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Antagonistic peptide technology for functional dissection of CLE peptides revisited

In the Arabidopsis thaliana genome, over 1000 putative genes encoding small, presumably secreted, signalling peptides can be recognized. However, a major obstacle in identifying the function of genes encoding small signalling peptides is the limited number of available loss-of-function mutants. To o...

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Autores principales: Czyzewicz, Nathan, Wildhagen, Mari, Cattaneo, Pietro, Stahl, Yvonne, Pinto, Karine Gustavo, Aalen, Reidunn B., Butenko, Melinka A., Simon, Rüdiger, Hardtke, Christian S., De Smet, Ive
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Oxford University Press 2015
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4526918/
https://www.ncbi.nlm.nih.gov/pubmed/26136270
http://dx.doi.org/10.1093/jxb/erv284
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author Czyzewicz, Nathan
Wildhagen, Mari
Cattaneo, Pietro
Stahl, Yvonne
Pinto, Karine Gustavo
Aalen, Reidunn B.
Butenko, Melinka A.
Simon, Rüdiger
Hardtke, Christian S.
De Smet, Ive
author_facet Czyzewicz, Nathan
Wildhagen, Mari
Cattaneo, Pietro
Stahl, Yvonne
Pinto, Karine Gustavo
Aalen, Reidunn B.
Butenko, Melinka A.
Simon, Rüdiger
Hardtke, Christian S.
De Smet, Ive
author_sort Czyzewicz, Nathan
collection PubMed
description In the Arabidopsis thaliana genome, over 1000 putative genes encoding small, presumably secreted, signalling peptides can be recognized. However, a major obstacle in identifying the function of genes encoding small signalling peptides is the limited number of available loss-of-function mutants. To overcome this, a promising new tool, antagonistic peptide technology, was recently developed. Here, this antagonistic peptide technology was tested on selected CLE peptides and the related IDA peptide and its usefulness in the context of studies of peptide function discussed. Based on the analyses, it was concluded that the antagonistic peptide approach is not the ultimate means to overcome redundancy or lack of loss-of-function lines. However, information collected using antagonistic peptide approaches (in the broad sense) can be very useful, but these approaches do not work in all cases and require a deep insight on the interaction between the ligand and its receptor to be successful. This, as well as peptide ligand structure considerations, should be taken into account before ordering a wide range of synthetic peptide variants and/or generating transgenic plants.
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spelling pubmed-45269182015-08-10 Antagonistic peptide technology for functional dissection of CLE peptides revisited Czyzewicz, Nathan Wildhagen, Mari Cattaneo, Pietro Stahl, Yvonne Pinto, Karine Gustavo Aalen, Reidunn B. Butenko, Melinka A. Simon, Rüdiger Hardtke, Christian S. De Smet, Ive J Exp Bot Research Paper In the Arabidopsis thaliana genome, over 1000 putative genes encoding small, presumably secreted, signalling peptides can be recognized. However, a major obstacle in identifying the function of genes encoding small signalling peptides is the limited number of available loss-of-function mutants. To overcome this, a promising new tool, antagonistic peptide technology, was recently developed. Here, this antagonistic peptide technology was tested on selected CLE peptides and the related IDA peptide and its usefulness in the context of studies of peptide function discussed. Based on the analyses, it was concluded that the antagonistic peptide approach is not the ultimate means to overcome redundancy or lack of loss-of-function lines. However, information collected using antagonistic peptide approaches (in the broad sense) can be very useful, but these approaches do not work in all cases and require a deep insight on the interaction between the ligand and its receptor to be successful. This, as well as peptide ligand structure considerations, should be taken into account before ordering a wide range of synthetic peptide variants and/or generating transgenic plants. Oxford University Press 2015-08 2015-06-30 /pmc/articles/PMC4526918/ /pubmed/26136270 http://dx.doi.org/10.1093/jxb/erv284 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
Czyzewicz, Nathan
Wildhagen, Mari
Cattaneo, Pietro
Stahl, Yvonne
Pinto, Karine Gustavo
Aalen, Reidunn B.
Butenko, Melinka A.
Simon, Rüdiger
Hardtke, Christian S.
De Smet, Ive
Antagonistic peptide technology for functional dissection of CLE peptides revisited
title Antagonistic peptide technology for functional dissection of CLE peptides revisited
title_full Antagonistic peptide technology for functional dissection of CLE peptides revisited
title_fullStr Antagonistic peptide technology for functional dissection of CLE peptides revisited
title_full_unstemmed Antagonistic peptide technology for functional dissection of CLE peptides revisited
title_short Antagonistic peptide technology for functional dissection of CLE peptides revisited
title_sort antagonistic peptide technology for functional dissection of cle peptides revisited
topic Research Paper
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4526918/
https://www.ncbi.nlm.nih.gov/pubmed/26136270
http://dx.doi.org/10.1093/jxb/erv284
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