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New insights into plant glycoside hydrolase family 32 in Agave species

In order to optimize the use of agaves for commercial applications, an understanding of fructan metabolism in these species at the molecular and genetic level is essential. Based on transcriptome data, this report describes the identification and molecular characterization of cDNAs and deduced amino...

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Autores principales: Avila de Dios, Emmanuel, Gomez Vargas, Alan D., Damián Santos, Maura L., Simpson, June
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Frontiers Media S.A. 2015
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4524927/
https://www.ncbi.nlm.nih.gov/pubmed/26300895
http://dx.doi.org/10.3389/fpls.2015.00594
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author Avila de Dios, Emmanuel
Gomez Vargas, Alan D.
Damián Santos, Maura L.
Simpson, June
author_facet Avila de Dios, Emmanuel
Gomez Vargas, Alan D.
Damián Santos, Maura L.
Simpson, June
author_sort Avila de Dios, Emmanuel
collection PubMed
description In order to optimize the use of agaves for commercial applications, an understanding of fructan metabolism in these species at the molecular and genetic level is essential. Based on transcriptome data, this report describes the identification and molecular characterization of cDNAs and deduced amino acid sequences for genes encoding fructosyltransferases, invertases and fructan exohydrolases (FEH) (enzymes belonging to plant glycoside hydrolase family 32) from four different agave species (A. tequilana, A. deserti, A. victoriae-reginae, and A. striata). Conserved amino acid sequences and a hypervariable domain allowed classification of distinct isoforms for each enzyme type. Notably however neither 1-FFT nor 6-SFT encoding cDNAs were identified. In silico analysis revealed that distinct isoforms for certain enzymes found in a single species, showed different levels and tissue specific patterns of expression whereas in other cases expression patterns were conserved both within the species and between different species. Relatively high levels of in silico expression for specific isoforms of both invertases and fructosyltransferases were observed in floral tissues in comparison to vegetative tissues such as leaves and stems and this pattern was confirmed by Quantitative Real Time PCR using RNA obtained from floral and leaf tissue of A. tequilana. Thin layer chromatography confirmed the presence of fructans with degree of polymerization (DP) greater than DP three in both immature buds and fully opened flowers also obtained from A. tequilana.
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spelling pubmed-45249272015-08-21 New insights into plant glycoside hydrolase family 32 in Agave species Avila de Dios, Emmanuel Gomez Vargas, Alan D. Damián Santos, Maura L. Simpson, June Front Plant Sci Plant Science In order to optimize the use of agaves for commercial applications, an understanding of fructan metabolism in these species at the molecular and genetic level is essential. Based on transcriptome data, this report describes the identification and molecular characterization of cDNAs and deduced amino acid sequences for genes encoding fructosyltransferases, invertases and fructan exohydrolases (FEH) (enzymes belonging to plant glycoside hydrolase family 32) from four different agave species (A. tequilana, A. deserti, A. victoriae-reginae, and A. striata). Conserved amino acid sequences and a hypervariable domain allowed classification of distinct isoforms for each enzyme type. Notably however neither 1-FFT nor 6-SFT encoding cDNAs were identified. In silico analysis revealed that distinct isoforms for certain enzymes found in a single species, showed different levels and tissue specific patterns of expression whereas in other cases expression patterns were conserved both within the species and between different species. Relatively high levels of in silico expression for specific isoforms of both invertases and fructosyltransferases were observed in floral tissues in comparison to vegetative tissues such as leaves and stems and this pattern was confirmed by Quantitative Real Time PCR using RNA obtained from floral and leaf tissue of A. tequilana. Thin layer chromatography confirmed the presence of fructans with degree of polymerization (DP) greater than DP three in both immature buds and fully opened flowers also obtained from A. tequilana. Frontiers Media S.A. 2015-08-05 /pmc/articles/PMC4524927/ /pubmed/26300895 http://dx.doi.org/10.3389/fpls.2015.00594 Text en Copyright © 2015 Avila de Dios, Gomez Vargas, Damián Santos and Simpson. http://creativecommons.org/licenses/by/4.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) or licensor are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.
spellingShingle Plant Science
Avila de Dios, Emmanuel
Gomez Vargas, Alan D.
Damián Santos, Maura L.
Simpson, June
New insights into plant glycoside hydrolase family 32 in Agave species
title New insights into plant glycoside hydrolase family 32 in Agave species
title_full New insights into plant glycoside hydrolase family 32 in Agave species
title_fullStr New insights into plant glycoside hydrolase family 32 in Agave species
title_full_unstemmed New insights into plant glycoside hydrolase family 32 in Agave species
title_short New insights into plant glycoside hydrolase family 32 in Agave species
title_sort new insights into plant glycoside hydrolase family 32 in agave species
topic Plant Science
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4524927/
https://www.ncbi.nlm.nih.gov/pubmed/26300895
http://dx.doi.org/10.3389/fpls.2015.00594
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