<HashMap><database>biostudies-literature</database><scores/><additional><omics_type>Unknown</omics_type><volume>63(4)</volume><submitter>Van Ooijen G</submitter><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</pubmed_abstract><journal>The Plant journal : for cell and molecular biology</journal><pagination>563-72</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC2988412</full_dataset_link><repository>biostudies-literature</repository><pubmed_title>The small heat shock protein 20 RSI2 interacts with and is required for stability and function of tomato resistance protein I-2.</pubmed_title><pmcid>PMC2988412</pmcid><pubmed_authors>Vossen JH</pubmed_authors><pubmed_authors>Takken FL</pubmed_authors><pubmed_authors>Van Ooijen G</pubmed_authors><pubmed_authors>Lukasik E</pubmed_authors><pubmed_authors>Van Den Burg HA</pubmed_authors><pubmed_authors>Cornelissen BJ</pubmed_authors></additional><is_claimable>false</is_claimable><name>The small heat shock protein 20 RSI2 interacts with and is required for stability and function of tomato resistance protein I-2.</name><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</description><dates><release>2010-01-01T00:00:00Z</release><publication>2010 Aug</publication><modification>2026-05-01T06:33:37.087Z</modification><creation>2019-03-27T00:36:48Z</creation></dates><accession>S-EPMC2988412</accession><cross_references><pubmed>20497382</pubmed><doi>10.1111/j.1365-313X.2010.04260.x</doi></cross_references></HashMap>