TY - JOUR
T1 - A modular BAM complex in the outer membrane of the alpha-proteobacterium caulobacter crescentus
AU - Anwari, Khatira
AU - Poggio, Sebastian
AU - Perry, Andrew
AU - Gatsos, Xenia
AU - Ramarathinam, Sri Harsha
AU - Williamson, Nicholas A
AU - Noinaj, Nicholas
AU - Buchanan, Susan
AU - Gabriel, Kip
AU - Purcell, Anthony W
AU - Jacobs-Wagner, Christine
AU - Lithgow, Trevor
PY - 2010
Y1 - 2010
N2 - Mitochondria are organelles derived from an intracellular alpha-proteobacterium. The biogenesis of mitochondria relies on the assembly of beta-barrel proteins into the mitochondrial outer membrane, a process inherited from the bacterial ancestor. Caulobacter crescentus is an alpha-proteobacterium, and the BAM (beta-barrel assembly machinery) complex was purified and characterized from this model organism. Like the mitochondrial sorting and assembly machinery complex, we find the BAM complex to be modular in nature. A approximately 150 kDa core BAM complex containing BamA, BamB, BamD, and BamE associates with additional modules in the outer membrane. One of these modules, Pal, is a lipoprotein that provides a means for anchorage to the peptidoglycan layer of the cell wall. We suggest the modular design of the BAM complex facilitates access to substrates from the protein translocase in the inner membrane.
AB - Mitochondria are organelles derived from an intracellular alpha-proteobacterium. The biogenesis of mitochondria relies on the assembly of beta-barrel proteins into the mitochondrial outer membrane, a process inherited from the bacterial ancestor. Caulobacter crescentus is an alpha-proteobacterium, and the BAM (beta-barrel assembly machinery) complex was purified and characterized from this model organism. Like the mitochondrial sorting and assembly machinery complex, we find the BAM complex to be modular in nature. A approximately 150 kDa core BAM complex containing BamA, BamB, BamD, and BamE associates with additional modules in the outer membrane. One of these modules, Pal, is a lipoprotein that provides a means for anchorage to the peptidoglycan layer of the cell wall. We suggest the modular design of the BAM complex facilitates access to substrates from the protein translocase in the inner membrane.
U2 - 10.1371/journal.pone.0008619
DO - 10.1371/journal.pone.0008619
M3 - Article
SN - 1932-6203
VL - 5
JO - PLoS ONE
JF - PLoS ONE
IS - 1
M1 - e8619
ER -