Cargando…

Phylogenetic, Molecular, and Biochemical Characterization of Caffeic Acid o-Methyltransferase Gene Family in Brachypodium distachyon

Caffeic acid o-methyltransferase (COMT) is one of the important enzymes controlling lignin monomer production in plant cell wall synthesis. Analysis of the genome sequence of the new grass model Brachypodium distachyon identified four COMT gene homologs, designated as BdCOMT1, BdCOMT2, BdCOMT3, and...

Descripción completa

Detalles Bibliográficos
Autores principales: Wu, Xianting, Wu, Jiajie, Luo, Yangfan, Bragg, Jennifer, Anderson, Olin, Vogel, John, Gu, Yong Q.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Hindawi Publishing Corporation 2013
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3562662/
https://www.ncbi.nlm.nih.gov/pubmed/23431288
http://dx.doi.org/10.1155/2013/423189
_version_ 1782258121362636800
author Wu, Xianting
Wu, Jiajie
Luo, Yangfan
Bragg, Jennifer
Anderson, Olin
Vogel, John
Gu, Yong Q.
author_facet Wu, Xianting
Wu, Jiajie
Luo, Yangfan
Bragg, Jennifer
Anderson, Olin
Vogel, John
Gu, Yong Q.
author_sort Wu, Xianting
collection PubMed
description Caffeic acid o-methyltransferase (COMT) is one of the important enzymes controlling lignin monomer production in plant cell wall synthesis. Analysis of the genome sequence of the new grass model Brachypodium distachyon identified four COMT gene homologs, designated as BdCOMT1, BdCOMT2, BdCOMT3, and BdCOMT4. Phylogenetic analysis suggested that they belong to the COMT gene family, whereas syntenic analysis through comparisons with rice and sorghum revealed that BdCOMT4 on Chromosome 3 is the orthologous copy of the COMT genes well characterized in other grass species. The other three COMT genes are unique to Brachypodium since orthologous copies are not found in the collinear regions of rice and sorghum genomes. Expression studies indicated that all four Brachypodium COMT genes are transcribed but with distinct patterns of tissue specificity. Full-length cDNAs were cloned in frame into the pQE-T7 expression vector for the purification of recombinant Brachypodium COMT proteins. Biochemical characterization of enzyme activity and substrate specificity showed that BdCOMT4 has significant effect on a broad range of substrates with the highest preference for caffeic acid. The other three COMTs had low or no effect on these substrates, suggesting that a diversified evolution occurred on these duplicate genes that not only impacted their pattern of expression, but also altered their biochemical properties.
format Online
Article
Text
id pubmed-3562662
institution National Center for Biotechnology Information
language English
publishDate 2013
publisher Hindawi Publishing Corporation
record_format MEDLINE/PubMed
spelling pubmed-35626622013-02-21 Phylogenetic, Molecular, and Biochemical Characterization of Caffeic Acid o-Methyltransferase Gene Family in Brachypodium distachyon Wu, Xianting Wu, Jiajie Luo, Yangfan Bragg, Jennifer Anderson, Olin Vogel, John Gu, Yong Q. Int J Plant Genomics Research Article Caffeic acid o-methyltransferase (COMT) is one of the important enzymes controlling lignin monomer production in plant cell wall synthesis. Analysis of the genome sequence of the new grass model Brachypodium distachyon identified four COMT gene homologs, designated as BdCOMT1, BdCOMT2, BdCOMT3, and BdCOMT4. Phylogenetic analysis suggested that they belong to the COMT gene family, whereas syntenic analysis through comparisons with rice and sorghum revealed that BdCOMT4 on Chromosome 3 is the orthologous copy of the COMT genes well characterized in other grass species. The other three COMT genes are unique to Brachypodium since orthologous copies are not found in the collinear regions of rice and sorghum genomes. Expression studies indicated that all four Brachypodium COMT genes are transcribed but with distinct patterns of tissue specificity. Full-length cDNAs were cloned in frame into the pQE-T7 expression vector for the purification of recombinant Brachypodium COMT proteins. Biochemical characterization of enzyme activity and substrate specificity showed that BdCOMT4 has significant effect on a broad range of substrates with the highest preference for caffeic acid. The other three COMTs had low or no effect on these substrates, suggesting that a diversified evolution occurred on these duplicate genes that not only impacted their pattern of expression, but also altered their biochemical properties. Hindawi Publishing Corporation 2013 2013-01-17 /pmc/articles/PMC3562662/ /pubmed/23431288 http://dx.doi.org/10.1155/2013/423189 Text en Copyright © 2013 Xianting Wu et al. https://creativecommons.org/licenses/by/3.0/ This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
spellingShingle Research Article
Wu, Xianting
Wu, Jiajie
Luo, Yangfan
Bragg, Jennifer
Anderson, Olin
Vogel, John
Gu, Yong Q.
Phylogenetic, Molecular, and Biochemical Characterization of Caffeic Acid o-Methyltransferase Gene Family in Brachypodium distachyon
title Phylogenetic, Molecular, and Biochemical Characterization of Caffeic Acid o-Methyltransferase Gene Family in Brachypodium distachyon
title_full Phylogenetic, Molecular, and Biochemical Characterization of Caffeic Acid o-Methyltransferase Gene Family in Brachypodium distachyon
title_fullStr Phylogenetic, Molecular, and Biochemical Characterization of Caffeic Acid o-Methyltransferase Gene Family in Brachypodium distachyon
title_full_unstemmed Phylogenetic, Molecular, and Biochemical Characterization of Caffeic Acid o-Methyltransferase Gene Family in Brachypodium distachyon
title_short Phylogenetic, Molecular, and Biochemical Characterization of Caffeic Acid o-Methyltransferase Gene Family in Brachypodium distachyon
title_sort phylogenetic, molecular, and biochemical characterization of caffeic acid o-methyltransferase gene family in brachypodium distachyon
topic Research Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3562662/
https://www.ncbi.nlm.nih.gov/pubmed/23431288
http://dx.doi.org/10.1155/2013/423189
work_keys_str_mv AT wuxianting phylogeneticmolecularandbiochemicalcharacterizationofcaffeicacidomethyltransferasegenefamilyinbrachypodiumdistachyon
AT wujiajie phylogeneticmolecularandbiochemicalcharacterizationofcaffeicacidomethyltransferasegenefamilyinbrachypodiumdistachyon
AT luoyangfan phylogeneticmolecularandbiochemicalcharacterizationofcaffeicacidomethyltransferasegenefamilyinbrachypodiumdistachyon
AT braggjennifer phylogeneticmolecularandbiochemicalcharacterizationofcaffeicacidomethyltransferasegenefamilyinbrachypodiumdistachyon
AT andersonolin phylogeneticmolecularandbiochemicalcharacterizationofcaffeicacidomethyltransferasegenefamilyinbrachypodiumdistachyon
AT vogeljohn phylogeneticmolecularandbiochemicalcharacterizationofcaffeicacidomethyltransferasegenefamilyinbrachypodiumdistachyon
AT guyongq phylogeneticmolecularandbiochemicalcharacterizationofcaffeicacidomethyltransferasegenefamilyinbrachypodiumdistachyon