Reconstruction of the sialylation pathway in the ancestor of eukaryotes

Autores
Petit, Daniel; Teppa, Roxana Elin; Cenci, Ugo; Ball, Steven; Harduin Lepers, Anne
Año de publicación
2018
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
The biosynthesis of sialylated molecules of crucial relevance for eukaryotic cell life is achieved by sialyltransferases (ST) of the CAZy family GT29. These enzymes are widespread in the Deuterostoma lineages and more rarely described in Protostoma, Viridiplantae and various protist lineages raising the question of their presence in the Last eukaryotes Common Ancestor (LECA). If so, it is expected that the main enzymes associated with sialic acids metabolism are also present in protists. We conducted phylogenomic and protein sequence analyses to gain insights into the origin and ancient evolution of ST and sialic acid pathway in eukaryotes, Bacteria and Archaea. Our study uncovered the unreported occurrence of bacterial GT29 ST and evidenced the existence of 2 ST groups in the LECA, likely originating from the endosymbiotic event that generated mitochondria. Furthermore, distribution of the major actors of the sialic acid pathway in the different eukaryotic phyla indicated that these were already present in the LECA, which could also access to this essential monosaccharide either endogenously or via a sialin/sialidase uptake mechanism involving vesicles. This pathway was lost in several basal eukaryotic lineages including Archaeplastida despite the presence of two different ST groups likely assigned to other functions.
Fil: Petit, Daniel. Université de Limoges; Francia
Fil: Teppa, Roxana Elin. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Investigaciones Bioquímicas de Buenos Aires. Fundación Instituto Leloir. Instituto de Investigaciones Bioquímicas de Buenos Aires; Argentina
Fil: Cenci, Ugo. Universite Lille; Francia
Fil: Ball, Steven. Universite Lille; Francia
Fil: Harduin Lepers, Anne. Universite Lille; Francia
Materia
sialyltransferases
sialylation pathway
Last eukaryotes Common Ancestor
GT29
Nivel de accesibilidad
acceso abierto
Condiciones de uso
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
Repositorio
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/88676
Acceder
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network_acronym_str CONICETDig
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network_name_str CONICET Digital (CONICET)
spelling Reconstruction of the sialylation pathway in the ancestor of eukaryotesPetit, DanielTeppa, Roxana ElinCenci, UgoBall, StevenHarduin Lepers, Annesialyltransferasessialylation pathwayLast eukaryotes Common AncestorGT29https://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1The biosynthesis of sialylated molecules of crucial relevance for eukaryotic cell life is achieved by sialyltransferases (ST) of the CAZy family GT29. These enzymes are widespread in the Deuterostoma lineages and more rarely described in Protostoma, Viridiplantae and various protist lineages raising the question of their presence in the Last eukaryotes Common Ancestor (LECA). If so, it is expected that the main enzymes associated with sialic acids metabolism are also present in protists. We conducted phylogenomic and protein sequence analyses to gain insights into the origin and ancient evolution of ST and sialic acid pathway in eukaryotes, Bacteria and Archaea. Our study uncovered the unreported occurrence of bacterial GT29 ST and evidenced the existence of 2 ST groups in the LECA, likely originating from the endosymbiotic event that generated mitochondria. Furthermore, distribution of the major actors of the sialic acid pathway in the different eukaryotic phyla indicated that these were already present in the LECA, which could also access to this essential monosaccharide either endogenously or via a sialin/sialidase uptake mechanism involving vesicles. This pathway was lost in several basal eukaryotic lineages including Archaeplastida despite the presence of two different ST groups likely assigned to other functions.Fil: Petit, Daniel. Université de Limoges; FranciaFil: Teppa, Roxana Elin. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Investigaciones Bioquímicas de Buenos Aires. Fundación Instituto Leloir. Instituto de Investigaciones Bioquímicas de Buenos Aires; ArgentinaFil: Cenci, Ugo. Universite Lille; FranciaFil: Ball, Steven. Universite Lille; FranciaFil: Harduin Lepers, Anne. Universite Lille; FranciaNature Publishing Group2018-12info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/88676Petit, Daniel; Teppa, Roxana Elin; Cenci, Ugo; Ball, Steven; Harduin Lepers, Anne; Reconstruction of the sialylation pathway in the ancestor of eukaryotes; Nature Publishing Group; Scientific Reports; 8; 1; 12-2018; 1-132045-2322CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/doi/10.1038/s41598-018-20920-1info:eu-repo/semantics/altIdentifier/url/https://www.nature.com/articles/s41598-018-20920-1info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-03T10:00:34Zoai:ri.conicet.gov.ar:11336/88676instacron:CONICETInstitucionalhttp://ri.conicet.gov.ar/Organismo científico-tecnológicoNo correspondehttp://ri.conicet.gov.ar/oai/requestdasensio@conicet.gov.ar; lcarlino@conicet.gov.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:34982025-09-03 10:00:34.4CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Reconstruction of the sialylation pathway in the ancestor of eukaryotes
title Reconstruction of the sialylation pathway in the ancestor of eukaryotes
spellingShingle Reconstruction of the sialylation pathway in the ancestor of eukaryotes
Petit, Daniel
sialyltransferases
sialylation pathway
Last eukaryotes Common Ancestor
GT29
title_short Reconstruction of the sialylation pathway in the ancestor of eukaryotes
title_full Reconstruction of the sialylation pathway in the ancestor of eukaryotes
title_fullStr Reconstruction of the sialylation pathway in the ancestor of eukaryotes
title_full_unstemmed Reconstruction of the sialylation pathway in the ancestor of eukaryotes
title_sort Reconstruction of the sialylation pathway in the ancestor of eukaryotes
dc.creator.none.fl_str_mv Petit, Daniel
Teppa, Roxana Elin
Cenci, Ugo
Ball, Steven
Harduin Lepers, Anne
author Petit, Daniel
author_facet Petit, Daniel
Teppa, Roxana Elin
Cenci, Ugo
Ball, Steven
Harduin Lepers, Anne
author_role author
author2 Teppa, Roxana Elin
Cenci, Ugo
Ball, Steven
Harduin Lepers, Anne
author2_role author
author
author
author
dc.subject.none.fl_str_mv sialyltransferases
sialylation pathway
Last eukaryotes Common Ancestor
GT29
topic sialyltransferases
sialylation pathway
Last eukaryotes Common Ancestor
GT29
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv The biosynthesis of sialylated molecules of crucial relevance for eukaryotic cell life is achieved by sialyltransferases (ST) of the CAZy family GT29. These enzymes are widespread in the Deuterostoma lineages and more rarely described in Protostoma, Viridiplantae and various protist lineages raising the question of their presence in the Last eukaryotes Common Ancestor (LECA). If so, it is expected that the main enzymes associated with sialic acids metabolism are also present in protists. We conducted phylogenomic and protein sequence analyses to gain insights into the origin and ancient evolution of ST and sialic acid pathway in eukaryotes, Bacteria and Archaea. Our study uncovered the unreported occurrence of bacterial GT29 ST and evidenced the existence of 2 ST groups in the LECA, likely originating from the endosymbiotic event that generated mitochondria. Furthermore, distribution of the major actors of the sialic acid pathway in the different eukaryotic phyla indicated that these were already present in the LECA, which could also access to this essential monosaccharide either endogenously or via a sialin/sialidase uptake mechanism involving vesicles. This pathway was lost in several basal eukaryotic lineages including Archaeplastida despite the presence of two different ST groups likely assigned to other functions.
Fil: Petit, Daniel. Université de Limoges; Francia
Fil: Teppa, Roxana Elin. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Investigaciones Bioquímicas de Buenos Aires. Fundación Instituto Leloir. Instituto de Investigaciones Bioquímicas de Buenos Aires; Argentina
Fil: Cenci, Ugo. Universite Lille; Francia
Fil: Ball, Steven. Universite Lille; Francia
Fil: Harduin Lepers, Anne. Universite Lille; Francia
description The biosynthesis of sialylated molecules of crucial relevance for eukaryotic cell life is achieved by sialyltransferases (ST) of the CAZy family GT29. These enzymes are widespread in the Deuterostoma lineages and more rarely described in Protostoma, Viridiplantae and various protist lineages raising the question of their presence in the Last eukaryotes Common Ancestor (LECA). If so, it is expected that the main enzymes associated with sialic acids metabolism are also present in protists. We conducted phylogenomic and protein sequence analyses to gain insights into the origin and ancient evolution of ST and sialic acid pathway in eukaryotes, Bacteria and Archaea. Our study uncovered the unreported occurrence of bacterial GT29 ST and evidenced the existence of 2 ST groups in the LECA, likely originating from the endosymbiotic event that generated mitochondria. Furthermore, distribution of the major actors of the sialic acid pathway in the different eukaryotic phyla indicated that these were already present in the LECA, which could also access to this essential monosaccharide either endogenously or via a sialin/sialidase uptake mechanism involving vesicles. This pathway was lost in several basal eukaryotic lineages including Archaeplastida despite the presence of two different ST groups likely assigned to other functions.
publishDate 2018
dc.date.none.fl_str_mv 2018-12
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
http://purl.org/coar/resource_type/c_6501
info:ar-repo/semantics/articulo
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv http://hdl.handle.net/11336/88676
Petit, Daniel; Teppa, Roxana Elin; Cenci, Ugo; Ball, Steven; Harduin Lepers, Anne; Reconstruction of the sialylation pathway in the ancestor of eukaryotes; Nature Publishing Group; Scientific Reports; 8; 1; 12-2018; 1-13
2045-2322
CONICET Digital
CONICET
url http://hdl.handle.net/11336/88676
identifier_str_mv Petit, Daniel; Teppa, Roxana Elin; Cenci, Ugo; Ball, Steven; Harduin Lepers, Anne; Reconstruction of the sialylation pathway in the ancestor of eukaryotes; Nature Publishing Group; Scientific Reports; 8; 1; 12-2018; 1-13
2045-2322
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/doi/10.1038/s41598-018-20920-1
info:eu-repo/semantics/altIdentifier/url/https://www.nature.com/articles/s41598-018-20920-1
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
eu_rights_str_mv openAccess
rights_invalid_str_mv https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.format.none.fl_str_mv application/pdf
application/pdf
dc.publisher.none.fl_str_mv Nature Publishing Group
publisher.none.fl_str_mv Nature Publishing Group
dc.source.none.fl_str_mv reponame:CONICET Digital (CONICET)
instname:Consejo Nacional de Investigaciones Científicas y Técnicas
reponame_str CONICET Digital (CONICET)
collection CONICET Digital (CONICET)
instname_str Consejo Nacional de Investigaciones Científicas y Técnicas
repository.name.fl_str_mv CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicas
repository.mail.fl_str_mv dasensio@conicet.gov.ar; lcarlino@conicet.gov.ar
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score 13.13397

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