersensitive response-induced reaction (HIR) proteins, which is characterized<br />

by the stomatin/prohibitin/flotillin/HflK/C (SPFH) domain motif. A close physical<br />

association between RPS2 and a HIR protein was confirmed by fluorescence<br />

resonance energy transfer (FRET) after transiently expressing RPS2::CFP and<br />

HIR::YFP in N. benthamiana. In addition, HIR proteins make homo- and hetero-<br />

HIR protein complexes. As HIR proteins are localized in lipid rafts in the plasma<br />

membrane, RPS2 may also be localized in lipid rafts prior to activation. We will<br />

report other classes of proteins in resistance protein complexes in addition to<br />

the HIR proteins.<br />

79<br />

C28<br />

Thursday 15:30 - 15:45<br />

Plant Defence<br />

Yiping Qi<br />

Fumiaki Katagiri<br />

Dept of Plant Biology<br />

Microbial and Plant<br />

Genomics Inst<br />

Univ of Minnesota<br />

St. Paul<br />

MN<br />

USA

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