A group of Populus trichocarpa DUF231 proteins exhibit differential O-acetyltransferase activities toward xylan
Wood represents the most abundant biomass produced by plants and one of its major components is acetyl xylan. Acetylation in xylan can occur at O-2 or O-3 of a xylosyl residue, at both O-2 and O-3 of a xylosyl residue, and at O-3 of a xylosyl residue substituted at O-2 with glucuronic acid. Acetyltr...
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ftpubmed:oai:pubmedcentral.nih.gov:5884507 2023-05-15T16:07:09+02:00 A group of Populus trichocarpa DUF231 proteins exhibit differential O-acetyltransferase activities toward xylan Zhong, Ruiqin Cui, Dongtao Ye, Zheng-Hua 2018-04-04 http://www.ncbi.nlm.nih.gov/pmc/articles/PMC5884507/ http://www.ncbi.nlm.nih.gov/pubmed/29617384 https://doi.org/10.1371/journal.pone.0194532 en eng Public Library of Science http://www.ncbi.nlm.nih.gov/pmc/articles/PMC5884507/ http://www.ncbi.nlm.nih.gov/pubmed/29617384 http://dx.doi.org/10.1371/journal.pone.0194532 © 2018 Zhong et al http://creativecommons.org/licenses/by/4.0/ This is an open access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0/) , which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited. CC-BY Research Article Text 2018 ftpubmed https://doi.org/10.1371/journal.pone.0194532 2018-04-22T01:10:05Z Wood represents the most abundant biomass produced by plants and one of its major components is acetyl xylan. Acetylation in xylan can occur at O-2 or O-3 of a xylosyl residue, at both O-2 and O-3 of a xylosyl residue, and at O-3 of a xylosyl residue substituted at O-2 with glucuronic acid. Acetyltransferases responsible for the regiospecific acetylation of xylan in tree species have not yet been characterized. Here we report the biochemical characterization of twelve Populus trichocarpa DUF231-containing proteins, named PtrXOATs, for their roles in the regiospecific acetylation of xylan. The PtrXOAT genes were found to be differentially expressed in Populus organs and among them, PtrXOAT1, PtrXOAT2, PtrXOAT9 and PtrXOAT10 exhibited the highest level of expression in stems undergoing wood formation. Activity assays of recombinant proteins demonstrated that all twelve PtrXOAT proteins were able to transfer acetyl groups from acetyl CoA onto a xylohexaose acceptor with PtrXOAT1, PtrXOAT2, PtrXOAT3, PtrXOAT11 and PtrXOAT12 having the highest activity. Structural analysis of the PtrXOAT-catalyzed reaction products using 1H NMR spectroscopy revealed that PtrXOAT1, PtrXAOT2 and PtrXOAT3 mediated 2-O- and 3-O-monoacetylation and 2,3-di-O-acetylation of xylosyl residues and PtrXOAT11 and PtrXOAT12 only catalyzed 2-O- and 3-O-monoacetylation of xylosyl residues. Of the twelve PtrXOATs, only PtrXOAT9 and PtrXOAT10 were capable of transferring acetyl groups onto the O-3 position of 2-O-glucuronic acid-substituted xylosyl residues. Furthermore, when expressed in the Arabidopsis eskimo1 mutant, PtrXOAT1, PtrXAOT2 and PtrXOAT3 were able to rescue the defects in xylan acetylation. Together, these results demonstrate that the twelve PtrXOATs are acetyltransferases with different roles in xylan acetylation in P. trichocarpa. Text eskimo* PubMed Central (PMC) PLOS ONE 13 4 e0194532 |
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Research Article Zhong, Ruiqin Cui, Dongtao Ye, Zheng-Hua A group of Populus trichocarpa DUF231 proteins exhibit differential O-acetyltransferase activities toward xylan |
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description |
Wood represents the most abundant biomass produced by plants and one of its major components is acetyl xylan. Acetylation in xylan can occur at O-2 or O-3 of a xylosyl residue, at both O-2 and O-3 of a xylosyl residue, and at O-3 of a xylosyl residue substituted at O-2 with glucuronic acid. Acetyltransferases responsible for the regiospecific acetylation of xylan in tree species have not yet been characterized. Here we report the biochemical characterization of twelve Populus trichocarpa DUF231-containing proteins, named PtrXOATs, for their roles in the regiospecific acetylation of xylan. The PtrXOAT genes were found to be differentially expressed in Populus organs and among them, PtrXOAT1, PtrXOAT2, PtrXOAT9 and PtrXOAT10 exhibited the highest level of expression in stems undergoing wood formation. Activity assays of recombinant proteins demonstrated that all twelve PtrXOAT proteins were able to transfer acetyl groups from acetyl CoA onto a xylohexaose acceptor with PtrXOAT1, PtrXOAT2, PtrXOAT3, PtrXOAT11 and PtrXOAT12 having the highest activity. Structural analysis of the PtrXOAT-catalyzed reaction products using 1H NMR spectroscopy revealed that PtrXOAT1, PtrXAOT2 and PtrXOAT3 mediated 2-O- and 3-O-monoacetylation and 2,3-di-O-acetylation of xylosyl residues and PtrXOAT11 and PtrXOAT12 only catalyzed 2-O- and 3-O-monoacetylation of xylosyl residues. Of the twelve PtrXOATs, only PtrXOAT9 and PtrXOAT10 were capable of transferring acetyl groups onto the O-3 position of 2-O-glucuronic acid-substituted xylosyl residues. Furthermore, when expressed in the Arabidopsis eskimo1 mutant, PtrXOAT1, PtrXAOT2 and PtrXOAT3 were able to rescue the defects in xylan acetylation. Together, these results demonstrate that the twelve PtrXOATs are acetyltransferases with different roles in xylan acetylation in P. trichocarpa. |
format |
Text |
author |
Zhong, Ruiqin Cui, Dongtao Ye, Zheng-Hua |
author_facet |
Zhong, Ruiqin Cui, Dongtao Ye, Zheng-Hua |
author_sort |
Zhong, Ruiqin |
title |
A group of Populus trichocarpa DUF231 proteins exhibit differential O-acetyltransferase activities toward xylan |
title_short |
A group of Populus trichocarpa DUF231 proteins exhibit differential O-acetyltransferase activities toward xylan |
title_full |
A group of Populus trichocarpa DUF231 proteins exhibit differential O-acetyltransferase activities toward xylan |
title_fullStr |
A group of Populus trichocarpa DUF231 proteins exhibit differential O-acetyltransferase activities toward xylan |
title_full_unstemmed |
A group of Populus trichocarpa DUF231 proteins exhibit differential O-acetyltransferase activities toward xylan |
title_sort |
group of populus trichocarpa duf231 proteins exhibit differential o-acetyltransferase activities toward xylan |
publisher |
Public Library of Science |
publishDate |
2018 |
url |
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC5884507/ http://www.ncbi.nlm.nih.gov/pubmed/29617384 https://doi.org/10.1371/journal.pone.0194532 |
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eskimo* |
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eskimo* |
op_relation |
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC5884507/ http://www.ncbi.nlm.nih.gov/pubmed/29617384 http://dx.doi.org/10.1371/journal.pone.0194532 |
op_rights |
© 2018 Zhong et al http://creativecommons.org/licenses/by/4.0/ This is an open access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0/) , which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited. |
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CC-BY |
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https://doi.org/10.1371/journal.pone.0194532 |
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PLOS ONE |
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13 |
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e0194532 |
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