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A Xanthomonas uridine 5′-monophosphate transferase inhibits plant immune kinases
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Journal Article
A Xanthomonas uridine 5′-monophosphate transferase inhibits plant immune kinases
2012
Overview
The plant pathogen
Xanthomonas campestris
effector, AvrAC, is shown to have uridine 5′-monophosphate transferase activity, enabling it to interfere with plant immune signalling by using this protein modification.
Black-rot pathogen targets plant immunity
The bacterium
Xanthomonas campestris,
which causes black rot disease in many types of brassica, translocates a number of effectors into the host cells to promote infection. This study shows that the
X. campestris
effector protein AvrAC inhibits plant immunity by specifically targeting BIK1 and RIPK, two receptor-like cytoplasmic kinases known to mediate immune signalling in
Arabidopsis
. AvrAC acts as a UMP transferase, targeting BIK1 and RIPK at sites where phosphorylation normally occurs.
Plant innate immunity is activated on the detection of pathogen-associated molecular patterns (PAMPs) at the cell surface, or of pathogen effector proteins inside the plant cell
1
,
2
,
3
,
4
. Together, PAMP-triggered immunity and effector-triggered immunity constitute powerful defences against various phytopathogens. Pathogenic bacteria inject a variety of effector proteins into the host cell to assist infection or propagation. A number of effector proteins have been shown to inhibit plant immunity
5
, but the biochemical basis remains unknown for the vast majority of these effectors. Here we show that the
Xanthomonas campestris
pathovar
campestris
type III effector AvrAC enhances virulence and inhibits plant immunity by specifically targeting
Arabidopsis
BIK1 and RIPK, two receptor-like cytoplasmic kinases known to mediate immune signalling
6
,
7
,
8
. AvrAC is a uridylyl transferase that adds uridine 5′-monophosphate to and conceals conserved phosphorylation sites in the activation loop of BIK1 and RIPK, reducing their kinase activity and consequently inhibiting downstream signalling.
Publisher
Nature Publishing Group UK,Nature Publishing Group
Subject
/ Arabidopsis Proteins - antagonists & inhibitors
/ Arabidopsis Proteins - chemistry
/ Arabidopsis Proteins - immunology
/ Arabidopsis Proteins - metabolism
/ Bacteria
/ Bacterial Proteins - metabolism
/ Biological and medical sciences
/ Fundamental and applied biological sciences. Psychology
/ Humanities and Social Sciences
/ Kinases
/ letter
/ Phytopathology. Animal pests. Plant and forest protection
/ Plant Diseases - microbiology
/ Plants, Genetically Modified
/ Protein Kinases - immunology
/ Protein Kinases - metabolism
/ Protein-Serine-Threonine Kinases - antagonists & inhibitors
/ Protein-Serine-Threonine Kinases - chemistry
/ Protein-Serine-Threonine Kinases - immunology
/ Protein-Serine-Threonine Kinases - metabolism
/ Proteins
/ Science
/ Xanthomonas campestris - enzymology
