{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"omics_type":["Unknown"],"volume":["63(4)"],"submitter":["Van Ooijen G"],"pubmed_abstract":["Race-specific disease resistance in plants depends on the presence of resistance (R) genes. Most R genes encode NB-ARC-LRR proteins that carry a C-terminal leucine-rich repeat (LRR). Of the few proteins found to interact with the LRR domain, most have proposed (co)chaperone activity. Here, we report the identification of RSI2 (Required for Stability of I-2) as a protein that interacts with the LRR domain of the tomato R protein I-2. RSI2 belongs to the family of small heat shock proteins (sHSPs or HSP20s). HSP20s are ATP-independent chaperones that form oligomeric complexes with client proteins to prevent unfolding and subsequent aggregation. Silencing of RSI2-related HSP20s in Nicotiana benthamiana compromised the hypersensitive response that is normally induced by auto-active variants of"],"journal":["The Plant journal : for cell and molecular biology"],"pagination":["563-72"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC2988412"],"repository":["biostudies-literature"],"pubmed_title":["The small heat shock protein 20 RSI2 interacts with and is required for stability and function of tomato resistance protein I-2."],"pmcid":["PMC2988412"],"pubmed_authors":["Vossen JH","Takken FL","Van Ooijen G","Lukasik E","Van Den Burg HA","Cornelissen BJ"],"additional_accession":[]},"is_claimable":false,"name":"The small heat shock protein 20 RSI2 interacts with and is required for stability and function of tomato resistance protein I-2.","description":"Race-specific disease resistance in plants depends on the presence of resistance (R) genes. Most R genes encode NB-ARC-LRR proteins that carry a C-terminal leucine-rich repeat (LRR). Of the few proteins found to interact with the LRR domain, most have proposed (co)chaperone activity. Here, we report the identification of RSI2 (Required for Stability of I-2) as a protein that interacts with the LRR domain of the tomato R protein I-2. RSI2 belongs to the family of small heat shock proteins (sHSPs or HSP20s). HSP20s are ATP-independent chaperones that form oligomeric complexes with client proteins to prevent unfolding and subsequent aggregation. Silencing of RSI2-related HSP20s in Nicotiana benthamiana compromised the hypersensitive response that is normally induced by auto-active variants of","dates":{"release":"2010-01-01T00:00:00Z","publication":"2010 Aug","modification":"2026-05-01T06:33:37.087Z","creation":"2019-03-27T00:36:48Z"},"accession":"S-EPMC2988412","cross_references":{"pubmed":["20497382"],"doi":["10.1111/j.1365-313X.2010.04260.x"]}}