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Registro Completo |
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Biblioteca(s): |
Embrapa Agroenergia. |
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Data corrente: |
17/03/2021 |
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Data da última atualização: |
17/03/2021 |
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Tipo da produção científica: |
Artigo em Periódico Indexado |
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Autoria: |
MOTA, T. R.; SOUZA, W. R. DE; OLIVEIRA, D. M.; MARTINS, P. K.; SAMPAIO, B. L.; VINECKY, F.; RIBEIRO, ANA. P.; DUARTE, K. E.; PACHECO, T. F.; MONTEIRO, N. DE K. V.; CAMPANHA, R. B.; MARCHIOSI, R.; VIEIRA, D. S.; KOBAYASHI, A. K.; OLIVEIRA, P. A. de; FERRARESE-FILHO, O.; MITCHELL, R. A. C.; MOLINARI, H. B. C.; SANTOS, W. D. D. |
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Afiliação: |
THATIANE R. MOTA, Universidade Estadual de Maringá; WAGNER R. DE SOUZA; DYONI M. OLIVEIRA, Universidade Estadual de Maringá; POLYANA K. MARTINS; BRUNO L. SAMPAIO; FELIPE VINECKY; ANA P. RIBEIRO; KAROLINE E. DUARTE; THALYTA FRAGA PACHECO, CNPAE; NORBERTO DE K. V. MONTEIRO, Universidade Federal do Rio Grande do Norte; RAQUEL BOMBARDA CAMPANHA, CNPAE; ROGÉRIO MARCHIOSI, Universidade Estadual de Maringá; DAVI S. VIEIRA, Universidade Federal do Ceará; ADILSON KENJI KOBAYASHI, CNPAE; PATRICIA ABRAO DE OLIVEIRA MOLINARI, CNPAE; OSVALDO FERRARESE-FILHO, Universidade Estadual de Maringá; ROWAN A. C. MITCHELL, Rothamsted Research; HUGO BRUNO CORREA MOLINARI, CNPAE; WANDERLEY D. DOS SANTOS, Universidade Estadual de Maringá. |
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Título: |
Suppression of a BAHD acyltransferase decreases p-coumaroyl on arabinoxylan and improves biomass digestibility in the model grass Setaria viridis. |
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Ano de publicação: |
2021 |
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Fonte/Imprenta: |
The Plant Journal, n. 105, p. 136-150, 2021. |
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DOI: |
https://doi.org/10.1111/tpj.15046 |
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Idioma: |
Inglês |
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Conteúdo: |
Abstract: Grass cell walls have hydroxycinnamic acids attached to arabinosyl residues of arabinoxylan (AX), and certain BAHD acyltransferases are involved in their addition. In this study, we characterized one of these BAHD genes in the cell wall of the model grass Setaria viridis. RNAi silenced lines of S. viridis (SvBAHD05) presented a decrease of up to 42% of ester-linked p-coumarate (pCA) and 50% of pCA-arabinofuranosyl, across three generations. Biomass from SvBAHD05 silenced plants exhibited up to 32% increase in biomass saccharification after acid pre-treatment, with no change in total lignin. Molecular dynamics simulations suggested that SvBAHD05 is a p-coumaroyl coenzyme A transferase (PAT) mainly involved in the addition of pCA to the arabinofuranosyl residues of AX in Setaria. Thus, our results provide evidence of p-coumaroylation of AX promoted by SvBAHD05 acyltransferase in the cell wall of the model grass S. viridis. Furthermore, SvBAHD05 is a promising biotechnological target to engineer crops for improved biomass digestibility for biofuels, biorefineries and animal feeding. |
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Palavras-Chave: |
Cell wall acylation; Grass xylan; Hydroxycinnamic acids. |
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Thesagro: |
Lignina. |
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Thesaurus Nal: |
Lignin; Lignocellulose; P-coumaric acid; Saccharification. |
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Categoria do assunto: |
-- |
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Marc: |
LEADER 02426naa a2200445 a 4500
001 2130767
005 2021-03-17
008 2021 bl uuuu u00u1 u #d
024 7 $ahttps://doi.org/10.1111/tpj.15046$2DOI
100 1 $aMOTA, T. R.
245 $aSuppression of a BAHD acyltransferase decreases p-coumaroyl on arabinoxylan and improves biomass digestibility in the model grass Setaria viridis.$h[electronic resource]
260 $c2021
520 $aAbstract: Grass cell walls have hydroxycinnamic acids attached to arabinosyl residues of arabinoxylan (AX), and certain BAHD acyltransferases are involved in their addition. In this study, we characterized one of these BAHD genes in the cell wall of the model grass Setaria viridis. RNAi silenced lines of S. viridis (SvBAHD05) presented a decrease of up to 42% of ester-linked p-coumarate (pCA) and 50% of pCA-arabinofuranosyl, across three generations. Biomass from SvBAHD05 silenced plants exhibited up to 32% increase in biomass saccharification after acid pre-treatment, with no change in total lignin. Molecular dynamics simulations suggested that SvBAHD05 is a p-coumaroyl coenzyme A transferase (PAT) mainly involved in the addition of pCA to the arabinofuranosyl residues of AX in Setaria. Thus, our results provide evidence of p-coumaroylation of AX promoted by SvBAHD05 acyltransferase in the cell wall of the model grass S. viridis. Furthermore, SvBAHD05 is a promising biotechnological target to engineer crops for improved biomass digestibility for biofuels, biorefineries and animal feeding.
650 $aLignin
650 $aLignocellulose
650 $aP-coumaric acid
650 $aSaccharification
650 $aLignina
653 $aCell wall acylation
653 $aGrass xylan
653 $aHydroxycinnamic acids
700 1 $aSOUZA, W. R. DE
700 1 $aOLIVEIRA, D. M.
700 1 $aMARTINS, P. K.
700 1 $aSAMPAIO, B. L.
700 1 $aVINECKY, F.
700 1 $aRIBEIRO, ANA. P.
700 1 $aDUARTE, K. E.
700 1 $aPACHECO, T. F.
700 1 $aMONTEIRO, N. DE K. V.
700 1 $aCAMPANHA, R. B.
700 1 $aMARCHIOSI, R.
700 1 $aVIEIRA, D. S.
700 1 $aKOBAYASHI, A. K.
700 1 $aOLIVEIRA, P. A. de
700 1 $aFERRARESE-FILHO, O.
700 1 $aMITCHELL, R. A. C.
700 1 $aMOLINARI, H. B. C.
700 1 $aSANTOS, W. D. D.
773 $tThe Plant Journal$gn. 105, p. 136-150, 2021.
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