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Evolutionary divergence of the plant elicitor peptides (Peps) and their receptors: interfamily incompatibility of perception but compatibility of downstream signalling.

Lori M, van Verk MC, Hander T, Schatowitz H, Klauser D, Flury P, Gehring CA, Boller T, Bartels S - J. Exp. Bot. (2015)

Bottom Line: Peps were not recognized by species outside of their plant family of origin, apparently because of a divergence of the Pep sequences.Three family-specific Pep motifs were defined and the integration of such a motif into the Pep sequence of an unrelated Pep enabled its perception.It was concluded that signalling machinery downstream of the PEPRs is highly conserved whereas the leucine-rich repeat domains of the PEPRs co-evolved with the Peps, leading to distinct motifs and, with it, interfamily incompatibility.

View Article: PubMed Central - PubMed

Affiliation: Zürich-Basel Plant Science Center, Department of Environmental Sciences - Botany, University of Basel, Hebelstrasse 1, CH-4056 Basel, Switzerland.

No MeSH data available.


Related in: MedlinePlus

Detection of Peps by transiently expressed PEPRs.N. benthamiana plants were transiently transformed with Agrobacteria containing pGWB517 plasmids harbouring the coding sequences of either AtPEPR1, SlPEPR1, or ZmPEPR1a (as indicated). Leaf discs were harvested one day past transformation. Columns represent averages of detected ethylene values of six biological replicates (containing three leaf discs each) 5h after treatment with the indicated peptides or without any peptide (control). Error bars show the standard error of the mean. Asterisks indicate significant differences of the labelled column to the control based on t-test results (*P < 0.05; *P < 0.01; ***P < 0.001).
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Figure 5: Detection of Peps by transiently expressed PEPRs.N. benthamiana plants were transiently transformed with Agrobacteria containing pGWB517 plasmids harbouring the coding sequences of either AtPEPR1, SlPEPR1, or ZmPEPR1a (as indicated). Leaf discs were harvested one day past transformation. Columns represent averages of detected ethylene values of six biological replicates (containing three leaf discs each) 5h after treatment with the indicated peptides or without any peptide (control). Error bars show the standard error of the mean. Asterisks indicate significant differences of the labelled column to the control based on t-test results (*P < 0.05; *P < 0.01; ***P < 0.001).

Mentions: A correlation between PEPR sequence divergence and interfamily incompatibility of the system was investigated. In the first study describing AtPEPR1, the authors used the alkalinization response of transgenic tobacco cells expressing AtPEPR1 to show that AtPEPR1 recognizes AtPep1 (Yamaguchi et al., 2006). Thus, at least AtPEPR1 functions also in tobacco cells and not just in Brassicaceae. Here, additional PEPRs were cloned and studied by introducing the coding sequences of AtPEPR1, the tomato PEPR SlPEPR1, and the maize PEPR ZmPEPR1a into the expression vector pGWB517 and transiently expressing them in N. benthamiana leaves. Again, the elevated production of ethylene was used as a read-out for the activation of PEPR signalling upon perception of Peps. Leaf tissue of N. benthamiana is naturally insensitive to AtPep1 and ZmPep1; however, when transformed with AtPEPR1 or ZmPEPR1, it responded with a strong production of ethylene (Fig. 5). Remarkably, in this assay no significant ethylene production was detected in SlPep6-treated leaf discs despite the previously noted sensitivity of wild-type N. benthamiana leaves to SlPep6 (Fig. 2 and Fig. 3B). In contrast, leaf discs transiently expressing SlPEPR1 again responded with strong ethylene production upon addition of SlPep6 (Fig. 5). This apparent discrepancy is based on the use of only three discs per replicate harvested from the transiently transformed leaves in this experiment compared to 10 discs per replicate used in the assays based on wild-type leaves. Three discs are not enough to detect the little ethylene production elicited in wild-type discs upon SlPep6 treatment but are sufficient to show the strong SlPep6-dependent production of ethylene in leaf discs transiently transformed with SlPEPR1. Thus as reported before (Flury et al., 2013), the overexpression of PEPRs boosts Pep-triggered responses.


Evolutionary divergence of the plant elicitor peptides (Peps) and their receptors: interfamily incompatibility of perception but compatibility of downstream signalling.

Lori M, van Verk MC, Hander T, Schatowitz H, Klauser D, Flury P, Gehring CA, Boller T, Bartels S - J. Exp. Bot. (2015)

Detection of Peps by transiently expressed PEPRs.N. benthamiana plants were transiently transformed with Agrobacteria containing pGWB517 plasmids harbouring the coding sequences of either AtPEPR1, SlPEPR1, or ZmPEPR1a (as indicated). Leaf discs were harvested one day past transformation. Columns represent averages of detected ethylene values of six biological replicates (containing three leaf discs each) 5h after treatment with the indicated peptides or without any peptide (control). Error bars show the standard error of the mean. Asterisks indicate significant differences of the labelled column to the control based on t-test results (*P < 0.05; *P < 0.01; ***P < 0.001).
© Copyright Policy - creative-commons
Related In: Results  -  Collection

License 1 - License 2
Show All Figures
getmorefigures.php?uid=PMC4526913&req=5

Figure 5: Detection of Peps by transiently expressed PEPRs.N. benthamiana plants were transiently transformed with Agrobacteria containing pGWB517 plasmids harbouring the coding sequences of either AtPEPR1, SlPEPR1, or ZmPEPR1a (as indicated). Leaf discs were harvested one day past transformation. Columns represent averages of detected ethylene values of six biological replicates (containing three leaf discs each) 5h after treatment with the indicated peptides or without any peptide (control). Error bars show the standard error of the mean. Asterisks indicate significant differences of the labelled column to the control based on t-test results (*P < 0.05; *P < 0.01; ***P < 0.001).
Mentions: A correlation between PEPR sequence divergence and interfamily incompatibility of the system was investigated. In the first study describing AtPEPR1, the authors used the alkalinization response of transgenic tobacco cells expressing AtPEPR1 to show that AtPEPR1 recognizes AtPep1 (Yamaguchi et al., 2006). Thus, at least AtPEPR1 functions also in tobacco cells and not just in Brassicaceae. Here, additional PEPRs were cloned and studied by introducing the coding sequences of AtPEPR1, the tomato PEPR SlPEPR1, and the maize PEPR ZmPEPR1a into the expression vector pGWB517 and transiently expressing them in N. benthamiana leaves. Again, the elevated production of ethylene was used as a read-out for the activation of PEPR signalling upon perception of Peps. Leaf tissue of N. benthamiana is naturally insensitive to AtPep1 and ZmPep1; however, when transformed with AtPEPR1 or ZmPEPR1, it responded with a strong production of ethylene (Fig. 5). Remarkably, in this assay no significant ethylene production was detected in SlPep6-treated leaf discs despite the previously noted sensitivity of wild-type N. benthamiana leaves to SlPep6 (Fig. 2 and Fig. 3B). In contrast, leaf discs transiently expressing SlPEPR1 again responded with strong ethylene production upon addition of SlPep6 (Fig. 5). This apparent discrepancy is based on the use of only three discs per replicate harvested from the transiently transformed leaves in this experiment compared to 10 discs per replicate used in the assays based on wild-type leaves. Three discs are not enough to detect the little ethylene production elicited in wild-type discs upon SlPep6 treatment but are sufficient to show the strong SlPep6-dependent production of ethylene in leaf discs transiently transformed with SlPEPR1. Thus as reported before (Flury et al., 2013), the overexpression of PEPRs boosts Pep-triggered responses.

Bottom Line: Peps were not recognized by species outside of their plant family of origin, apparently because of a divergence of the Pep sequences.Three family-specific Pep motifs were defined and the integration of such a motif into the Pep sequence of an unrelated Pep enabled its perception.It was concluded that signalling machinery downstream of the PEPRs is highly conserved whereas the leucine-rich repeat domains of the PEPRs co-evolved with the Peps, leading to distinct motifs and, with it, interfamily incompatibility.

View Article: PubMed Central - PubMed

Affiliation: Zürich-Basel Plant Science Center, Department of Environmental Sciences - Botany, University of Basel, Hebelstrasse 1, CH-4056 Basel, Switzerland.

No MeSH data available.


Related in: MedlinePlus