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Reconstruction of the sialylation pathway in the ancestor of eukaryotes
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...
Autores principales: | , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Nature Publishing Group UK
2018
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5811610/ https://www.ncbi.nlm.nih.gov/pubmed/29440651 http://dx.doi.org/10.1038/s41598-018-20920-1 |
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author | Petit, Daniel Teppa, Elin Cenci, Ugo Ball, Steven Harduin-Lepers, Anne |
author_facet | Petit, Daniel Teppa, Elin Cenci, Ugo Ball, Steven Harduin-Lepers, Anne |
author_sort | Petit, Daniel |
collection | PubMed |
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. |
format | Online Article Text |
id | pubmed-5811610 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2018 |
publisher | Nature Publishing Group UK |
record_format | MEDLINE/PubMed |
spelling | pubmed-58116102018-02-16 Reconstruction of the sialylation pathway in the ancestor of eukaryotes Petit, Daniel Teppa, Elin Cenci, Ugo Ball, Steven Harduin-Lepers, Anne Sci Rep Article 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. Nature Publishing Group UK 2018-02-13 /pmc/articles/PMC5811610/ /pubmed/29440651 http://dx.doi.org/10.1038/s41598-018-20920-1 Text en © The Author(s) 2018 Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/. |
spellingShingle | Article Petit, Daniel Teppa, Elin Cenci, Ugo Ball, Steven Harduin-Lepers, Anne Reconstruction of the sialylation pathway in the ancestor of eukaryotes |
title | 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_short | Reconstruction of the sialylation pathway in the ancestor of eukaryotes |
title_sort | reconstruction of the sialylation pathway in the ancestor of eukaryotes |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5811610/ https://www.ncbi.nlm.nih.gov/pubmed/29440651 http://dx.doi.org/10.1038/s41598-018-20920-1 |
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