Selective autophagy regulates heat stress memory in Arabidopsis by NBR1-mediated targeting of HSP90.1 and ROF1
| Autor: | Karina Schulz, Céline Masclaux-Daubresse, Venkatesh P Thirumalaikumar, Michal Gorka, Arun Sampathkumar, Richard D. Vierstra, Salma Balazadeh, Aleksandra Skirycz |
|---|---|
| Jazyk: | angličtina |
| Rok vydání: | 2020 |
| Předmět: |
0301 basic medicine
Yellow fluorescent protein Proteomics Arabidopsis thaliana Arabidopsis HSFA2 ROF1 stress recovery Green fluorescent protein heat stress Tacrolimus Binding Proteins 03 medical and health sciences Bimolecular fluorescence complementation Gene Expression Regulation Plant Tandem Mass Spectrometry Heat shock protein Macroautophagy Autophagy HSP90 Heat-Shock Proteins Molecular Biology Transcription factor stress memory 2. Zero hunger HSP90.1 selective autophagy 030102 biochemistry & molecular biology biology Arabidopsis Proteins Cell Biology NBR1 Hsp90 Cell biology Heat shock factor 030104 developmental biology FKBP biology.protein Carrier Proteins Heat-Shock Response Research Article Research Paper |
| Zdroj: | Autophagy article-version (VoR) Version of Record |
| ISSN: | 1554-8635 1554-8627 |
| Popis: | In nature, plants are constantly exposed to many transient, but recurring, stresses. Thus, to complete their life cycles, plants require a dynamic balance between capacities to recover following cessation of stress and maintenance of stress memory. Recently, we uncovered a new functional role for macroautophagy/autophagy in regulating recovery from heat stress (HS) and resetting cellular memory of HS in Arabidopsis thaliana. Here, we demonstrated that NBR1 (next to BRCA1 gene 1) plays a crucial role as a receptor for selective autophagy during recovery from HS. Immunoblot analysis and confocal microscopy revealed that levels of the NBR1 protein, NBR1-labeled puncta, and NBR1 activity are all higher during the HS recovery phase than before. Co-immunoprecipitation analysis of proteins interacting with NBR1 and comparative proteomic analysis of an nbr1-null mutant and wild-type plants identified 58 proteins as potential novel targets of NBR1. Cellular, biochemical and functional genetic studies confirmed that NBR1 interacts with HSP90.1 (heat shock protein 90.1) and ROF1 (rotamase FKBP 1), a member of the FKBP family, and mediates their degradation by autophagy, which represses the response to HS by attenuating the expression of HSP genes regulated by the HSFA2 transcription factor. Accordingly, loss-of-function mutation of NBR1 resulted in a stronger HS memory phenotype. Together, our results provide new insights into the mechanistic principles by which autophagy regulates plant response to recurrent HS. Abbreviations: AIM: Atg8-interacting motif; ATG: autophagy-related; BiFC: bimolecular fluorescence complementation; ConA: concanamycinA; CoIP: co-immunoprecipitation; DMSO: dimethyl sulfoxide; FKBP: FK506-binding protein; FBPASE: fructose 1,6-bisphosphatase; GFP: green fluorescent protein; HS: heat stress; HSF: heat shock factor; HSFA2: heat shock factor A2; HSP: heat shock protein; HSP90: heat shock protein 90; LC-MS/MS: Liquid chromatography-tandem mass spectrometry; 3-MA: 3-methyladenine; NBR1: next-to-BRCA1; PQC: protein quality control; RFP: red fluorescent protein; ROF1: rotamase FKBP1; TF: transcription factor; TUB: tubulin; UBA: ubiquitin-associated; YFP: yellow fluorescent protein |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|