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OsCESA9 conserved‐site mutation leads to largely enhanced plant lodging resistance and biomass enzymatic saccharification by reducing cellulose DP and crystallinity in rice
Genetic modification of plant cell walls has been posed to reduce lignocellulose recalcitrance for enhancing biomass saccharification. Since cellulose synthase (CESA) gene was first identified, several dozen CESA mutants have been reported, but almost all mutants exhibit the defective phenotypes in...
Autores principales: | , , , , , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
John Wiley and Sons Inc.
2017
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5552474/ https://www.ncbi.nlm.nih.gov/pubmed/28117552 http://dx.doi.org/10.1111/pbi.12700 |
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author | Li, Fengcheng Xie, Guosheng Huang, Jiangfeng Zhang, Ran Li, Yu Zhang, Miaomiao Wang, Yanting Li, Ao Li, Xukai Xia, Tao Qu, Chengcheng Hu, Fan Ragauskas, Arthur J. Peng, Liangcai |
author_facet | Li, Fengcheng Xie, Guosheng Huang, Jiangfeng Zhang, Ran Li, Yu Zhang, Miaomiao Wang, Yanting Li, Ao Li, Xukai Xia, Tao Qu, Chengcheng Hu, Fan Ragauskas, Arthur J. Peng, Liangcai |
author_sort | Li, Fengcheng |
collection | PubMed |
description | Genetic modification of plant cell walls has been posed to reduce lignocellulose recalcitrance for enhancing biomass saccharification. Since cellulose synthase (CESA) gene was first identified, several dozen CESA mutants have been reported, but almost all mutants exhibit the defective phenotypes in plant growth and development. In this study, the rice (Oryza sativa) Osfc16 mutant with substitutions (W481C, P482S) at P‐CR conserved site in CESA9 shows a slightly affected plant growth and higher biomass yield by 25%–41% compared with wild type (Nipponbare, a japonica variety). Chemical and ultrastructural analyses indicate that Osfc16 has a significantly reduced cellulose crystallinity (CrI) and thinner secondary cell walls compared with wild type. CESA co‐IP detection, together with implementations of a proteasome inhibitor (MG132) and two distinct cellulose inhibitors (Calcofluor, CGA), shows that CESA9 mutation could affect integrity of CESA4/7/9 complexes, which may lead to rapid CESA proteasome degradation for low‐DP cellulose biosynthesis. These may reduce cellulose CrI, which improves plant lodging resistance, a major and integrated agronomic trait on plant growth and grain production, and enhances biomass enzymatic saccharification by up to 2.3‐fold and ethanol productivity by 34%–42%. This study has for the first time reported a direct modification for the low‐DP cellulose production that has broad applications in biomass industries. |
format | Online Article Text |
id | pubmed-5552474 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2017 |
publisher | John Wiley and Sons Inc. |
record_format | MEDLINE/PubMed |
spelling | pubmed-55524742017-08-25 OsCESA9 conserved‐site mutation leads to largely enhanced plant lodging resistance and biomass enzymatic saccharification by reducing cellulose DP and crystallinity in rice Li, Fengcheng Xie, Guosheng Huang, Jiangfeng Zhang, Ran Li, Yu Zhang, Miaomiao Wang, Yanting Li, Ao Li, Xukai Xia, Tao Qu, Chengcheng Hu, Fan Ragauskas, Arthur J. Peng, Liangcai Plant Biotechnol J Research Articles Genetic modification of plant cell walls has been posed to reduce lignocellulose recalcitrance for enhancing biomass saccharification. Since cellulose synthase (CESA) gene was first identified, several dozen CESA mutants have been reported, but almost all mutants exhibit the defective phenotypes in plant growth and development. In this study, the rice (Oryza sativa) Osfc16 mutant with substitutions (W481C, P482S) at P‐CR conserved site in CESA9 shows a slightly affected plant growth and higher biomass yield by 25%–41% compared with wild type (Nipponbare, a japonica variety). Chemical and ultrastructural analyses indicate that Osfc16 has a significantly reduced cellulose crystallinity (CrI) and thinner secondary cell walls compared with wild type. CESA co‐IP detection, together with implementations of a proteasome inhibitor (MG132) and two distinct cellulose inhibitors (Calcofluor, CGA), shows that CESA9 mutation could affect integrity of CESA4/7/9 complexes, which may lead to rapid CESA proteasome degradation for low‐DP cellulose biosynthesis. These may reduce cellulose CrI, which improves plant lodging resistance, a major and integrated agronomic trait on plant growth and grain production, and enhances biomass enzymatic saccharification by up to 2.3‐fold and ethanol productivity by 34%–42%. This study has for the first time reported a direct modification for the low‐DP cellulose production that has broad applications in biomass industries. John Wiley and Sons Inc. 2017-03-15 2017-09 /pmc/articles/PMC5552474/ /pubmed/28117552 http://dx.doi.org/10.1111/pbi.12700 Text en © 2017 The Authors. Plant Biotechnology Journal published by Society for Experimental Biology and The Association of Applied Biologists and John Wiley & Sons Ltd. This is an open access article under the terms of the Creative Commons Attribution (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 Articles Li, Fengcheng Xie, Guosheng Huang, Jiangfeng Zhang, Ran Li, Yu Zhang, Miaomiao Wang, Yanting Li, Ao Li, Xukai Xia, Tao Qu, Chengcheng Hu, Fan Ragauskas, Arthur J. Peng, Liangcai OsCESA9 conserved‐site mutation leads to largely enhanced plant lodging resistance and biomass enzymatic saccharification by reducing cellulose DP and crystallinity in rice |
title | OsCESA9 conserved‐site mutation leads to largely enhanced plant lodging resistance and biomass enzymatic saccharification by reducing cellulose DP and crystallinity in rice |
title_full | OsCESA9 conserved‐site mutation leads to largely enhanced plant lodging resistance and biomass enzymatic saccharification by reducing cellulose DP and crystallinity in rice |
title_fullStr | OsCESA9 conserved‐site mutation leads to largely enhanced plant lodging resistance and biomass enzymatic saccharification by reducing cellulose DP and crystallinity in rice |
title_full_unstemmed | OsCESA9 conserved‐site mutation leads to largely enhanced plant lodging resistance and biomass enzymatic saccharification by reducing cellulose DP and crystallinity in rice |
title_short | OsCESA9 conserved‐site mutation leads to largely enhanced plant lodging resistance and biomass enzymatic saccharification by reducing cellulose DP and crystallinity in rice |
title_sort | oscesa9 conserved‐site mutation leads to largely enhanced plant lodging resistance and biomass enzymatic saccharification by reducing cellulose dp and crystallinity in rice |
topic | Research Articles |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5552474/ https://www.ncbi.nlm.nih.gov/pubmed/28117552 http://dx.doi.org/10.1111/pbi.12700 |
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