AvrRpm1 Functions as an ADP-Ribosyl Transferase to Modify NOI-domain Containing Proteins, Including Arabidopsis and Soybean RPM1-interacting Protein 4.

Autor:	Redditt TJ; Indiana University CITY: Bloomington STATE: IN United States Of America [US]., Chung EH; University of North Carolina CITY: Chappel Hill STATE: NC United States Of America [US]., Zand Karimi H; Indiana University CITY: Bloomington STATE: Indiana United States Of America [US]., Rodibaugh N; Indiana University CITY: Bloomington STATE: IN United States Of America [US]., Zhang Y; Indiana University CITY: Bloomington STATE: IN United States Of America [US]., Trinidad JC; Indiana University CITY: Bloomington STATE: IN United States Of America [US]., Kim JH; Center for Plant Aging Research, Institute for Basic Science (IBS) CITY: Daegu Korea (South), Republic Of., Zhou Q; Ohio State University CITY: Columbus STATE: OH United States Of America [US]., Shen M; Gyeongsang National University CITY: Jinju Korea (South), Republic Of., Dangl JL; University of North Carolina CITY: Chapel Hill STATE: North Carolina POSTAL_CODE: 27599-3280 United States Of America [US]., Mackey DM; Ohio State University CITY: Columbus STATE: Ohio POSTAL_CODE: 43210 United States Of America [US]., Innes RW; Indiana University CITY: Bloomington STATE: Indiana POSTAL_CODE: 47405-7107 United States Of America [US] rinnes@indiana.edu.
Jazyk:	angličtina
Zdroj:	The Plant cell [Plant Cell] 2019 Sep 23. Date of Electronic Publication: 2019 Sep 23.
DOI:	10.1105/tpc.19.00020
Abstrakt:	The Pseudomonas syringae effector protein AvrRpm1 activates the Arabidopsis intracellular innate immune receptor protein RPM1 via modification of a second Arabidopsis protein, RIN4. Prior work has shown that AvrRpm1 induces phosphorylation of AtRIN4, but homology modeling indicated that AvrRpm1 may be an ADP-ribosyl transferase. Here we show that AvrRpm1 induces ADP-ribosylation of RIN4 proteins from both Arabidopsis and soybean within two highly conserved nitrate-induced (NOI) domains. It also ADP-ribosylates at least ten additional Arabidopsis NOI domain-containing proteins. The ADP-ribosylation activity of AvrRpm1 is required for subsequent phosphorylation on threonine 166 of Arabidopsis RIN4, an event that is necessary and sufficient for RPM1 activation. We also show that the C-terminal NOI domain of AtRIN4 interacts with the exocyst subunits EXO70B1, EXO70E1, EXO70E2 and EXO70F1. Mutation of either EXO70B1 or EXO70E2 inhibited secretion of callose induced by the bacterial flagellin-derived peptide flg22. Substitution of RIN4 threonine 166 with aspartate enhanced the association of AtRIN4 with EXO70E2, which we posit inhibits its callose deposition function. Collectively, these data indicate that AvrRpm1 ADP-ribosyl transferase activity contributes to virulence by promoting phosphorylation of RIN4 threonine 166, which inhibits the secretion of defense compounds by promoting the inhibitory association of RIN4 with EXO70 proteins. (© 2019 American Society of Plant Biologists. All rights reserved.)
Databáze:	MEDLINE
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