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Arabidopsis B‐cell lymphoma2 (Bcl‐2)‐associated athanogene 7 ( BAG 7)‐mediated heat tolerance requires translocation, sumoylation and binding to WRKY 29
Author(s) -
Li Yurong,
Williams Brett,
Dickman Martin
Publication year - 2017
Publication title -
new phytologist
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.742
H-Index - 244
eISSN - 1469-8137
pISSN - 0028-646X
DOI - 10.1111/nph.14388
Subject(s) - arabidopsis , microbiology and biotechnology , sumo protein , unfolded protein response , transcription factor , endoplasmic reticulum , biology , chaperone (clinical) , wrky protein domain , nucleus , genetics , ubiquitin , mutant , gene , medicine , pathology
Summary To cope with stress and increased accumulation of misfolded proteins, plants and animals use a survival pathway known as the unfolded protein response ( UPR ) that signals between the endoplasmic reticulum ( ER ) and the nucleus to maintain cell homeostasis via proper folding of proteins. B‐cell lymphoma2 (Bcl‐2)‐associated athanogene ( BAG ) proteins are an evolutionarily conserved family of co‐chaperones that are linked to disease states in mammals and responses to environmental stimuli (biotic and abiotic) in plants. Molecular and physiological techniques were used to functionally characterize a newly identified branch of the UPR initiated by the ER ‐localized co‐chaperone from Arabidopsis thaliana , At BAG 7. At BAG 7 has functional roles in both the ER and the nucleus. Upon heat stress, At BAG 7 is sumoylated, proteolytically processed and translocated from the ER to the nucleus, where interaction with the WRKY 29 transcription factor occurs. Sumoylation and translocation are required for the At BAG 7– WRKY 29 interaction and subsequent stress tolerance. In the ER , At BAG 7 interacts with the ER‐localized transcription factor, AtbZIP28, and established UPR regulator, the AtBiP2 chaperone. The results indicate that At BAG 7 plays a central regulatory role in the heat‐induced UPR pathway.