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PIRIN2 suppresses S‐type lignin accumulation in a noncell‐autonomous manner in Arabidopsis xylem elements
PIRIN (PRN) genes encode cupin domain‐containing proteins that function as transcriptional co‐regulators in humans but that are poorly described in plants. A previous study in xylogenic cell cultures of Zinnia elegans suggested a role for a PRN protein in lignification. This study aimed to identify...
Autores principales: | , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
John Wiley and Sons Inc.
2019
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7027918/ https://www.ncbi.nlm.nih.gov/pubmed/31625609 http://dx.doi.org/10.1111/nph.16271 |
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author | Zhang, Bo Sztojka, Bernadette Escamez, Sacha Vanholme, Ruben Hedenström, Mattias Wang, Yin Turumtay, Halbay Gorzsás, András Boerjan, Wout Tuominen, Hannele |
author_facet | Zhang, Bo Sztojka, Bernadette Escamez, Sacha Vanholme, Ruben Hedenström, Mattias Wang, Yin Turumtay, Halbay Gorzsás, András Boerjan, Wout Tuominen, Hannele |
author_sort | Zhang, Bo |
collection | PubMed |
description | PIRIN (PRN) genes encode cupin domain‐containing proteins that function as transcriptional co‐regulators in humans but that are poorly described in plants. A previous study in xylogenic cell cultures of Zinnia elegans suggested a role for a PRN protein in lignification. This study aimed to identify the function of Arabidopsis (Arabidopsis thaliana) PRN proteins in lignification of xylem tissues. Chemical composition of the secondary cell walls was analysed in Arabidopsis stems and/or hypocotyls by pyrolysis–gas chromatography/mass spectrometry, 2D‐nuclear magnetic resonance and phenolic profiling. Secondary cell walls of individual xylem elements were chemotyped by Fourier transform infrared and Raman microspectroscopy. Arabidopsis PRN2 suppressed accumulation of S‐type lignin in Arabidopsis stems and hypocotyls. PRN2 promoter activity and PRN2:GFP fusion protein were localised specifically in cells next to the vessel elements, suggesting a role for PRN2 in noncell‐autonomous lignification of xylem vessels. Accordingly, PRN2 modulated lignin chemistry in the secondary cell walls of the neighbouring vessel elements. These results indicate that PRN2 suppresses S‐type lignin accumulation in the neighbourhood of xylem vessels to bestow G‐type enriched lignin composition on the secondary cell walls of the vessel elements. Gene expression analyses suggested that PRN2 function is mediated by regulation of the expression of the lignin‐biosynthetic genes. |
format | Online Article Text |
id | pubmed-7027918 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2019 |
publisher | John Wiley and Sons Inc. |
record_format | MEDLINE/PubMed |
spelling | pubmed-70279182020-02-24 PIRIN2 suppresses S‐type lignin accumulation in a noncell‐autonomous manner in Arabidopsis xylem elements Zhang, Bo Sztojka, Bernadette Escamez, Sacha Vanholme, Ruben Hedenström, Mattias Wang, Yin Turumtay, Halbay Gorzsás, András Boerjan, Wout Tuominen, Hannele New Phytol Research PIRIN (PRN) genes encode cupin domain‐containing proteins that function as transcriptional co‐regulators in humans but that are poorly described in plants. A previous study in xylogenic cell cultures of Zinnia elegans suggested a role for a PRN protein in lignification. This study aimed to identify the function of Arabidopsis (Arabidopsis thaliana) PRN proteins in lignification of xylem tissues. Chemical composition of the secondary cell walls was analysed in Arabidopsis stems and/or hypocotyls by pyrolysis–gas chromatography/mass spectrometry, 2D‐nuclear magnetic resonance and phenolic profiling. Secondary cell walls of individual xylem elements were chemotyped by Fourier transform infrared and Raman microspectroscopy. Arabidopsis PRN2 suppressed accumulation of S‐type lignin in Arabidopsis stems and hypocotyls. PRN2 promoter activity and PRN2:GFP fusion protein were localised specifically in cells next to the vessel elements, suggesting a role for PRN2 in noncell‐autonomous lignification of xylem vessels. Accordingly, PRN2 modulated lignin chemistry in the secondary cell walls of the neighbouring vessel elements. These results indicate that PRN2 suppresses S‐type lignin accumulation in the neighbourhood of xylem vessels to bestow G‐type enriched lignin composition on the secondary cell walls of the vessel elements. Gene expression analyses suggested that PRN2 function is mediated by regulation of the expression of the lignin‐biosynthetic genes. John Wiley and Sons Inc. 2019-11-11 2020-03 /pmc/articles/PMC7027918/ /pubmed/31625609 http://dx.doi.org/10.1111/nph.16271 Text en © 2019 The Authors. New Phytologist © 2019 New Phytologist Trust This is an open access article under the terms of the http://creativecommons.org/licenses/by/4.0/ License, which permits use, distribution and reproduction in any medium, provided the original work is properly cited. |
spellingShingle | Research Zhang, Bo Sztojka, Bernadette Escamez, Sacha Vanholme, Ruben Hedenström, Mattias Wang, Yin Turumtay, Halbay Gorzsás, András Boerjan, Wout Tuominen, Hannele PIRIN2 suppresses S‐type lignin accumulation in a noncell‐autonomous manner in Arabidopsis xylem elements |
title | PIRIN2 suppresses S‐type lignin accumulation in a noncell‐autonomous manner in Arabidopsis xylem elements |
title_full | PIRIN2 suppresses S‐type lignin accumulation in a noncell‐autonomous manner in Arabidopsis xylem elements |
title_fullStr | PIRIN2 suppresses S‐type lignin accumulation in a noncell‐autonomous manner in Arabidopsis xylem elements |
title_full_unstemmed | PIRIN2 suppresses S‐type lignin accumulation in a noncell‐autonomous manner in Arabidopsis xylem elements |
title_short | PIRIN2 suppresses S‐type lignin accumulation in a noncell‐autonomous manner in Arabidopsis xylem elements |
title_sort | pirin2 suppresses s‐type lignin accumulation in a noncell‐autonomous manner in arabidopsis xylem elements |
topic | Research |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7027918/ https://www.ncbi.nlm.nih.gov/pubmed/31625609 http://dx.doi.org/10.1111/nph.16271 |
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