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 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.
Podar
Mircea
M
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
MA
Makarova
Kira S
KS
Koonin
Eugene V
EV
D000595:Amino Acid Sequence; D000818:Animals; D019843:Archaeal Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D001693:Biological Transport, Active / Q000235:genetics; D003198:Computer Simulation; D022162:Cytoplasmic Vesicles / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D005057:Eukaryotic Cells / Q000737:chemistry / Q000378:metabolism*; D019143:Evolution, Molecular; D008958:Models, Molecular; D008969:Molecular Sequence Data; D011387:Prokaryotic Cells / Q000737:chemistry / Q000378:metabolism; D017434:Protein Structure, Tertiary / Q000235:genetics
D019843:Archaeal Proteins