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Two members of the DUF579 family are responsible for arabinogalactan methylation in Arabidopsis

All members of the DUF579 family characterized so far have been described to affect the integrity of the hemicellulosic cell wall component xylan: GXMs are glucuronoxylan methyltransferases catalyzing 4‐O–methylation of glucuronic acid on xylan; IRX15 and IRX15L, although their enzymatic activity is...

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Autores principales: Temple, Henry, Mortimer, Jenny C., Tryfona, Theodora, Yu, Xiaolan, Lopez‐Hernandez, Federico, Sorieul, Mathias, Anders, Nadine, Dupree, Paul
Formato: Online Artículo Texto
Lenguaje:English
Publicado: John Wiley and Sons Inc. 2019
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6508755/
https://www.ncbi.nlm.nih.gov/pubmed/31245760
http://dx.doi.org/10.1002/pld3.117
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author Temple, Henry
Mortimer, Jenny C.
Tryfona, Theodora
Yu, Xiaolan
Lopez‐Hernandez, Federico
Sorieul, Mathias
Anders, Nadine
Dupree, Paul
author_facet Temple, Henry
Mortimer, Jenny C.
Tryfona, Theodora
Yu, Xiaolan
Lopez‐Hernandez, Federico
Sorieul, Mathias
Anders, Nadine
Dupree, Paul
author_sort Temple, Henry
collection PubMed
description All members of the DUF579 family characterized so far have been described to affect the integrity of the hemicellulosic cell wall component xylan: GXMs are glucuronoxylan methyltransferases catalyzing 4‐O–methylation of glucuronic acid on xylan; IRX15 and IRX15L, although their enzymatic activity is unknown, are required for xylan biosynthesis and/or xylan deposition. Here we show that the DUF579 family members, AGM1 and AGM2, are required for 4‐O–methylation of glucuronic acid of a different plant cell wall component, the highly glycosylated arabinogalactan proteins (AGPs).
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spelling pubmed-65087552019-06-26 Two members of the DUF579 family are responsible for arabinogalactan methylation in Arabidopsis Temple, Henry Mortimer, Jenny C. Tryfona, Theodora Yu, Xiaolan Lopez‐Hernandez, Federico Sorieul, Mathias Anders, Nadine Dupree, Paul Plant Direct Original Research All members of the DUF579 family characterized so far have been described to affect the integrity of the hemicellulosic cell wall component xylan: GXMs are glucuronoxylan methyltransferases catalyzing 4‐O–methylation of glucuronic acid on xylan; IRX15 and IRX15L, although their enzymatic activity is unknown, are required for xylan biosynthesis and/or xylan deposition. Here we show that the DUF579 family members, AGM1 and AGM2, are required for 4‐O–methylation of glucuronic acid of a different plant cell wall component, the highly glycosylated arabinogalactan proteins (AGPs). John Wiley and Sons Inc. 2019-02-12 /pmc/articles/PMC6508755/ /pubmed/31245760 http://dx.doi.org/10.1002/pld3.117 Text en © 2019 The Authors. Plant Direct published by American Society of Plant Biologists, Society for Experimental Biology and John Wiley & Sons Ltd. 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 Original Research
Temple, Henry
Mortimer, Jenny C.
Tryfona, Theodora
Yu, Xiaolan
Lopez‐Hernandez, Federico
Sorieul, Mathias
Anders, Nadine
Dupree, Paul
Two members of the DUF579 family are responsible for arabinogalactan methylation in Arabidopsis
title Two members of the DUF579 family are responsible for arabinogalactan methylation in Arabidopsis
title_full Two members of the DUF579 family are responsible for arabinogalactan methylation in Arabidopsis
title_fullStr Two members of the DUF579 family are responsible for arabinogalactan methylation in Arabidopsis
title_full_unstemmed Two members of the DUF579 family are responsible for arabinogalactan methylation in Arabidopsis
title_short Two members of the DUF579 family are responsible for arabinogalactan methylation in Arabidopsis
title_sort two members of the duf579 family are responsible for arabinogalactan methylation in arabidopsis
topic Original Research
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6508755/
https://www.ncbi.nlm.nih.gov/pubmed/31245760
http://dx.doi.org/10.1002/pld3.117
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