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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

Bootstrapped neighbour-joining tree of PROPEP and PEPR sequences. (A) Full-length amino-acid sequences of published and novel HMMER identified PROPEP sequences were used to build a bootstrapped neighbour-joining tree. PROPEPs in red highlight PROPEPs of which the respective Pep was shown to be an active elicitor in this study. Asterisks mark PROPEPs of which the respective Pep was shown in previous studies to be an active elicitor. Major families are highlighted with colours according to the legend. Scale-bar: amino-acid substitutions per site. (B) Full-length amino-acid sequences of PEPR sequences were used to build a bootstrapped neighbour-joining tree. Major families are highlighted with colours according to the legend. Scale-bar: amino-acid substitutions per site.
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Figure 1: Bootstrapped neighbour-joining tree of PROPEP and PEPR sequences. (A) Full-length amino-acid sequences of published and novel HMMER identified PROPEP sequences were used to build a bootstrapped neighbour-joining tree. PROPEPs in red highlight PROPEPs of which the respective Pep was shown to be an active elicitor in this study. Asterisks mark PROPEPs of which the respective Pep was shown in previous studies to be an active elicitor. Major families are highlighted with colours according to the legend. Scale-bar: amino-acid substitutions per site. (B) Full-length amino-acid sequences of PEPR sequences were used to build a bootstrapped neighbour-joining tree. Major families are highlighted with colours according to the legend. Scale-bar: amino-acid substitutions per site.

Mentions: The structure and function of the Pep-PEPR system has been studied mainly in the model plants A. thaliana and Z. mays (Huffaker et al., 2006; Krol et al., 2010; Yamaguchi et al., 2010; Huffaker et al., 2011; Bartels et al., 2013). However, already in the earliest of these publications was the suggestion that PROPEPs might be present in a couple of plant species and not limited to Arabidopsis (Huffaker et al., 2006). Here, an extensive sequence search in public databases using the few previously described PROPEP sequences as well as the sequences of the hitherto only known PEPRs, AtPEPR1 and AtPEPR2, identified a large number of novel PROPEPs and PEPRs (Supplementary Table S2). Figure 1 shows the phylogenetic trees of all PROPEPs (Fig. 1A) and PEPRs (Fig. 1B). PROPEPs form plant family–specific clusters, for example AtPROPEP1 clusters primarily with most Brassicaceae PROPEPs and not with PROPEP1 orthologues of distantly related plant species. A sequence comparison of all identified PROPEPs found an astonishingly small sequence identity between PROPEPs (Supplementary Table S3). For example the orthologues AtPROPEP1/ZmPROPEP1 and AtPROPEP3/ZmPROPEP3, which have been linked to fungal and herbivore resistance, respectively (Huffaker et al., 2006; Huffaker et al., 2011; Huffaker et al., 2013; Liu et al., 2013; Klauser et al., 2015), show as little as 5.5% and 5.3% identical amino acids, respectively. In general, a large number of PROPEPs show less than 10% identical amino acids compared to other PROPEPs. Only within family-specific clusters and subclusters inside the Brassicaceae sequence identity ranged above 50% (Supplementary Table S3). It has been proposed that the PROPEP C-terminal end containing the Pep sequence is more strictly conserved (Huffaker et al., 2006; Pearce et al., 2008). However, a comparison of AtPep1 and ZmPep1, the first plant ortholog reported, revealed only a Pep-sequence identity of 20.8%; this is a typical value for the sequence conservation of Peps in general (Supplementary Table S4). It is slightly higher than the typical value for PROPEPs but still too low to support the idea that whole Pep sequences are strictly conserved over the whole structure. Notably, the sequence identity of Peps within a cluster, even as large as the one of the Poaceae Peps, ranged from 43.5% to 100% (Supplementary Table S4).


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)

Bootstrapped neighbour-joining tree of PROPEP and PEPR sequences. (A) Full-length amino-acid sequences of published and novel HMMER identified PROPEP sequences were used to build a bootstrapped neighbour-joining tree. PROPEPs in red highlight PROPEPs of which the respective Pep was shown to be an active elicitor in this study. Asterisks mark PROPEPs of which the respective Pep was shown in previous studies to be an active elicitor. Major families are highlighted with colours according to the legend. Scale-bar: amino-acid substitutions per site. (B) Full-length amino-acid sequences of PEPR sequences were used to build a bootstrapped neighbour-joining tree. Major families are highlighted with colours according to the legend. Scale-bar: amino-acid substitutions per site.
© Copyright Policy - creative-commons
Related In: Results  -  Collection

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

Figure 1: Bootstrapped neighbour-joining tree of PROPEP and PEPR sequences. (A) Full-length amino-acid sequences of published and novel HMMER identified PROPEP sequences were used to build a bootstrapped neighbour-joining tree. PROPEPs in red highlight PROPEPs of which the respective Pep was shown to be an active elicitor in this study. Asterisks mark PROPEPs of which the respective Pep was shown in previous studies to be an active elicitor. Major families are highlighted with colours according to the legend. Scale-bar: amino-acid substitutions per site. (B) Full-length amino-acid sequences of PEPR sequences were used to build a bootstrapped neighbour-joining tree. Major families are highlighted with colours according to the legend. Scale-bar: amino-acid substitutions per site.
Mentions: The structure and function of the Pep-PEPR system has been studied mainly in the model plants A. thaliana and Z. mays (Huffaker et al., 2006; Krol et al., 2010; Yamaguchi et al., 2010; Huffaker et al., 2011; Bartels et al., 2013). However, already in the earliest of these publications was the suggestion that PROPEPs might be present in a couple of plant species and not limited to Arabidopsis (Huffaker et al., 2006). Here, an extensive sequence search in public databases using the few previously described PROPEP sequences as well as the sequences of the hitherto only known PEPRs, AtPEPR1 and AtPEPR2, identified a large number of novel PROPEPs and PEPRs (Supplementary Table S2). Figure 1 shows the phylogenetic trees of all PROPEPs (Fig. 1A) and PEPRs (Fig. 1B). PROPEPs form plant family–specific clusters, for example AtPROPEP1 clusters primarily with most Brassicaceae PROPEPs and not with PROPEP1 orthologues of distantly related plant species. A sequence comparison of all identified PROPEPs found an astonishingly small sequence identity between PROPEPs (Supplementary Table S3). For example the orthologues AtPROPEP1/ZmPROPEP1 and AtPROPEP3/ZmPROPEP3, which have been linked to fungal and herbivore resistance, respectively (Huffaker et al., 2006; Huffaker et al., 2011; Huffaker et al., 2013; Liu et al., 2013; Klauser et al., 2015), show as little as 5.5% and 5.3% identical amino acids, respectively. In general, a large number of PROPEPs show less than 10% identical amino acids compared to other PROPEPs. Only within family-specific clusters and subclusters inside the Brassicaceae sequence identity ranged above 50% (Supplementary Table S3). It has been proposed that the PROPEP C-terminal end containing the Pep sequence is more strictly conserved (Huffaker et al., 2006; Pearce et al., 2008). However, a comparison of AtPep1 and ZmPep1, the first plant ortholog reported, revealed only a Pep-sequence identity of 20.8%; this is a typical value for the sequence conservation of Peps in general (Supplementary Table S4). It is slightly higher than the typical value for PROPEPs but still too low to support the idea that whole Pep sequences are strictly conserved over the whole structure. Notably, the sequence identity of Peps within a cluster, even as large as the one of the Poaceae Peps, ranged from 43.5% to 100% (Supplementary Table S4).

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