期刊
CELL REPORTS
卷 23, 期 9, 页码 2782-2794出版社
CELL PRESS
DOI: 10.1016/j.celrep.2018.04.093
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资金
- Multi-modal Australian Sciences Imaging and Visualisation Environment (MASSIVE)
- Australian Research Council (ARC) Laureate fellowship award [FL30100038]
- ARC LIEF grant [LE150100110]
- NHMRC program grant [1092262]
- ARC
- ARC Laureate postgraduate research scholarship
- National Health and Medical Research Council of Australia [1092262] Funding Source: NHMRC
- Australian Research Council [LE150100110] Funding Source: Australian Research Council
The beta-barrel assembly machinery (BAM) complex is essential for localization of surface proteins on bacterial cells, but the mechanism by which it functions is unclear. We developed a direct stochastic optical reconstruction microscopy (dSTORM) methodology to view the BAM complex in situ. Single-cell analysis showed that discrete membrane precincts housing several BAM complexes are distributed across the E. coli surface, with a nearest neighbor distance of similar to 200 nm. The auxiliary lipoprotein subunit BamB was crucial for this spatial distribution, and in situ crosslinking shows that BamB makes intimate contacts with BamA and BamB in neighboring BAM complexes within the precinct. The BAM complex precincts swell when outer membrane protein synthesis is maximal, visual proof that the precincts are active in protein assembly. This nanoscale interrogation of the BAM complex in situ suggests a model whereby bacterial outer membranes contain highly organized assembly precincts to drive integral protein assembly.
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