HydroxyprolineO-arabinosyltransferase mutants oppositely alter tip growth inArabidopsis thalianaandPhyscomitrella patens
Autor(a) principal: | |
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Data de Publicação: | 2016 |
Outros Autores: | , , , |
Tipo de documento: | Artigo |
Idioma: | eng |
Título da fonte: | Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) |
Texto Completo: | http://hdl.handle.net/10400.7/712 |
Resumo: | Hydroxyproline O-arabinosyltransferases (HPATs) are members of a small, deeply conserved family of plant-specific glycosyltransferases that add arabinose sugars to diverse proteins including cell wall-associated extensins and small signaling peptides. Recent genetic studies in flowering plants suggest that different HPAT homologs have been co-opted to function in diverse species-specific developmental contexts. However, nothing is known about the roles of HPATs in basal plants. We show that complete loss of HPAT function in Arabidopsis thaliana and the moss Physcomitrella patens results in a shared defect in gametophytic tip cell growth. Arabidopsis hpat1/2/3 triple knockout mutants suffer from a strong male sterility defect as a consequence of pollen tubes that fail to fully elongate following pollination. Knocking out the two HPAT genes of Physcomitrella results in larger multicellular filamentous networks due to increased elongation of protonemal tip cells. Physcomitrella hpat mutants lack cell-wall associated hydroxyproline arabinosides and can be rescued with exogenous cellulose, while global expression profiling shows that cell wall-associated genes are severely misexpressed, implicating a defect in cell wall formation during tip growth. Our findings point to a major role for HPATs in influencing cell elongation during tip growth in plants. |
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HydroxyprolineO-arabinosyltransferase mutants oppositely alter tip growth inArabidopsis thalianaandPhyscomitrella patensArabidopsis thalianaPhyscomitrella patenscell walltip growthglycosylationarabinosylationdevelopmentextensinspollinationprotonemaHydroxyproline O-arabinosyltransferases (HPATs) are members of a small, deeply conserved family of plant-specific glycosyltransferases that add arabinose sugars to diverse proteins including cell wall-associated extensins and small signaling peptides. Recent genetic studies in flowering plants suggest that different HPAT homologs have been co-opted to function in diverse species-specific developmental contexts. However, nothing is known about the roles of HPATs in basal plants. We show that complete loss of HPAT function in Arabidopsis thaliana and the moss Physcomitrella patens results in a shared defect in gametophytic tip cell growth. Arabidopsis hpat1/2/3 triple knockout mutants suffer from a strong male sterility defect as a consequence of pollen tubes that fail to fully elongate following pollination. Knocking out the two HPAT genes of Physcomitrella results in larger multicellular filamentous networks due to increased elongation of protonemal tip cells. Physcomitrella hpat mutants lack cell-wall associated hydroxyproline arabinosides and can be rescued with exogenous cellulose, while global expression profiling shows that cell wall-associated genes are severely misexpressed, implicating a defect in cell wall formation during tip growth. Our findings point to a major role for HPATs in influencing cell elongation during tip growth in plants.Gordon and Betty Moore Foundation grant: (GBMF 2550.01); US Department of Agriculture grant: (2015-67013-22823); National Institute of Food and Agriculture.WileyARCAMacAlister, Cora A.Ortiz-Ramírez, CarlosBecker, Jörg D.Feijó, José A.Lippman, Zachary B.2017-01-01T01:30:08Z2016-012016-01-01T00:00:00Zinfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articleapplication/pdfapplication/pdfapplication/postscriptapplication/postscriptapplication/postscriptapplication/postscriptapplication/postscriptapplication/postscriptapplication/postscriptapplication/postscriptapplication/postscriptapplication/pdfapplication/vnd.openxmlformats-officedocument.spreadsheetml.sheetapplication/vnd.openxmlformats-officedocument.spreadsheetml.sheetapplication/vnd.openxmlformats-officedocument.spreadsheetml.sheetapplication/vnd.openxmlformats-officedocument.spreadsheetml.sheetapplication/vnd.openxmlformats-officedocument.spreadsheetml.sheetapplication/vnd.openxmlformats-officedocument.wordprocessingml.documenthttp://hdl.handle.net/10400.7/712engMacAlister, C. A., Ortiz-Ramírez, C., Becker, J. D., Feijó, J. A. and Lippman, Z. B. (2016), Hydroxyproline O-arabinosyltransferase mutants oppositely alter tip growth in Arabidopsis thaliana and Physcomitrella patens. Plant J, 85: 193–208. doi:10.1111/tpj.1307910.1111/tpj.13079info:eu-repo/semantics/embargoedAccessreponame:Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)instname:Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informaçãoinstacron:RCAAP2022-11-29T14:35:06Zoai:arca.igc.gulbenkian.pt:10400.7/712Portal AgregadorONGhttps://www.rcaap.pt/oai/openaireopendoar:71602024-03-19T16:11:56.687280Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) - Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informaçãofalse |
dc.title.none.fl_str_mv |
HydroxyprolineO-arabinosyltransferase mutants oppositely alter tip growth inArabidopsis thalianaandPhyscomitrella patens |
title |
HydroxyprolineO-arabinosyltransferase mutants oppositely alter tip growth inArabidopsis thalianaandPhyscomitrella patens |
spellingShingle |
HydroxyprolineO-arabinosyltransferase mutants oppositely alter tip growth inArabidopsis thalianaandPhyscomitrella patens MacAlister, Cora A. Arabidopsis thaliana Physcomitrella patens cell wall tip growth glycosylation arabinosylation development extensins pollination protonema |
title_short |
HydroxyprolineO-arabinosyltransferase mutants oppositely alter tip growth inArabidopsis thalianaandPhyscomitrella patens |
title_full |
HydroxyprolineO-arabinosyltransferase mutants oppositely alter tip growth inArabidopsis thalianaandPhyscomitrella patens |
title_fullStr |
HydroxyprolineO-arabinosyltransferase mutants oppositely alter tip growth inArabidopsis thalianaandPhyscomitrella patens |
title_full_unstemmed |
HydroxyprolineO-arabinosyltransferase mutants oppositely alter tip growth inArabidopsis thalianaandPhyscomitrella patens |
title_sort |
HydroxyprolineO-arabinosyltransferase mutants oppositely alter tip growth inArabidopsis thalianaandPhyscomitrella patens |
author |
MacAlister, Cora A. |
author_facet |
MacAlister, Cora A. Ortiz-Ramírez, Carlos Becker, Jörg D. Feijó, José A. Lippman, Zachary B. |
author_role |
author |
author2 |
Ortiz-Ramírez, Carlos Becker, Jörg D. Feijó, José A. Lippman, Zachary B. |
author2_role |
author author author author |
dc.contributor.none.fl_str_mv |
ARCA |
dc.contributor.author.fl_str_mv |
MacAlister, Cora A. Ortiz-Ramírez, Carlos Becker, Jörg D. Feijó, José A. Lippman, Zachary B. |
dc.subject.por.fl_str_mv |
Arabidopsis thaliana Physcomitrella patens cell wall tip growth glycosylation arabinosylation development extensins pollination protonema |
topic |
Arabidopsis thaliana Physcomitrella patens cell wall tip growth glycosylation arabinosylation development extensins pollination protonema |
description |
Hydroxyproline O-arabinosyltransferases (HPATs) are members of a small, deeply conserved family of plant-specific glycosyltransferases that add arabinose sugars to diverse proteins including cell wall-associated extensins and small signaling peptides. Recent genetic studies in flowering plants suggest that different HPAT homologs have been co-opted to function in diverse species-specific developmental contexts. However, nothing is known about the roles of HPATs in basal plants. We show that complete loss of HPAT function in Arabidopsis thaliana and the moss Physcomitrella patens results in a shared defect in gametophytic tip cell growth. Arabidopsis hpat1/2/3 triple knockout mutants suffer from a strong male sterility defect as a consequence of pollen tubes that fail to fully elongate following pollination. Knocking out the two HPAT genes of Physcomitrella results in larger multicellular filamentous networks due to increased elongation of protonemal tip cells. Physcomitrella hpat mutants lack cell-wall associated hydroxyproline arabinosides and can be rescued with exogenous cellulose, while global expression profiling shows that cell wall-associated genes are severely misexpressed, implicating a defect in cell wall formation during tip growth. Our findings point to a major role for HPATs in influencing cell elongation during tip growth in plants. |
publishDate |
2016 |
dc.date.none.fl_str_mv |
2016-01 2016-01-01T00:00:00Z 2017-01-01T01:30:08Z |
dc.type.status.fl_str_mv |
info:eu-repo/semantics/publishedVersion |
dc.type.driver.fl_str_mv |
info:eu-repo/semantics/article |
format |
article |
status_str |
publishedVersion |
dc.identifier.uri.fl_str_mv |
http://hdl.handle.net/10400.7/712 |
url |
http://hdl.handle.net/10400.7/712 |
dc.language.iso.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
MacAlister, C. A., Ortiz-Ramírez, C., Becker, J. D., Feijó, J. A. and Lippman, Z. B. (2016), Hydroxyproline O-arabinosyltransferase mutants oppositely alter tip growth in Arabidopsis thaliana and Physcomitrella patens. Plant J, 85: 193–208. doi:10.1111/tpj.13079 10.1111/tpj.13079 |
dc.rights.driver.fl_str_mv |
info:eu-repo/semantics/embargoedAccess |
eu_rights_str_mv |
embargoedAccess |
dc.format.none.fl_str_mv |
application/pdf application/pdf application/postscript application/postscript application/postscript application/postscript application/postscript application/postscript application/postscript application/postscript application/postscript application/pdf application/vnd.openxmlformats-officedocument.spreadsheetml.sheet application/vnd.openxmlformats-officedocument.spreadsheetml.sheet application/vnd.openxmlformats-officedocument.spreadsheetml.sheet application/vnd.openxmlformats-officedocument.spreadsheetml.sheet application/vnd.openxmlformats-officedocument.spreadsheetml.sheet application/vnd.openxmlformats-officedocument.wordprocessingml.document |
dc.publisher.none.fl_str_mv |
Wiley |
publisher.none.fl_str_mv |
Wiley |
dc.source.none.fl_str_mv |
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Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) |
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Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) |
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Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) - Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação |
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