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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...
Autores principales: | , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Oxford University Press
2015
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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. |
format | Online Article Text |
id | pubmed-4526918 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2015 |
publisher | Oxford University Press |
record_format | MEDLINE/PubMed |
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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