Journal
CURRENT OPINION IN PLANT BIOLOGY
Volume 12, Issue 4, Pages 427-436Publisher
CURRENT BIOLOGY LTD
DOI: 10.1016/j.pbi.2009.03.001
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Funding
- CBSG
- EC Integrated Project BIOEXPLOIT [CT-2005-513959]
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Resistance (R) proteins are involved in specific pathogen recognition and subsequent initiation of host defence. Most R proteins are nucleotide binding - leucine rich repeat (NB-LRR) proteins, which form a subgroup within the STAND (signal transduction ATPases with numerous domains) family. Activity of these multi-domain proteins depends on their ability to bind and hydrolyse nucleotides. Since R protein activation often triggers cell-death tight regulation of activation is essential. Autoinhibition, which seems to be accomplished by intramolecular interactions between the various domains, is important to retain R proteins inactive. This review summarizes recent data on intra- and intermolecular interactions that support a model in which pathogen perception triggers a series of conformational changes, allowing the newly exposed NB domain to interact with downstream signalling partners and activate defence signalling.
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