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PMID: 18221539 Published · epublish English Comparative Study Journal Article Research Support, N.I.H., Intramural Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, Non-P.H.S. Review

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

Biology direct ·Vol. 3 ·2008-01-25 ·Pages 2

Podar M, Wall MA, Makarova KS, Koonin EV

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.

MeSH Terms
Amino Acid Sequence Animals Archaeal Proteins/chemistry,genetics,metabolism Biological Transport, Active/genetics Computer Simulation Cytoplasmic Vesicles/chemistry,genetics,metabolism Eukaryotic Cells/chemistry,metabolism Evolution, Molecular Models, Molecular Molecular Sequence Data Prokaryotic Cells/chemistry,metabolism Protein Structure, Tertiary/genetics
Chemicals
Archaeal Proteins
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Podar Mircea
Biosciences Division and the Bioenergy Science Center, Oak Ridge National Laboratory, 1 Bethel Valley Rd, Oak Ridge, TN 37831, USA. podarm@ornl.gov
Wall Mark A
Makarova Kira S
Koonin Eugene V
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Article Info
Journal
Biology direct
Abbr.
Biol Direct
ISSN
1745-6150
DOI
10.1186/1745-6150-3-2
Email
podarm@ornl.gov
Published
2008-01-25
Epub
2008-00-25
Pages
2
Language
English
Region
England
NLM ID
101258412
PMCID
PMC2253512
Subset
IM
Grants
Intramural NIH HHS · United States
External Links
PubMed source DOI: 10.1186/1745-6150-3-2 PMC Full Text View journal details
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