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Review: structure and modifications of arabinogalactan proteins (AGPs)

The aim of this report is to provide general information on the molecular structure and synthesis of arabinogalactan proteins (AGPs) in association to their physiological significance. Assessment of genetic modifications of the activity of enzymes involved in the AGP biosynthesis is an efficient too...

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Autores principales: Leszczuk, Agata, Kalaitzis, Panagiotis, Kulik, Joanna, Zdunek, Artur
Formato: Online Artículo Texto
Lenguaje:English
Publicado: BioMed Central 2023
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9854139/
https://www.ncbi.nlm.nih.gov/pubmed/36670377
http://dx.doi.org/10.1186/s12870-023-04066-5
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author Leszczuk, Agata
Kalaitzis, Panagiotis
Kulik, Joanna
Zdunek, Artur
author_facet Leszczuk, Agata
Kalaitzis, Panagiotis
Kulik, Joanna
Zdunek, Artur
author_sort Leszczuk, Agata
collection PubMed
description The aim of this report is to provide general information on the molecular structure and synthesis of arabinogalactan proteins (AGPs) in association to their physiological significance. Assessment of genetic modifications of the activity of enzymes involved in the AGP biosynthesis is an efficient tool to study AGP functions. Thus, P4H (prolyl 4 hydroxylase) mutants, GLCAT (β-glucuronosyltransferase) mutants, and GH43 (glycoside hydrolase family 43) mutants have been described. We focused on the overview of AGPs modifications observed at the molecular, cellular, and organ levels. Inhibition of the hydroxylation process results in an increase in the intensity of cell divisions and thus, has an impact on root system length and leaf area. In turn, overexpression of P4H genes stimulates the density of root hairs. A mutation in GLCAT genes responsible for the transfer of glucuronic acid to the AGP molecule revealed that the reduction of GlcA in AGP disrupts the substantial assembly of the primary cell wall. Furthermore, silencing of genes encoding GH43, which has the ability to hydrolyze the AGP glycan by removing incorrectly synthesized β-1,3-galactans, induces changes in the abundance of other cell wall constituents, which finally leads to root growth defects. This information provides insight into AGPs as a crucial players in the structural interactions present in the plant extracellular matrix.
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spelling pubmed-98541392023-01-21 Review: structure and modifications of arabinogalactan proteins (AGPs) Leszczuk, Agata Kalaitzis, Panagiotis Kulik, Joanna Zdunek, Artur BMC Plant Biol Review The aim of this report is to provide general information on the molecular structure and synthesis of arabinogalactan proteins (AGPs) in association to their physiological significance. Assessment of genetic modifications of the activity of enzymes involved in the AGP biosynthesis is an efficient tool to study AGP functions. Thus, P4H (prolyl 4 hydroxylase) mutants, GLCAT (β-glucuronosyltransferase) mutants, and GH43 (glycoside hydrolase family 43) mutants have been described. We focused on the overview of AGPs modifications observed at the molecular, cellular, and organ levels. Inhibition of the hydroxylation process results in an increase in the intensity of cell divisions and thus, has an impact on root system length and leaf area. In turn, overexpression of P4H genes stimulates the density of root hairs. A mutation in GLCAT genes responsible for the transfer of glucuronic acid to the AGP molecule revealed that the reduction of GlcA in AGP disrupts the substantial assembly of the primary cell wall. Furthermore, silencing of genes encoding GH43, which has the ability to hydrolyze the AGP glycan by removing incorrectly synthesized β-1,3-galactans, induces changes in the abundance of other cell wall constituents, which finally leads to root growth defects. This information provides insight into AGPs as a crucial players in the structural interactions present in the plant extracellular matrix. BioMed Central 2023-01-20 /pmc/articles/PMC9854139/ /pubmed/36670377 http://dx.doi.org/10.1186/s12870-023-04066-5 Text en © The Author(s) 2023 https://creativecommons.org/licenses/by/4.0/Open AccessThis article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons licence, and indicate if changes were made. The images or other third party material in this article are included in the article's Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article's Creative Commons licence and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this licence, visit http://creativecommons.org/licenses/by/4.0/ (https://creativecommons.org/licenses/by/4.0/) . The Creative Commons Public Domain Dedication waiver (http://creativecommons.org/publicdomain/zero/1.0/ (https://creativecommons.org/publicdomain/zero/1.0/) ) applies to the data made available in this article, unless otherwise stated in a credit line to the data.
spellingShingle Review
Leszczuk, Agata
Kalaitzis, Panagiotis
Kulik, Joanna
Zdunek, Artur
Review: structure and modifications of arabinogalactan proteins (AGPs)
title Review: structure and modifications of arabinogalactan proteins (AGPs)
title_full Review: structure and modifications of arabinogalactan proteins (AGPs)
title_fullStr Review: structure and modifications of arabinogalactan proteins (AGPs)
title_full_unstemmed Review: structure and modifications of arabinogalactan proteins (AGPs)
title_short Review: structure and modifications of arabinogalactan proteins (AGPs)
title_sort review: structure and modifications of arabinogalactan proteins (agps)
topic Review
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9854139/
https://www.ncbi.nlm.nih.gov/pubmed/36670377
http://dx.doi.org/10.1186/s12870-023-04066-5
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