Unknown

Dataset Information

0

Site-specific cleavage of bacterial MucD by secreted proteases mediates antibacterial resistance in Arabidopsis.


ABSTRACT: Plant innate immunity restricts growth of bacterial pathogens that threaten global food security. However, the mechanisms by which plant immunity suppresses bacterial growth remain enigmatic. Here we show that Arabidopsis thaliana secreted aspartic protease 1 and 2 (SAP1 and SAP2) cleave the evolutionarily conserved bacterial protein MucD to redundantly inhibit the growth of the bacterial pathogen Pseudomonas syringae. Antibacterial activity of SAP1 requires its protease activity in planta and in vitro. Plants overexpressing SAP1 exhibit enhanced MucD cleavage and resistance but incur no penalties in growth and reproduction, while sap1 sap2 double mutant plants exhibit compromised MucD cleavage and resistance against P. syringae. P. syringae lacking mucD shows compromised growth in planta and in vitro. Notably, growth of ?mucD complemented with the non-cleavable MucDF106Y is not affected by SAP activity in planta and in vitro. Our findings identify the genetic factors and biochemical process underlying an antibacterial mechanism in plants.

SUBMITTER: Wang Y 

PROVIDER: S-EPMC6599210 | biostudies-literature | 2019 Jun

REPOSITORIES: biostudies-literature

altmetric image

Publications

Site-specific cleavage of bacterial MucD by secreted proteases mediates antibacterial resistance in Arabidopsis.

Wang Yiming Y   Garrido-Oter Ruben R   Wu Jingni J   Winkelmüller Thomas M TM   Agler Matthew M   Colby Thomas T   Nobori Tatsuya T   Kemen Eric E   Tsuda Kenichi K  

Nature communications 20190628 1


Plant innate immunity restricts growth of bacterial pathogens that threaten global food security. However, the mechanisms by which plant immunity suppresses bacterial growth remain enigmatic. Here we show that Arabidopsis thaliana secreted aspartic protease 1 and 2 (SAP1 and SAP2) cleave the evolutionarily conserved bacterial protein MucD to redundantly inhibit the growth of the bacterial pathogen Pseudomonas syringae. Antibacterial activity of SAP1 requires its protease activity in planta and i  ...[more]

Similar Datasets

| S-EPMC6638631 | biostudies-literature
| S-EPMC5805785 | biostudies-literature
| S-EPMC3656315 | biostudies-literature
| S-EPMC6649664 | biostudies-literature
| S-EPMC7180472 | biostudies-literature
| S-EPMC3871983 | biostudies-literature
| S-EPMC5041906 | biostudies-literature
| S-EPMC2663817 | biostudies-literature
| S-EPMC3107323 | biostudies-literature
| S-EPMC2566267 | biostudies-literature