The prokaryotic V4R domain is the likely ancestor of a key component of the eukaryotic vesicle transport system

Intracellular vesicle traffic that enables delivery of proteins between the endoplasmic reticulum, Golgi and various endosomal subcompartments is one of the hallmarks of the eukaryotic cell. Its evolutionary history is not well understood but the process itself and the core vesicle traffic machinery...

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Detalles Bibliográficos
Autores principales: Podar, Mircea, Wall, Mark A, Makarova, Kira S, Koonin, Eugene V
Formato: Texto
Lenguaje:English
Publicado: BioMed Central 2008
Materias:
Discovery Notes
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2253512/
https://www.ncbi.nlm.nih.gov/pubmed/18221539
http://dx.doi.org/10.1186/1745-6150-3-2
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author Podar, Mircea
Wall, Mark A
Makarova, Kira S
Koonin, Eugene V
author_facet Podar, Mircea
Wall, Mark A
Makarova, Kira S
Koonin, Eugene V
author_sort Podar, Mircea
collection PubMed
description Intracellular vesicle traffic that enables delivery of proteins between the endoplasmic reticulum, Golgi and various endosomal subcompartments is one of the hallmarks of the eukaryotic cell. Its evolutionary history is not well understood but the process itself and the core vesicle traffic machinery are believed to be ancient. We show here that the 4-vinyl reductase (V4R) protein domain present in bacteria and archaea is homologous to the Bet3 subunit of the TRAPP1 vesicle-tethering complex that is conserved in all eukaryotes. This suggests, for the first time, a prokaryotic origin for one of the key eukaryotic trafficking proteins. This article was reviewed by Gaspar Jekely and Mark A. Ragan
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spelling pubmed-22535122008-02-23 The prokaryotic V4R domain is the likely ancestor of a key component of the eukaryotic vesicle transport system Podar, Mircea Wall, Mark A Makarova, Kira S Koonin, Eugene V Biol Direct Discovery Notes Intracellular vesicle traffic that enables delivery of proteins between the endoplasmic reticulum, Golgi and various endosomal subcompartments is one of the hallmarks of the eukaryotic cell. Its evolutionary history is not well understood but the process itself and the core vesicle traffic machinery are believed to be ancient. We show here that the 4-vinyl reductase (V4R) protein domain present in bacteria and archaea is homologous to the Bet3 subunit of the TRAPP1 vesicle-tethering complex that is conserved in all eukaryotes. This suggests, for the first time, a prokaryotic origin for one of the key eukaryotic trafficking proteins. This article was reviewed by Gaspar Jekely and Mark A. Ragan BioMed Central 2008-01-25 /pmc/articles/PMC2253512/ /pubmed/18221539 http://dx.doi.org/10.1186/1745-6150-3-2 Text en Copyright © 2008 Podar et al; licensee BioMed Central Ltd. http://creativecommons.org/licenses/by/2.0 This is an Open Access article distributed under the terms of the Creative Commons Attribution License ( (http://creativecommons.org/licenses/by/2.0) ), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
spellingShingle Discovery Notes
Podar, Mircea
Wall, Mark A
Makarova, Kira S
Koonin, Eugene V
The prokaryotic V4R domain is the likely ancestor of a key component of the eukaryotic vesicle transport system
title The prokaryotic V4R domain is the likely ancestor of a key component of the eukaryotic vesicle transport system
title_full The prokaryotic V4R domain is the likely ancestor of a key component of the eukaryotic vesicle transport system
title_fullStr The prokaryotic V4R domain is the likely ancestor of a key component of the eukaryotic vesicle transport system
title_full_unstemmed The prokaryotic V4R domain is the likely ancestor of a key component of the eukaryotic vesicle transport system
title_short The prokaryotic V4R domain is the likely ancestor of a key component of the eukaryotic vesicle transport system
title_sort prokaryotic v4r domain is the likely ancestor of a key component of the eukaryotic vesicle transport system
topic Discovery Notes
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2253512/
https://www.ncbi.nlm.nih.gov/pubmed/18221539
http://dx.doi.org/10.1186/1745-6150-3-2
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