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Journal Article

A trimeric lipoprotein assists in trimeric autotransporter biogenesis in enterobacteria

MPS-Authors
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Grin,  I
Department Protein Evolution, Max Planck Institute for Developmental Biology, Max Planck Society;

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Hartmann,  MD
Department Protein Evolution, Max Planck Institute for Developmental Biology, Max Planck Society;
Molecular Recognition and Catalysis Group, Department Protein Evolution, Max Planck Institute for Developmental Biology, Max Planck Society;

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Sauer,  G
Department Biochemistry, Max Planck Institute for Developmental Biology, Max Planck Society;

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Hernandez Alvarez,  B
Department Protein Evolution, Max Planck Institute for Developmental Biology, Max Planck Society;
Conservation of Protein Structure and Function Group, Department Protein Evolution, Max Planck Institute for Developmental Biology, Max Planck Society;

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Lupas,  AN
Department Protein Evolution, Max Planck Institute for Developmental Biology, Max Planck Society;

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Linke,  D
Department Protein Evolution, Max Planck Institute for Developmental Biology, Max Planck Society;

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Citation

Grin, I., Hartmann, M., Sauer, G., Hernandez Alvarez, B., Schütz, M., Wagner, S., et al. (2014). A trimeric lipoprotein assists in trimeric autotransporter biogenesis in enterobacteria. The Journal of Biological Chemistry, 289(11), 3788-3798. doi:10.1074/jbc.M113.513275.


Cite as: https://hdl.handle.net/21.11116/0000-000A-B6DC-1
Abstract
Trimeric autotransporter adhesins (TAAs) are important virulence factors of many Gram-negative bacterial pathogens. TAAs form fibrous, adhesive structures on the bacterial cell surface. Their N-terminal extracellular domains are exported through a C-terminal membrane pore; the insertion of the pore domain into the bacterial outer membrane follows the rules of β-barrel transmembrane protein biogenesis and is dependent on the essential Bam complex. We have recently described the full fiber structure of SadA, a TAA of unknown function in Salmonella and other enterobacteria. In this work, we describe the structure and function of SadB, a small inner membrane lipoprotein. The sadB gene is located in an operon with sadA; orthologous operons are only found in enterobacteria, whereas other TAAs are not typically associated with lipoproteins. Strikingly, SadB is also a trimer, and its co-expression with SadA has a direct influence on SadA structural integrity. This is the first report of a specific export factor of a TAA, suggesting that at least in some cases TAA autotransport is assisted by additional periplasmic proteins.