Edinburgh, Scotland, United Kingdom - TAIR
Edinburgh, Scotland, United Kingdom - TAIR
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