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The Bcl-2 associated athanogene (BAG) family is an evolutionarily conserved group of co-chaperones that confers stress protection against a variety of cellular insults extending from yeasts, plants to humans. Little is known, however, regarding the biological role of BAG proteins in phytopathogenic fungi. Here, we identified the unique BAG gene ( BcBAG1 ) from the necrotrophic fungal pathogen,  Botrytis cinerea . BcBAG1 is the homolog of  Arabidopsis thaliana  AtBAG4, and ectopic expression of  BcBAG1  in  atbag4  knock-out mutants restores salt tolerance.  BcBAG1  deletion mutants (Δ Bcbag1 ) exhibited decreased conidiation, enhanced melanin accumulation and lost the ability to develop sclerotia. Also,  BcBAG1  disruption blocked fungal conidial germination and successful penetration, leading to a reduced virulence in host plants. BcBAG1 contains BAG (BD) domain at C-terminus and ubiquitin-like (UBL) domain at N-terminus. Complementation assays indicated that BD can largely restored pathogenicity of Δ Bcbag1 . Abiotic stress assays showed Δ Bcbag1  was more sensitive than the wild-type strain to NaCl, calcofluor white, SDS, tunicamycin, dithiothreitol (DTT), heat and cold stress, suggesting BcBAG1 plays a cytoprotective role during salt stress, cell wall stress, and ER stress. BcBAG1 negatively regulated the expression of  BcBIP1 ,  BcIRE1  and the splicing of  BcHAC1  mRNA, which are core regulators of unfolded protein response (UPR) during ER stress. Moreover, BcBAG1 interacted with HSP70-type chaperones, BcBIP1 and BcSKS2. In summary, this work demonstrates that BcBAG1 is pleiotropic and not only essential for fungal development, hyphal melanization, and virulence, but also required for response to multiple abiotic stresses and UPR pathway of  B. cinerea .

Cytoprotective Co-chaperone BcBAG1 Is a Component for Fungal Development, Virulence, and Unfolded Protein Response (UPR) of Botrytis cinerea