Perception of the bacterial PAMP EF-Tu by the receptor EFR restricts Agrobacterium-mediated transformation.
Higher eukaryotes sense microbes through the perception of pathogen-associated molecular patterns (PAMPs). Arabidopsis plants detect a variety of PAMPs including conserved domains of bacterial flagellin and of bacterial EF-Tu. Here, we show that flagellin and EF-Tu activate a common set of signaling events and defense responses but without clear synergistic effects. Treatment with either PAMP results in increased binding sites for both PAMPs. We used this finding in a targeted reverse-genetic approach to identify a receptor kinase essential for EF-Tu perception, which we called EFR. Nicotiana benthamiana, a plant unable to perceive EF-Tu, acquires EF-Tu binding sites and responsiveness upon transient expression of EFR. Arabidopsis efr mutants show enhanced susceptibility to the bacterium Agrobacterium tumefaciens, as revealed by a higher efficiency of T-DNA transformation. These results demonstrate that EFR is the EF-Tu receptor and that plant defense responses induced by PAMPs such as EF-Tu reduce transformation by Agrobacterium.
Zipfel
Cyril
C
Botanical Institute, Zurich-Basel Plant Science Centre, University of Basel, Hebelstrasse 1, CH-4056 Basel, Switzerland. cyril.zipfel@sainsbury-laboratory.ac.uk
Kunze
Gernot
G
Chinchilla
Delphine
D
Caniard
Anne
A
Jones
Jonathan D G
JD
Boller
Thomas
T
Felix
Georg
G
D016960:Agrobacterium tumefaciens / Q000378:metabolism*; D000595:Amino Acid Sequence; D017360:Arabidopsis / Q000166:cytology / Q000235:genetics / Q000382:microbiology / Q000502:physiology; D029681:Arabidopsis Proteins / Q000235:genetics / Q000378:metabolism*; D001426:Bacterial Proteins / Q000235:genetics / Q000378:metabolism*; D001665:Binding Sites; D005408:Flagellin / Q000378:metabolism; D018506:Gene Expression Regulation, Plant; D008969:Molecular Sequence Data; D009154:Mutation; D010444:Peptide Elongation Factor Tu / Q000235:genetics / Q000378:metabolism*; D011494:Protein Kinases / Q000235:genetics / Q000378:metabolism*; D011956:Receptors, Cell Surface / Q000235:genetics / Q000378:metabolism*; D016415:Sequence Alignment; D015398:Signal Transduction / Q000502:physiology*; D014026:Nicotiana / Q000166:cytology / Q000382:microbiology / Q000502:physiology; D014158:Transcription, Genetic; D014170:Transformation, Genetic
D029681:Arabidopsis Proteins; D001426:Bacterial Proteins; D011956:Receptors, Cell Surface; D005408:Flagellin; D011494:Protein Kinases; D010444:Peptide Elongation Factor Tu