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Pseudomonas effector AvrB is a glycosyltransferase that rhamnosylates plant guardee protein RIN4.


ABSTRACT: The plant pathogen Pseudomonas syringae encodes a type III secretion system avirulence effector protein, AvrB, that induces a form of programmed cell death called the hypersensitive response in plants as a defense mechanism against systemic infection. Despite the well-documented catalytic activities observed in other Fido (Fic, Doc, and AvrB) proteins, the enzymatic activity and target substrates of AvrB have remained elusive. Here, we show that AvrB is an unprecedented glycosyltransferase that transfers rhamnose from UDP-rhamnose to a threonine residue of the Arabidopsis guardee protein RIN4. We report structures of various enzymatic states of the AvrB-catalyzed rhamnosylation reaction of RIN4, which reveal the structural and mechanistic basis for rhamnosylation by a Fido protein. Collectively, our results uncover an unexpected reaction performed by a prototypical member of the Fido superfamily while providing important insights into the plant hypersensitive response pathway and foreshadowing more diverse chemistry used by Fido proteins and their substrates.

SUBMITTER: Peng W 

PROVIDER: S-EPMC10866546 | biostudies-literature | 2024 Feb

REPOSITORIES: biostudies-literature

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<i>Pseudomonas</i> effector AvrB is a glycosyltransferase that rhamnosylates plant guardee protein RIN4.

Peng Wei W   Garcia Nalleli N   Servage Kelly A KA   Kohler Jennifer J JJ   Ready Joseph M JM   Tomchick Diana R DR   Fernandez Jessie J   Orth Kim K  

Science advances 20240214 7


The plant pathogen <i>Pseudomonas syringae</i> encodes a type III secretion system avirulence effector protein, AvrB, that induces a form of programmed cell death called the hypersensitive response in plants as a defense mechanism against systemic infection. Despite the well-documented catalytic activities observed in other Fido (<u>Fi</u>c, <u>Do</u>c, and AvrB) proteins, the enzymatic activity and target substrates of AvrB have remained elusive. Here, we show that AvrB is an unprecedented glyc  ...[more]

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