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

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, a...

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Bibliographic Details
Published in:PloS one 2010-01, Vol.5 (1), p.e8619-e8619
Main Authors: Anwari, Khatira, Poggio, Sebastian, Perry, Andrew, Gatsos, Xenia, Ramarathinam, Sri Harsha, Williamson, Nicholas A, Noinaj, Nicholas, Buchanan, Susan, Gabriel, Kipros, Purcell, Anthony W, Jacobs-Wagner, Christine, Lithgow, Trevor
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Assembly
Bacteria
Bacterial Outer Membrane Proteins - chemistry
Bacterial Outer Membrane Proteins - metabolism
Bacterial proteins
Base Sequence
Biochemistry
Biochemistry/Cell Signaling and Trafficking Structures
Biochemistry/Membrane Proteins and Energy Transduction
Biosynthesis
Caulobacter crescentus - metabolism
Cell Biology/Membranes and Sorting
Cell Biology/Microbial Growth and Development
Cell walls
Developmental biology
Diabetes
DNA Primers
E coli
Electrophoresis, Polyacrylamide Gel
Escherichia coli
Kidney diseases
Machinery and equipment
Mass Spectrometry
Membranes
Mitochondria
Modular design
Modules
Molecular biology
Molecular Sequence Data
Neisseria meningitidis
Organelles
Pathogenesis
Peptidoglycans
Polymerase Chain Reaction
Polypeptides
Proteins
Pseudomonas aeruginosa
Sequence Homology, Amino Acid
Substrates
Translocase
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Summary: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.
ISSN:1932-6203
1932-6203
DOI:10.1371/journal.pone.0008619