Alterations of the degree of xylan acetylation in Arabidopsis xylan mutants
Xylan is the second most abundant polysaccharide in secondary walls of dicot plants and one of its structural features is the high degree of acetylation of xylosyl residues. In Arabidopsis, about 60% of xylosyl residues in xylan are acetylated and the biochemical mechanisms controlling xylan acetyla...
Published in: | Plant Signaling & Behavior |
---|---|
Main Authors: | , , , |
Format: | Text |
Language: | English |
Published: |
Landes Bioscience
2014
|
Subjects: | |
Online Access: | http://www.ncbi.nlm.nih.gov/pmc/articles/PMC4091231 http://www.ncbi.nlm.nih.gov/pubmed/24518588 https://doi.org/10.4161/psb.27797 |
id |
ftpubmed:oai:pubmedcentral.nih.gov:4091231 |
---|---|
record_format |
openpolar |
spelling |
ftpubmed:oai:pubmedcentral.nih.gov:4091231 2023-05-15T16:07:20+02:00 Alterations of the degree of xylan acetylation in Arabidopsis xylan mutants Lee, Chanhui Teng, Quincy Zhong, Ruiqin Ye, Zheng-Hua 2014-02-11 http://www.ncbi.nlm.nih.gov/pmc/articles/PMC4091231 http://www.ncbi.nlm.nih.gov/pubmed/24518588 https://doi.org/10.4161/psb.27797 en eng Landes Bioscience http://www.ncbi.nlm.nih.gov/pmc/articles/PMC http://www.ncbi.nlm.nih.gov/pubmed/24518588 http://dx.doi.org/10.4161/psb.27797 Copyright © 2014 Landes Bioscience Addendum Text 2014 ftpubmed https://doi.org/10.4161/psb.27797 2014-08-17T00:42:24Z Xylan is the second most abundant polysaccharide in secondary walls of dicot plants and one of its structural features is the high degree of acetylation of xylosyl residues. In Arabidopsis, about 60% of xylosyl residues in xylan are acetylated and the biochemical mechanisms controlling xylan acetylation are largely unknown. A recent report by Yuan et al. (2013) revealed the essential role of a DUF231 domain-containing protein, ESKIMO1 (ESK1), in xylan acetylation in Arabidopsis as the esk1 mutation caused specific reductions in the degree of xylan 2-O or 3-O-monoacetylation and in the activity of xylan acetyltransferase. Interestingly, the esk1 mutation also resulted in an elevation of glucuronic acid (GlcA) substitutions in xylan. Since GlcA substitutions in xylan occur at the O-2 position of xylosyl residues, it is plausible that the increase in GlcA substitutions in the esk1 mutant is attributed to the reduction in acetylation at O-2 of xylosyl residues, which renders more O-2 positions available for GlcA substitutions. Here, we investigated the effect of removal of GlcA substitutions on the degree of xylan acetylation. We found that a complete loss of GlcA substitutions in the xylan of the gux1/2/3 triple mutant led to a significant increase in the degree of xylan acetylation, indicating that xylan acetyltransferases and glucuronyltransferases compete with each other for xylosyl residues for their acetylation or GlcA substitutions in planta. In addition, detailed structure analysis of xylan from the rwa1/2/3/4 quadruple mutant revealed that it had a uniform reduction of acetyl substitutions at different positions of the xylosyl residues, which is consistent with the proposed role of RWAs as acetyl coenzyme A transporters. The significance of these findings is discussed. Text eskimo* PubMed Central (PMC) Plant Signaling & Behavior 9 2 e27797 |
institution |
Open Polar |
collection |
PubMed Central (PMC) |
op_collection_id |
ftpubmed |
language |
English |
topic |
Addendum |
spellingShingle |
Addendum Lee, Chanhui Teng, Quincy Zhong, Ruiqin Ye, Zheng-Hua Alterations of the degree of xylan acetylation in Arabidopsis xylan mutants |
topic_facet |
Addendum |
description |
Xylan is the second most abundant polysaccharide in secondary walls of dicot plants and one of its structural features is the high degree of acetylation of xylosyl residues. In Arabidopsis, about 60% of xylosyl residues in xylan are acetylated and the biochemical mechanisms controlling xylan acetylation are largely unknown. A recent report by Yuan et al. (2013) revealed the essential role of a DUF231 domain-containing protein, ESKIMO1 (ESK1), in xylan acetylation in Arabidopsis as the esk1 mutation caused specific reductions in the degree of xylan 2-O or 3-O-monoacetylation and in the activity of xylan acetyltransferase. Interestingly, the esk1 mutation also resulted in an elevation of glucuronic acid (GlcA) substitutions in xylan. Since GlcA substitutions in xylan occur at the O-2 position of xylosyl residues, it is plausible that the increase in GlcA substitutions in the esk1 mutant is attributed to the reduction in acetylation at O-2 of xylosyl residues, which renders more O-2 positions available for GlcA substitutions. Here, we investigated the effect of removal of GlcA substitutions on the degree of xylan acetylation. We found that a complete loss of GlcA substitutions in the xylan of the gux1/2/3 triple mutant led to a significant increase in the degree of xylan acetylation, indicating that xylan acetyltransferases and glucuronyltransferases compete with each other for xylosyl residues for their acetylation or GlcA substitutions in planta. In addition, detailed structure analysis of xylan from the rwa1/2/3/4 quadruple mutant revealed that it had a uniform reduction of acetyl substitutions at different positions of the xylosyl residues, which is consistent with the proposed role of RWAs as acetyl coenzyme A transporters. The significance of these findings is discussed. |
format |
Text |
author |
Lee, Chanhui Teng, Quincy Zhong, Ruiqin Ye, Zheng-Hua |
author_facet |
Lee, Chanhui Teng, Quincy Zhong, Ruiqin Ye, Zheng-Hua |
author_sort |
Lee, Chanhui |
title |
Alterations of the degree of xylan acetylation in Arabidopsis xylan mutants |
title_short |
Alterations of the degree of xylan acetylation in Arabidopsis xylan mutants |
title_full |
Alterations of the degree of xylan acetylation in Arabidopsis xylan mutants |
title_fullStr |
Alterations of the degree of xylan acetylation in Arabidopsis xylan mutants |
title_full_unstemmed |
Alterations of the degree of xylan acetylation in Arabidopsis xylan mutants |
title_sort |
alterations of the degree of xylan acetylation in arabidopsis xylan mutants |
publisher |
Landes Bioscience |
publishDate |
2014 |
url |
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC4091231 http://www.ncbi.nlm.nih.gov/pubmed/24518588 https://doi.org/10.4161/psb.27797 |
genre |
eskimo* |
genre_facet |
eskimo* |
op_relation |
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC http://www.ncbi.nlm.nih.gov/pubmed/24518588 http://dx.doi.org/10.4161/psb.27797 |
op_rights |
Copyright © 2014 Landes Bioscience |
op_doi |
https://doi.org/10.4161/psb.27797 |
container_title |
Plant Signaling & Behavior |
container_volume |
9 |
container_issue |
2 |
container_start_page |
e27797 |
_version_ |
1766403398045794304 |