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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

Identification of family-specific Pep motifs. (A–C) Ten leaf discs of indicated plant species were treated for 5h with 1 µM of the indicated elicitor peptides or without any peptide (control). Columns represent averages of detected ethylene values of five biological replicates normalized to the ethylene response triggered by flg22 (set to 100%). Error bars show the normalized 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). (D) Depiction of the consensus sequences of aligned Brassicaceae-, Solanaceae-, and Poaceae-specific Pep sequences (from A–C) using the WebLogo tool (Crooks et al., 2004).
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Figure 3: Identification of family-specific Pep motifs. (A–C) Ten leaf discs of indicated plant species were treated for 5h with 1 µM of the indicated elicitor peptides or without any peptide (control). Columns represent averages of detected ethylene values of five biological replicates normalized to the ethylene response triggered by flg22 (set to 100%). Error bars show the normalized 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). (D) Depiction of the consensus sequences of aligned Brassicaceae-, Solanaceae-, and Poaceae-specific Pep sequences (from A–C) using the WebLogo tool (Crooks et al., 2004).

Mentions: The peptides SlPep6 and ZmPep1 used in Fig. 2 do not conform to this rule. SlPep6 contains a glycine at position 15 instead of a serine and ZmPep1 shows a histidine at the terminal position 23 instead of an asparagine. This might explain why they were not recognized by the Brassicaceae. In order to identify plant family-specific motifs, a larger number of family-specific peptides were tested and consensus sequences derived. Fig. 3A shows the recognition of all eight AtPeps and two BrPeps from B. rapa by Arabidopsis and B. rapa. In Fig. 3B, a similar experiment is shown using four peptides from Solanaceae together with S. lycopersicum and N. benthamiana. Fig. 3C shows six peptides from Poaceae tested using Z. mays and L. perenne. Consistently, the collection of family-specific peptides triggered a significant induction of ethylene production, indicating that these peptides were perceived by the respective species. This indicates that the Peps derived from the newly identified PROPEPs are indeed active Peps and that all peptides related to a plant family are recognized by (at least two) species from this plant family. Given these findings, the Pep sequences were used to build a weblogo for the visualization of the consensus sequence of each peptide group (Fig. 3D). It shows that each family has evolved distinct and specific Pep motifs. For example, in the Brassicaceae-specific sequence there is only one partially conserved proline, whereas proline residues seem to play an important role in the sequence of Peps from Solanaceae, and the Poaceae-specific consensus sequence is rich in glycine residues and conserved histidine residues at the terminal end of the peptides.


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)

Identification of family-specific Pep motifs. (A–C) Ten leaf discs of indicated plant species were treated for 5h with 1 µM of the indicated elicitor peptides or without any peptide (control). Columns represent averages of detected ethylene values of five biological replicates normalized to the ethylene response triggered by flg22 (set to 100%). Error bars show the normalized 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). (D) Depiction of the consensus sequences of aligned Brassicaceae-, Solanaceae-, and Poaceae-specific Pep sequences (from A–C) using the WebLogo tool (Crooks et al., 2004).
© Copyright Policy - creative-commons
Related In: Results  -  Collection

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

Figure 3: Identification of family-specific Pep motifs. (A–C) Ten leaf discs of indicated plant species were treated for 5h with 1 µM of the indicated elicitor peptides or without any peptide (control). Columns represent averages of detected ethylene values of five biological replicates normalized to the ethylene response triggered by flg22 (set to 100%). Error bars show the normalized 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). (D) Depiction of the consensus sequences of aligned Brassicaceae-, Solanaceae-, and Poaceae-specific Pep sequences (from A–C) using the WebLogo tool (Crooks et al., 2004).
Mentions: The peptides SlPep6 and ZmPep1 used in Fig. 2 do not conform to this rule. SlPep6 contains a glycine at position 15 instead of a serine and ZmPep1 shows a histidine at the terminal position 23 instead of an asparagine. This might explain why they were not recognized by the Brassicaceae. In order to identify plant family-specific motifs, a larger number of family-specific peptides were tested and consensus sequences derived. Fig. 3A shows the recognition of all eight AtPeps and two BrPeps from B. rapa by Arabidopsis and B. rapa. In Fig. 3B, a similar experiment is shown using four peptides from Solanaceae together with S. lycopersicum and N. benthamiana. Fig. 3C shows six peptides from Poaceae tested using Z. mays and L. perenne. Consistently, the collection of family-specific peptides triggered a significant induction of ethylene production, indicating that these peptides were perceived by the respective species. This indicates that the Peps derived from the newly identified PROPEPs are indeed active Peps and that all peptides related to a plant family are recognized by (at least two) species from this plant family. Given these findings, the Pep sequences were used to build a weblogo for the visualization of the consensus sequence of each peptide group (Fig. 3D). It shows that each family has evolved distinct and specific Pep motifs. For example, in the Brassicaceae-specific sequence there is only one partially conserved proline, whereas proline residues seem to play an important role in the sequence of Peps from Solanaceae, and the Poaceae-specific consensus sequence is rich in glycine residues and conserved histidine residues at the terminal end of the peptides.

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