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Updated: Jan 22, 2026

Size Exclusion Chromatography to Analyze Bacterial Outer Membrane Vesicle Heterogeneity
Published on: March 31, 2021
Assembly and targeting of secretins in the bacterial outer membrane
Janani Natarajan1, Nidhi Singh2, Doron Rapaport1
1Interfaculty Institute of Biochemistry, University of Tübingen, Hoppe-Seyler-Str. 4, 72076 Tübingen, Germany.
Abstract:
In Gram-negative bacteria, secretion of toxins ensure the survival of the bacterium. Such toxins are secreted by sophisticated multiprotein systems. The most conserved part in some of these secretion systems are components, called secretins, which form the outer membrane ring in these systems. Recent structural studies shed some light on the oligomeric organization of secretins. However, the mechanisms by which these proteins are targeted to the outer membrane and assemble there into ring structures are still not fully understood. This review discusses the various species-specific targeting and assembly pathways that are taken by secretins in order to form their functional oligomers.
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