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Early origin and evolution of the FtsZ/tubulin protein family
The origin of the FtsZ/tubulin protein family was extremely relevant for life since these proteins are present in nearly all organisms, carrying out essential functions such as cell division or forming a major part of the cytoskeleton in eukaryotes. Therefore, investigating the early evolution of th...
Autores principales: | , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Frontiers Media S.A.
2023
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9871819/ https://www.ncbi.nlm.nih.gov/pubmed/36704558 http://dx.doi.org/10.3389/fmicb.2022.1100249 |
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author | Santana-Molina, Carlos del Saz-Navarro, DMaría Devos, Damien P. |
author_facet | Santana-Molina, Carlos del Saz-Navarro, DMaría Devos, Damien P. |
author_sort | Santana-Molina, Carlos |
collection | PubMed |
description | The origin of the FtsZ/tubulin protein family was extremely relevant for life since these proteins are present in nearly all organisms, carrying out essential functions such as cell division or forming a major part of the cytoskeleton in eukaryotes. Therefore, investigating the early evolution of the FtsZ/tubulin protein family could reveal crucial aspects of the diversification of the three domains of life. In this study, we revisited the phylogenies of the FtsZ/tubulin protein family in an extensive prokaryotic diversity, focusing on the main evolutionary events that occurred during its evolution. We found evidence of its early origin in the last universal common ancestor since FtsZ was present in the last common ancestor of Bacteria and Archaea. In bacteria, ftsZ genes are genomically associated with the bacterial division gene cluster, while in archaea, ftsZ duplicated prior to archaeal diversification, and one of the copies is associated with protein biosynthesis genes. Archaea have expanded the FtsZ/tubulin protein family with sequences closely related to eukaryotic tubulins. In addition, we report novel CetZ-like groups in Halobacterota and Asgardarchaeota. Investigating the C-termini of prokaryotic paralogs basal to eukaryotic tubulins, we show that archaeal CetZ, as well as the plasmidic TubZ from Firmicutes, most likely originated from archaeal FtsZ. Finally, prokaryotic tubulins are restricted to Odinarchaeaota and Prosthecobacter species, and they seem to belong to different molecular systems. However, their phylogenies suggest that they are closely related to α/β-tubulins pointing to a potential ancestrality of these eukaryotic paralogs of tubulins. |
format | Online Article Text |
id | pubmed-9871819 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2023 |
publisher | Frontiers Media S.A. |
record_format | MEDLINE/PubMed |
spelling | pubmed-98718192023-01-25 Early origin and evolution of the FtsZ/tubulin protein family Santana-Molina, Carlos del Saz-Navarro, DMaría Devos, Damien P. Front Microbiol Microbiology The origin of the FtsZ/tubulin protein family was extremely relevant for life since these proteins are present in nearly all organisms, carrying out essential functions such as cell division or forming a major part of the cytoskeleton in eukaryotes. Therefore, investigating the early evolution of the FtsZ/tubulin protein family could reveal crucial aspects of the diversification of the three domains of life. In this study, we revisited the phylogenies of the FtsZ/tubulin protein family in an extensive prokaryotic diversity, focusing on the main evolutionary events that occurred during its evolution. We found evidence of its early origin in the last universal common ancestor since FtsZ was present in the last common ancestor of Bacteria and Archaea. In bacteria, ftsZ genes are genomically associated with the bacterial division gene cluster, while in archaea, ftsZ duplicated prior to archaeal diversification, and one of the copies is associated with protein biosynthesis genes. Archaea have expanded the FtsZ/tubulin protein family with sequences closely related to eukaryotic tubulins. In addition, we report novel CetZ-like groups in Halobacterota and Asgardarchaeota. Investigating the C-termini of prokaryotic paralogs basal to eukaryotic tubulins, we show that archaeal CetZ, as well as the plasmidic TubZ from Firmicutes, most likely originated from archaeal FtsZ. Finally, prokaryotic tubulins are restricted to Odinarchaeaota and Prosthecobacter species, and they seem to belong to different molecular systems. However, their phylogenies suggest that they are closely related to α/β-tubulins pointing to a potential ancestrality of these eukaryotic paralogs of tubulins. Frontiers Media S.A. 2023-01-10 /pmc/articles/PMC9871819/ /pubmed/36704558 http://dx.doi.org/10.3389/fmicb.2022.1100249 Text en Copyright © 2023 Santana-Molina, Saz-Navarro and Devos. https://creativecommons.org/licenses/by/4.0/This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms. |
spellingShingle | Microbiology Santana-Molina, Carlos del Saz-Navarro, DMaría Devos, Damien P. Early origin and evolution of the FtsZ/tubulin protein family |
title | Early origin and evolution of the FtsZ/tubulin protein family |
title_full | Early origin and evolution of the FtsZ/tubulin protein family |
title_fullStr | Early origin and evolution of the FtsZ/tubulin protein family |
title_full_unstemmed | Early origin and evolution of the FtsZ/tubulin protein family |
title_short | Early origin and evolution of the FtsZ/tubulin protein family |
title_sort | early origin and evolution of the ftsz/tubulin protein family |
topic | Microbiology |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9871819/ https://www.ncbi.nlm.nih.gov/pubmed/36704558 http://dx.doi.org/10.3389/fmicb.2022.1100249 |
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