Abstract
RPM1 -interacting protein 4 (RIN4), a negative regulator of the basal defense response in plants, is targeted by multiple bacterial virulence effectors. We show that RIN4 degradation is induced by the effector AvrPto from Pseudomonas syringae and that this degradation in Solanaceous plants is dependent on the resistance protein, Pto, a protein kinase, and Prf, a nucleotide binding site-leucine-rich repeat protein. Our data demonstrate overlap between two of the best-characterized pathways for recognition of pathogen virulence effectors in plants. RIN4 interacts with multiple plant signaling components and bacterial effectors in yeast and in planta. AvrPto induces an endogenous proteolytic activity in both tomato [Solanum lycopersicum) and Nicotiana benthamiana that degrades RIN4 and requires the consensus site cleaved by the protease effector AvrRpt2. The interaction between AvrPto and Pto, but not the kinase activity of Pto, is required for proteolysis of RIN4. Analysis of many of the effectors comprising the secretome of P. syringae pv tomato DC3000 led to the identification of two additional sequence-unrelated effectors that can also induce degradation of RIN4. Therefore, multiple bacterial effectors besides AvrRpt2 elicit proteolysis of RIN4 in planta.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 2458-2472 |
| Number of pages | 15 |
| Journal | Plant Cell |
| Volume | 21 |
| Issue number | 8 |
| DOIs | |
| State | Published - Aug 2009 |
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ASJC Scopus subject areas
- Plant Science
- Cell Biology
Cite this
Proteolysis of a negative regulator of innate immunity is dependent on resistance genes in tomato and nicotiana benthamiana and induced by multiple bacterial effectors. / Luo, Yao; Caldwell, Katherine S.; Wroblewski, Tadeusz; Wright, Michael E.; Michelmore, Richard W.
In: Plant Cell, Vol. 21, No. 8, 08.2009, p. 2458-2472.Research output: Contribution to journal › Article
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TY - JOUR
T1 - Proteolysis of a negative regulator of innate immunity is dependent on resistance genes in tomato and nicotiana benthamiana and induced by multiple bacterial effectors
AU - Luo, Yao
AU - Caldwell, Katherine S.
AU - Wroblewski, Tadeusz
AU - Wright, Michael E.
AU - Michelmore, Richard W
PY - 2009/8
Y1 - 2009/8
N2 - RPM1 -interacting protein 4 (RIN4), a negative regulator of the basal defense response in plants, is targeted by multiple bacterial virulence effectors. We show that RIN4 degradation is induced by the effector AvrPto from Pseudomonas syringae and that this degradation in Solanaceous plants is dependent on the resistance protein, Pto, a protein kinase, and Prf, a nucleotide binding site-leucine-rich repeat protein. Our data demonstrate overlap between two of the best-characterized pathways for recognition of pathogen virulence effectors in plants. RIN4 interacts with multiple plant signaling components and bacterial effectors in yeast and in planta. AvrPto induces an endogenous proteolytic activity in both tomato [Solanum lycopersicum) and Nicotiana benthamiana that degrades RIN4 and requires the consensus site cleaved by the protease effector AvrRpt2. The interaction between AvrPto and Pto, but not the kinase activity of Pto, is required for proteolysis of RIN4. Analysis of many of the effectors comprising the secretome of P. syringae pv tomato DC3000 led to the identification of two additional sequence-unrelated effectors that can also induce degradation of RIN4. Therefore, multiple bacterial effectors besides AvrRpt2 elicit proteolysis of RIN4 in planta.
AB - RPM1 -interacting protein 4 (RIN4), a negative regulator of the basal defense response in plants, is targeted by multiple bacterial virulence effectors. We show that RIN4 degradation is induced by the effector AvrPto from Pseudomonas syringae and that this degradation in Solanaceous plants is dependent on the resistance protein, Pto, a protein kinase, and Prf, a nucleotide binding site-leucine-rich repeat protein. Our data demonstrate overlap between two of the best-characterized pathways for recognition of pathogen virulence effectors in plants. RIN4 interacts with multiple plant signaling components and bacterial effectors in yeast and in planta. AvrPto induces an endogenous proteolytic activity in both tomato [Solanum lycopersicum) and Nicotiana benthamiana that degrades RIN4 and requires the consensus site cleaved by the protease effector AvrRpt2. The interaction between AvrPto and Pto, but not the kinase activity of Pto, is required for proteolysis of RIN4. Analysis of many of the effectors comprising the secretome of P. syringae pv tomato DC3000 led to the identification of two additional sequence-unrelated effectors that can also induce degradation of RIN4. Therefore, multiple bacterial effectors besides AvrRpt2 elicit proteolysis of RIN4 in planta.
UR - http://www.scopus.com/inward/record.url?scp=70349656645&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=70349656645&partnerID=8YFLogxK
U2 - 10.1105/tpc.107.056044
DO - 10.1105/tpc.107.056044
M3 - Article
C2 - 19671880
AN - SCOPUS:70349656645
VL - 21
SP - 2458
EP - 2472
JO - Plant Cell
JF - Plant Cell
SN - 1040-4651
IS - 8
ER -