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Maize EMBRYO SAC family peptides interact differentially with pollen tubes and fungal cells

EMBRYO SAC1-4 (ES1-4) peptides belong to the defensin subgroup of cysteine-rich peptides known to mediate pollen tube burst in Zea mays (maize). ES1-4 are reported here to also be capable of inhibiting germination and growth of the maize fungal pathogens Fusarium graminearum and Ustilago maydis at h...

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Autores principales: Woriedh, Mayada, Merkl, Rainer, Dresselhaus, Thomas
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Oxford University Press 2015
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4526917/
https://www.ncbi.nlm.nih.gov/pubmed/26071527
http://dx.doi.org/10.1093/jxb/erv268
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author Woriedh, Mayada
Merkl, Rainer
Dresselhaus, Thomas
author_facet Woriedh, Mayada
Merkl, Rainer
Dresselhaus, Thomas
author_sort Woriedh, Mayada
collection PubMed
description EMBRYO SAC1-4 (ES1-4) peptides belong to the defensin subgroup of cysteine-rich peptides known to mediate pollen tube burst in Zea mays (maize). ES1-4 are reported here to also be capable of inhibiting germination and growth of the maize fungal pathogens Fusarium graminearum and Ustilago maydis at higher concentrations. Dividing the peptides into smaller pieces showed that a 15-amino-acid peptide located in a highly variable loop region lacking similarity to other defensins or defensin-like peptides binds to maize pollen tube surfaces, causing swelling prior to burst. This peptide fragment and a second conserved neighbouring fragment showed suppression of fungal germination and growth. The two peptides caused swelling of fungal cells, production of reactive oxygen species, and finally the formation of big vacuoles prior to burst at high peptide concentration. Furthermore, peptide fragments were found to bind differently to fungal cells. In necrotrophic F. graminearum, a peptide fragment named ES-d bound only at cell surfaces whereas the peptide ES-c bound at cell surfaces and also accumulated inside cells. Conversely, in biotrophic U. maydis, both peptide fragments accumulated inside cells, but, if applied at higher concentration, ES-c but not ES-d accumulated mainly in vacuoles. Mapping of peptide interaction sites identified amino acids differing in pollen tube burst and fungal response reactions. In summary, these findings indicate that residues targeting pollen tube burst in maize are specific to the ES family, while residues targeting fungal growth are conserved within defensins and defensin-like peptides.
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spelling pubmed-45269172015-08-10 Maize EMBRYO SAC family peptides interact differentially with pollen tubes and fungal cells Woriedh, Mayada Merkl, Rainer Dresselhaus, Thomas J Exp Bot Research Paper EMBRYO SAC1-4 (ES1-4) peptides belong to the defensin subgroup of cysteine-rich peptides known to mediate pollen tube burst in Zea mays (maize). ES1-4 are reported here to also be capable of inhibiting germination and growth of the maize fungal pathogens Fusarium graminearum and Ustilago maydis at higher concentrations. Dividing the peptides into smaller pieces showed that a 15-amino-acid peptide located in a highly variable loop region lacking similarity to other defensins or defensin-like peptides binds to maize pollen tube surfaces, causing swelling prior to burst. This peptide fragment and a second conserved neighbouring fragment showed suppression of fungal germination and growth. The two peptides caused swelling of fungal cells, production of reactive oxygen species, and finally the formation of big vacuoles prior to burst at high peptide concentration. Furthermore, peptide fragments were found to bind differently to fungal cells. In necrotrophic F. graminearum, a peptide fragment named ES-d bound only at cell surfaces whereas the peptide ES-c bound at cell surfaces and also accumulated inside cells. Conversely, in biotrophic U. maydis, both peptide fragments accumulated inside cells, but, if applied at higher concentration, ES-c but not ES-d accumulated mainly in vacuoles. Mapping of peptide interaction sites identified amino acids differing in pollen tube burst and fungal response reactions. In summary, these findings indicate that residues targeting pollen tube burst in maize are specific to the ES family, while residues targeting fungal growth are conserved within defensins and defensin-like peptides. Oxford University Press 2015-08 2015-06-12 /pmc/articles/PMC4526917/ /pubmed/26071527 http://dx.doi.org/10.1093/jxb/erv268 Text en © The Author 2015. Published by Oxford University Press on behalf of the Society for Experimental Biology. http://creativecommons.org/licenses/by/3.0 This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/3.0/), which permits unrestricted reuse, distribution, and reproduction in any medium, provided the original work is properly cited.
spellingShingle Research Paper
Woriedh, Mayada
Merkl, Rainer
Dresselhaus, Thomas
Maize EMBRYO SAC family peptides interact differentially with pollen tubes and fungal cells
title Maize EMBRYO SAC family peptides interact differentially with pollen tubes and fungal cells
title_full Maize EMBRYO SAC family peptides interact differentially with pollen tubes and fungal cells
title_fullStr Maize EMBRYO SAC family peptides interact differentially with pollen tubes and fungal cells
title_full_unstemmed Maize EMBRYO SAC family peptides interact differentially with pollen tubes and fungal cells
title_short Maize EMBRYO SAC family peptides interact differentially with pollen tubes and fungal cells
title_sort maize embryo sac family peptides interact differentially with pollen tubes and fungal cells
topic Research Paper
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4526917/
https://www.ncbi.nlm.nih.gov/pubmed/26071527
http://dx.doi.org/10.1093/jxb/erv268
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