Phylogenetic-derived insights into the evolution of sialylation in eukaryotes: Comprehensive analysis of vertebrate β-galactoside α2,3/6-sialyltransferases (ST3Gal and ST6Gal)
- Autores
- Teppa, Roxana Elin; Petit, Daniel; Plechakova, Olga; Cogez, Virginie; Harduin-Lepers, Anne
- Año de publicación
- 2016
- Idioma
- inglés
- Tipo de recurso
- artículo
- Estado
- versión publicada
- Descripción
- Cell surface of eukaryotic cells is covered with a wide variety of sialylated molecules involved in diverse biological processes and taking part in cell-cell interactions. Although the physiological relevance of these sialylated glycoconjugates in vertebrates begins to be deciphered, the origin and evolution of the genetic machinery implicated in their biosynthetic pathway are poorly understood. Among the variety of actors involved in the sialylation machinery, sialyltransferases are key enzymes for the biosynthesis of sialylated molecules. This review focus on β-galactoside α2,3/6-sialyltransferases belonging to the ST3Gal and ST6Gal families. We propose here an outline of the evolutionary history of these two major ST families. Comparative genomics, molecular phylogeny and structural bioinformatics provided insights into the functional innovations in sialic acid metabolism and enabled to explore how ST-gene function evolved in vertebrates.
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: Petit, Daniel. Université de Limoges; Francia
Fil: Plechakova, Olga. Universite Lille; Francia. Centre National de la Recherche Scientifique; Francia
Fil: Cogez, Virginie. Universite Lille; Francia. Centre National de la Recherche Scientifique; Francia
Fil: Harduin-Lepers, Anne. Universite Lille; Francia. Centre National de la Recherche Scientifique; Francia - Materia
-
EVOLUTION
FUNCTIONAL GENOMICS
MOLECULAR PHYLOGENY
SIALIC ACID
SIALYLTRANSFERASES - Nivel de accesibilidad
- acceso abierto
- Condiciones de uso
- https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
- Repositorio
- Institución
- Consejo Nacional de Investigaciones Científicas y Técnicas
- OAI Identificador
- oai:ri.conicet.gov.ar:11336/84338
Ver los metadatos del registro completo
id |
CONICETDig_6d5565cccf0930e2a250806f43da9052 |
---|---|
oai_identifier_str |
oai:ri.conicet.gov.ar:11336/84338 |
network_acronym_str |
CONICETDig |
repository_id_str |
3498 |
network_name_str |
CONICET Digital (CONICET) |
spelling |
Phylogenetic-derived insights into the evolution of sialylation in eukaryotes: Comprehensive analysis of vertebrate β-galactoside α2,3/6-sialyltransferases (ST3Gal and ST6Gal)Teppa, Roxana ElinPetit, DanielPlechakova, OlgaCogez, VirginieHarduin-Lepers, AnneEVOLUTIONFUNCTIONAL GENOMICSMOLECULAR PHYLOGENYSIALIC ACIDSIALYLTRANSFERASEShttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1Cell surface of eukaryotic cells is covered with a wide variety of sialylated molecules involved in diverse biological processes and taking part in cell-cell interactions. Although the physiological relevance of these sialylated glycoconjugates in vertebrates begins to be deciphered, the origin and evolution of the genetic machinery implicated in their biosynthetic pathway are poorly understood. Among the variety of actors involved in the sialylation machinery, sialyltransferases are key enzymes for the biosynthesis of sialylated molecules. This review focus on β-galactoside α2,3/6-sialyltransferases belonging to the ST3Gal and ST6Gal families. We propose here an outline of the evolutionary history of these two major ST families. Comparative genomics, molecular phylogeny and structural bioinformatics provided insights into the functional innovations in sialic acid metabolism and enabled to explore how ST-gene function evolved in vertebrates.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; ArgentinaFil: Petit, Daniel. Université de Limoges; FranciaFil: Plechakova, Olga. Universite Lille; Francia. Centre National de la Recherche Scientifique; FranciaFil: Cogez, Virginie. Universite Lille; Francia. Centre National de la Recherche Scientifique; FranciaFil: Harduin-Lepers, Anne. Universite Lille; Francia. Centre National de la Recherche Scientifique; FranciaMolecular Diversity Preservation International2016-08info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/84338Teppa, Roxana Elin; Petit, Daniel; Plechakova, Olga; Cogez, Virginie; Harduin-Lepers, Anne; Phylogenetic-derived insights into the evolution of sialylation in eukaryotes: Comprehensive analysis of vertebrate β-galactoside α2,3/6-sialyltransferases (ST3Gal and ST6Gal); Molecular Diversity Preservation International; International Journal of Molecular Sciences; 17; 8; 8-20161422-0067CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/http://www.mdpi.com/1422-0067/17/8/1286/htmlinfo:eu-repo/semantics/altIdentifier/doi/10.3390/ijms17081286info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-03T10:06:29Zoai:ri.conicet.gov.ar:11336/84338instacron: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 10:06:29.992CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse |
dc.title.none.fl_str_mv |
Phylogenetic-derived insights into the evolution of sialylation in eukaryotes: Comprehensive analysis of vertebrate β-galactoside α2,3/6-sialyltransferases (ST3Gal and ST6Gal) |
title |
Phylogenetic-derived insights into the evolution of sialylation in eukaryotes: Comprehensive analysis of vertebrate β-galactoside α2,3/6-sialyltransferases (ST3Gal and ST6Gal) |
spellingShingle |
Phylogenetic-derived insights into the evolution of sialylation in eukaryotes: Comprehensive analysis of vertebrate β-galactoside α2,3/6-sialyltransferases (ST3Gal and ST6Gal) Teppa, Roxana Elin EVOLUTION FUNCTIONAL GENOMICS MOLECULAR PHYLOGENY SIALIC ACID SIALYLTRANSFERASES |
title_short |
Phylogenetic-derived insights into the evolution of sialylation in eukaryotes: Comprehensive analysis of vertebrate β-galactoside α2,3/6-sialyltransferases (ST3Gal and ST6Gal) |
title_full |
Phylogenetic-derived insights into the evolution of sialylation in eukaryotes: Comprehensive analysis of vertebrate β-galactoside α2,3/6-sialyltransferases (ST3Gal and ST6Gal) |
title_fullStr |
Phylogenetic-derived insights into the evolution of sialylation in eukaryotes: Comprehensive analysis of vertebrate β-galactoside α2,3/6-sialyltransferases (ST3Gal and ST6Gal) |
title_full_unstemmed |
Phylogenetic-derived insights into the evolution of sialylation in eukaryotes: Comprehensive analysis of vertebrate β-galactoside α2,3/6-sialyltransferases (ST3Gal and ST6Gal) |
title_sort |
Phylogenetic-derived insights into the evolution of sialylation in eukaryotes: Comprehensive analysis of vertebrate β-galactoside α2,3/6-sialyltransferases (ST3Gal and ST6Gal) |
dc.creator.none.fl_str_mv |
Teppa, Roxana Elin Petit, Daniel Plechakova, Olga Cogez, Virginie Harduin-Lepers, Anne |
author |
Teppa, Roxana Elin |
author_facet |
Teppa, Roxana Elin Petit, Daniel Plechakova, Olga Cogez, Virginie Harduin-Lepers, Anne |
author_role |
author |
author2 |
Petit, Daniel Plechakova, Olga Cogez, Virginie Harduin-Lepers, Anne |
author2_role |
author author author author |
dc.subject.none.fl_str_mv |
EVOLUTION FUNCTIONAL GENOMICS MOLECULAR PHYLOGENY SIALIC ACID SIALYLTRANSFERASES |
topic |
EVOLUTION FUNCTIONAL GENOMICS MOLECULAR PHYLOGENY SIALIC ACID SIALYLTRANSFERASES |
purl_subject.fl_str_mv |
https://purl.org/becyt/ford/1.6 https://purl.org/becyt/ford/1 |
dc.description.none.fl_txt_mv |
Cell surface of eukaryotic cells is covered with a wide variety of sialylated molecules involved in diverse biological processes and taking part in cell-cell interactions. Although the physiological relevance of these sialylated glycoconjugates in vertebrates begins to be deciphered, the origin and evolution of the genetic machinery implicated in their biosynthetic pathway are poorly understood. Among the variety of actors involved in the sialylation machinery, sialyltransferases are key enzymes for the biosynthesis of sialylated molecules. This review focus on β-galactoside α2,3/6-sialyltransferases belonging to the ST3Gal and ST6Gal families. We propose here an outline of the evolutionary history of these two major ST families. Comparative genomics, molecular phylogeny and structural bioinformatics provided insights into the functional innovations in sialic acid metabolism and enabled to explore how ST-gene function evolved in vertebrates. 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: Petit, Daniel. Université de Limoges; Francia Fil: Plechakova, Olga. Universite Lille; Francia. Centre National de la Recherche Scientifique; Francia Fil: Cogez, Virginie. Universite Lille; Francia. Centre National de la Recherche Scientifique; Francia Fil: Harduin-Lepers, Anne. Universite Lille; Francia. Centre National de la Recherche Scientifique; Francia |
description |
Cell surface of eukaryotic cells is covered with a wide variety of sialylated molecules involved in diverse biological processes and taking part in cell-cell interactions. Although the physiological relevance of these sialylated glycoconjugates in vertebrates begins to be deciphered, the origin and evolution of the genetic machinery implicated in their biosynthetic pathway are poorly understood. Among the variety of actors involved in the sialylation machinery, sialyltransferases are key enzymes for the biosynthesis of sialylated molecules. This review focus on β-galactoside α2,3/6-sialyltransferases belonging to the ST3Gal and ST6Gal families. We propose here an outline of the evolutionary history of these two major ST families. Comparative genomics, molecular phylogeny and structural bioinformatics provided insights into the functional innovations in sialic acid metabolism and enabled to explore how ST-gene function evolved in vertebrates. |
publishDate |
2016 |
dc.date.none.fl_str_mv |
2016-08 |
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/11336/84338 Teppa, Roxana Elin; Petit, Daniel; Plechakova, Olga; Cogez, Virginie; Harduin-Lepers, Anne; Phylogenetic-derived insights into the evolution of sialylation in eukaryotes: Comprehensive analysis of vertebrate β-galactoside α2,3/6-sialyltransferases (ST3Gal and ST6Gal); Molecular Diversity Preservation International; International Journal of Molecular Sciences; 17; 8; 8-2016 1422-0067 CONICET Digital CONICET |
url |
http://hdl.handle.net/11336/84338 |
identifier_str_mv |
Teppa, Roxana Elin; Petit, Daniel; Plechakova, Olga; Cogez, Virginie; Harduin-Lepers, Anne; Phylogenetic-derived insights into the evolution of sialylation in eukaryotes: Comprehensive analysis of vertebrate β-galactoside α2,3/6-sialyltransferases (ST3Gal and ST6Gal); Molecular Diversity Preservation International; International Journal of Molecular Sciences; 17; 8; 8-2016 1422-0067 CONICET Digital CONICET |
dc.language.none.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
info:eu-repo/semantics/altIdentifier/url/http://www.mdpi.com/1422-0067/17/8/1286/html info:eu-repo/semantics/altIdentifier/doi/10.3390/ijms17081286 |
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 |
Molecular Diversity Preservation International |
publisher.none.fl_str_mv |
Molecular Diversity Preservation International |
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 |
_version_ |
1842269960883142656 |
score |
13.13397 |