ZmXTH1, a new xyloglucan endotransglucosylase/hydrolase in maize, affects cell wall structure and composition in Arabidopsis thaliana

Xyloglucan endotransglucosylase/hydrolases (XTHs; EC 2.4.1.207 and/or EC 3.2.1.151) are enzymes involved in the modification of cell wall structure by cleaving and, often, also re-joining xyloglucan molecules in primary plant cell walls. Using a pool of antibodies raised against an enriched cell wal...

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Autores: Genovesi, Valeria, Fornalé, Silvia, Fry, Stephen C., Ruel, Katia, Ferrer, Pau|||0000-0002-5287-4127, Encina, Antonio, Sonbol, Fathi-Mohamed, Bosch Argilagós, Josep|||0000-0002-2610-1120, Puigdomènech, Pere|||0000-0002-9866-861X, Rigau, Joan, Caparrós Ruiz, David|||0000-0002-7461-8888
Tipo de recurso: artículo
Fecha de publicación:2008
País:España
Institución:Universitat Autònoma de Barcelona
Repositorio:Dipòsit Digital de Documents de la UAB
Idioma:inglés
OAI Identifier:oai:ddd.uab.cat:215518
Acceso en línea:https://ddd.uab.cat/record/215518
https://dx.doi.org/urn:doi:10.1093/jxb/ern013
Access Level:acceso abierto
Palabra clave:Cell elongation
Cell wall
Plant transformation
XEH
XET
XTH
Zea mays
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spelling ZmXTH1, a new xyloglucan endotransglucosylase/hydrolase in maize, affects cell wall structure and composition in Arabidopsis thalianaGenovesi, ValeriaFornalé, SilviaFry, Stephen C.Ruel, KatiaFerrer, Pau|||0000-0002-5287-4127Encina, AntonioSonbol, Fathi-MohamedBosch Argilagós, Josep|||0000-0002-2610-1120Puigdomènech, Pere|||0000-0002-9866-861XRigau, JoanCaparrós Ruiz, David|||0000-0002-7461-8888Cell elongationCell wallPlant transformationXEHXETXTHZea maysXyloglucan endotransglucosylase/hydrolases (XTHs; EC 2.4.1.207 and/or EC 3.2.1.151) are enzymes involved in the modification of cell wall structure by cleaving and, often, also re-joining xyloglucan molecules in primary plant cell walls. Using a pool of antibodies raised against an enriched cell wall protein fraction, a new XTH cDNA in maize, ZmXTH1, has been isolated from a cDNA expression library obtained from the elongation zone of the maize root. The predicted protein has a putative N-terminal signal peptide and possesses the typical domains of this enzyme family, such as a catalytic domain that is homologous to that of Bacillus macerans β-glucanase, a putative N-glycosylation motif, and four cysteine residues in the central and C terminal regions of the ZmXTH1 protein. Phylogenetic analysis of ZmXTH1 reveals that it belongs to subgroup 4, so far only reported from Poaceae monocot species. ZmXTH1 has been expressed in Pichia pastoris (a methylotrophic yeast) and the recombinant enzyme showed xyloglucan endotransglucosylase but not xyloglucan endohydrolase activity, representing the first enzyme belonging to subgroup 4 characterized in maize so far. Expression data indicate that ZmXTH1 is expressed in elongating tissues, modulated by culture conditions, and induced by gibberellins. Transient expression assays in onion cells reveal that ZmXTH1 is directed to the cell wall, although weakly bound. Finally, Arabidopsis thaliana plants expressing ZmXTH1 show slightly increased xyloglucan endohydrolase activity and alterations in the cell wall structure and composition. 22008-01-0120082008-01-01Articlehttp://purl.org/coar/resource_type/c_6501VoRhttp://purl.org/coar/version/c_970fb48d4fbd8a85info:eu-repo/semantics/articleapplication/pdfhttps://ddd.uab.cat/record/215518https://dx.doi.org/urn:doi:10.1093/jxb/ern013reponame:Dipòsit Digital de Documents de la UABinstname:Universitat Autònoma de BarcelonaInglésengAgència de Gestió d'Ajuts Universitaris i de Recerca https://doi.org/10.13039/501100003030 2003/FI00090Ministerio de Ciencia y Tecnología https://doi.org/10.13039/501100006280 BIO2001-1140Agència de Gestió d'Ajuts Universitaris i de Recerca https://doi.org/10.13039/501100003030 2005/BE00104Agència de Gestió d'Ajuts Universitaris i de Recerca https://doi.org/10.13039/501100003030 2006/BE00668Agència de Gestió d'Ajuts Universitaris i de Recerca https://doi.org/10.13039/501100003030 2003/PIV-A-00033open accesshttp://purl.org/coar/access_right/c_abf2Aquest document està subjecte a una llicència d'ús Creative Commons. Es permet la reproducció total o parcial, la distribució, la comunicació pública de l'obra i la creació d'obres derivades, sempre que no sigui amb finalitats comercials, i sempre que es reconegui l'autoria de l'obra original.https://creativecommons.org/licenses/by-nc/4.0/info:eu-repo/semantics/openAccessoai:ddd.uab.cat:2155182026-06-06T12:50:31Z
dc.title.none.fl_str_mv ZmXTH1, a new xyloglucan endotransglucosylase/hydrolase in maize, affects cell wall structure and composition in Arabidopsis thaliana
title ZmXTH1, a new xyloglucan endotransglucosylase/hydrolase in maize, affects cell wall structure and composition in Arabidopsis thaliana
spellingShingle ZmXTH1, a new xyloglucan endotransglucosylase/hydrolase in maize, affects cell wall structure and composition in Arabidopsis thaliana
Genovesi, Valeria
Cell elongation
Cell wall
Plant transformation
XEH
XET
XTH
Zea mays
title_short ZmXTH1, a new xyloglucan endotransglucosylase/hydrolase in maize, affects cell wall structure and composition in Arabidopsis thaliana
title_full ZmXTH1, a new xyloglucan endotransglucosylase/hydrolase in maize, affects cell wall structure and composition in Arabidopsis thaliana
title_fullStr ZmXTH1, a new xyloglucan endotransglucosylase/hydrolase in maize, affects cell wall structure and composition in Arabidopsis thaliana
title_full_unstemmed ZmXTH1, a new xyloglucan endotransglucosylase/hydrolase in maize, affects cell wall structure and composition in Arabidopsis thaliana
title_sort ZmXTH1, a new xyloglucan endotransglucosylase/hydrolase in maize, affects cell wall structure and composition in Arabidopsis thaliana
dc.creator.none.fl_str_mv Genovesi, Valeria
Fornalé, Silvia
Fry, Stephen C.
Ruel, Katia
Ferrer, Pau|||0000-0002-5287-4127
Encina, Antonio
Sonbol, Fathi-Mohamed
Bosch Argilagós, Josep|||0000-0002-2610-1120
Puigdomènech, Pere|||0000-0002-9866-861X
Rigau, Joan
Caparrós Ruiz, David|||0000-0002-7461-8888
author Genovesi, Valeria
author_facet Genovesi, Valeria
Fornalé, Silvia
Fry, Stephen C.
Ruel, Katia
Ferrer, Pau|||0000-0002-5287-4127
Encina, Antonio
Sonbol, Fathi-Mohamed
Bosch Argilagós, Josep|||0000-0002-2610-1120
Puigdomènech, Pere|||0000-0002-9866-861X
Rigau, Joan
Caparrós Ruiz, David|||0000-0002-7461-8888
author_role author
author2 Fornalé, Silvia
Fry, Stephen C.
Ruel, Katia
Ferrer, Pau|||0000-0002-5287-4127
Encina, Antonio
Sonbol, Fathi-Mohamed
Bosch Argilagós, Josep|||0000-0002-2610-1120
Puigdomènech, Pere|||0000-0002-9866-861X
Rigau, Joan
Caparrós Ruiz, David|||0000-0002-7461-8888
author2_role author
author
author
author
author
author
author
author
author
author
dc.subject.none.fl_str_mv Cell elongation
Cell wall
Plant transformation
XEH
XET
XTH
Zea mays
topic Cell elongation
Cell wall
Plant transformation
XEH
XET
XTH
Zea mays
description Xyloglucan endotransglucosylase/hydrolases (XTHs; EC 2.4.1.207 and/or EC 3.2.1.151) are enzymes involved in the modification of cell wall structure by cleaving and, often, also re-joining xyloglucan molecules in primary plant cell walls. Using a pool of antibodies raised against an enriched cell wall protein fraction, a new XTH cDNA in maize, ZmXTH1, has been isolated from a cDNA expression library obtained from the elongation zone of the maize root. The predicted protein has a putative N-terminal signal peptide and possesses the typical domains of this enzyme family, such as a catalytic domain that is homologous to that of Bacillus macerans β-glucanase, a putative N-glycosylation motif, and four cysteine residues in the central and C terminal regions of the ZmXTH1 protein. Phylogenetic analysis of ZmXTH1 reveals that it belongs to subgroup 4, so far only reported from Poaceae monocot species. ZmXTH1 has been expressed in Pichia pastoris (a methylotrophic yeast) and the recombinant enzyme showed xyloglucan endotransglucosylase but not xyloglucan endohydrolase activity, representing the first enzyme belonging to subgroup 4 characterized in maize so far. Expression data indicate that ZmXTH1 is expressed in elongating tissues, modulated by culture conditions, and induced by gibberellins. Transient expression assays in onion cells reveal that ZmXTH1 is directed to the cell wall, although weakly bound. Finally, Arabidopsis thaliana plants expressing ZmXTH1 show slightly increased xyloglucan endohydrolase activity and alterations in the cell wall structure and composition.
publishDate 2008
dc.date.none.fl_str_mv 2
2008-01-01
2008
2008-01-01
dc.type.none.fl_str_mv Article
http://purl.org/coar/resource_type/c_6501
VoR
http://purl.org/coar/version/c_970fb48d4fbd8a85
dc.type.openaire.fl_str_mv info:eu-repo/semantics/article
format article
dc.identifier.none.fl_str_mv https://ddd.uab.cat/record/215518
https://dx.doi.org/urn:doi:10.1093/jxb/ern013
url https://ddd.uab.cat/record/215518
https://dx.doi.org/urn:doi:10.1093/jxb/ern013
dc.language.none.fl_str_mv Inglés
eng
language_invalid_str_mv Inglés
language eng
dc.relation.none.fl_str_mv Agència de Gestió d'Ajuts Universitaris i de Recerca https://doi.org/10.13039/501100003030 2003/FI00090
Ministerio de Ciencia y Tecnología https://doi.org/10.13039/501100006280 BIO2001-1140
Agència de Gestió d'Ajuts Universitaris i de Recerca https://doi.org/10.13039/501100003030 2005/BE00104
Agència de Gestió d'Ajuts Universitaris i de Recerca https://doi.org/10.13039/501100003030 2006/BE00668
Agència de Gestió d'Ajuts Universitaris i de Recerca https://doi.org/10.13039/501100003030 2003/PIV-A-00033
dc.rights.none.fl_str_mv open access
http://purl.org/coar/access_right/c_abf2
https://creativecommons.org/licenses/by-nc/4.0/
dc.rights.openaire.fl_str_mv info:eu-repo/semantics/openAccess
rights_invalid_str_mv open access
http://purl.org/coar/access_right/c_abf2
https://creativecommons.org/licenses/by-nc/4.0/
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv application/pdf
dc.source.none.fl_str_mv reponame:Dipòsit Digital de Documents de la UAB
instname:Universitat Autònoma de Barcelona
instname_str Universitat Autònoma de Barcelona
reponame_str Dipòsit Digital de Documents de la UAB
collection Dipòsit Digital de Documents de la UAB
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