Abstract
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.
Original language | English |
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Article number | 2 |
Journal | Biology Direct |
Volume | 3 |
DOIs | |
State | Published - Jan 25 2008 |
Funding
MP is supported by the U.S. Department of Energy, Office of Science, Biological and Environmental Research programs at Oak Ridge National Laboratory (ORNL). ORNL is managed by UT-Battelle, LLC, for the U.S. Department of Energy under contract DE-AC05-00OR22725. KSM and EVK are supported by the Intramural Research Program of the National Institutes of Health, National Library of Medicine. M.P. acknowledges the support obtained from the Joint Genome Institute with the Ignicoccus hos-pitalis genome sequencing and analysis.
Funders | Funder number |
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National Institutes of Health | Z01LM000073 |
U.S. Department of Energy | |
U.S. National Library of Medicine | |
Oak Ridge National Laboratory | DE-AC05-00OR22725 |