Evolutionary divergence of the plant elicitor peptides (Peps)

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1 Evolutionary divergence of the plant elicitor peptides (Peps) and their receptors: interfamily incompatibility of perception but compatibility of downstream signalling Item Type Article Authors Lori, M.; van Verk, M. C.; Hander, T.; Schatowitz, H.; Klauser, D.; Flury, P.; Gehring, Christoph A; Boller, T.; Bartels, S. Citation Evolutionary divergence of the plant elicitor peptides (Peps) and their receptors: interfamily incompatibility of perception but compatibility of downstream signalling 2015 Journal of Experimental Botany Eprint version Publisher's Version/PDF DOI /jxb/erv236 Publisher Oxford University Press (OUP) Journal Journal of Experimental Botany Rights This is an Open Access article distributed under the terms of the Creative Commons Attribution License ( creativecommons.org/licenses/by/3.0/), which permits unrestricted reuse, distribution, and reproduction in any medium, provided the original work is properly cited. Download date 05/07/ :38:39 Link to Item

2 Evolutionary divergence of the plant elicitor peptides (Peps) and their receptors: interfamily incompatibility of perception but compatibility of downstream signalling Martina Lori, Marcel van Verk, Tim Hander, Hendrik Schatowitz, Dominik Klauser, Pascale Flury, Chris Gehring, Thomas Boller, and Sebastian Bartels Supplemental Files Supplementary Table S3: Identity comparison of PROPEP sequences Full-length amino-acid sequences of published and novel HMMER identified PROPEP sequences were compared for the percentage of identical residues in aligned positions (upper half), and the number of identical residues in aligned positions (lower half). Colours indicate increasing amount of identity from low (blue) via white to high (red). Supplementary Table S4: Identity comparison of Pep sequences Pep amino-acid sequences deduced from published and novel HMMER identified PROPEP sequences were compared for the percentage of identical residues in aligned positions (upper half), and the number of identical residues in aligned positions (lower half). Colours indicate increasing amount of identity from low (blue) via white to high (red). Supplementary Table S5: Identity comparison of PEPR sequences Full-length amino-acid sequences of PEPR sequences were compared for the percentage of identical residues in aligned positions (upper half), and the number of identical residues in aligned positions (lower half). Colours indicate increasing amount of identity from low (blue) via white to high (red). Supplementary Table S6: Identity comparison of PEPR LRR domains The LRR domains of PEPR sequences were compared for the percentage of identical residues in aligned positions (upper half), and the number of identical residues in aligned positions (lower half). Colours indicate increasing amount of identity from low (blue) via white to high (red). Supplementary Table S7: Identity comparison of PEPR kinase domains The kinase domains of PEPR sequences were compared for the percentage of identical residues in aligned positions (upper half), and the number of identical residues in aligned positions (lower half). Colours indicate increasing amount of identity from low (blue) via white to high (red). Supplementary Figure S1: Plasticity of the Pep-PEPR-LRR interaction site Sequence alignment of the LRR region of the PEPR sequences from Figure 1B. Amino acid residues are coloured based on the conservation and interacting residues of AtPEPR1-LRR (underlined in red) as described by Tang et al., The LRR sequence of SlPEPR1 and ZmPEPR1a, used in this study, are underlined in grey. Yellow residues: conserved amino acids of AtPEPR1LRR. Magenta residues: AtPep1 interacting amino acids of AtPEPR1LRR. Below the sequence alignment the overall conservation is indicated by pink bars and a sequence logo.

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