A modular BAM complex in the outer membrane of the alpha-proteobacterium caulobacter crescentus

Khatira Anwari, Sebastian Poggio, Andrew Perry, Xenia Gatsos, Sri Harsha Ramarathinam, Nicholas A Williamson, Nicholas Noinaj, Susan Buchanan, Kip Gabriel, Anthony W Purcell, Christine Jacobs-Wagner, Trevor Lithgow

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53 Citations (Scopus)


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.
Original languageEnglish
Pages (from-to)1 - 8
Number of pages8
JournalPLoS ONE
Issue number1 (e8619)
Publication statusPublished - 2010

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