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

Mircea Podar1*, Mark A Wall2, Kira S Makarova3 and Eugene V Koonin3

Author Affiliations

1 Biosciences Division and the Bioenergy Science Center, Oak Ridge National Laboratory, 1 Bethel Valley Rd, Oak Ridge, TN 37831, USA

2 Bioinformatics Department, Verenium Corporation, 4955 Directors Place, San Diego, CA 92121, USA

3 National Center for Biotechnology Information, National Library of Medicine, National Institutes of Health, Bethesda, MD 20894, USA

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Biology Direct 2008, 3:2  doi:10.1186/1745-6150-3-2

Published: 25 January 2008


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