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  A trimeric lipoprotein assists in trimeric autotransporter biogenesis in enterobacteria

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.

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 Creators:
Grin, I1, Author           
Hartmann, MD1, 2, Author           
Sauer, G3, Author           
Hernandez Alvarez, B1, 4, Author           
Schütz, M, Author
Wagner, S, Author
Madlung, J, Author
Macek, B, Author           
Felipe-Lopez, A, Author
Hensel, M, Author
Lupas, AN1, Author           
Linke, D1, Author           
Affiliations:
1Department Protein Evolution, Max Planck Institute for Developmental Biology, Max Planck Society, ou_3375791              
2Molecular Recognition and Catalysis Group, Department Protein Evolution, Max Planck Institute for Developmental Biology, Max Planck Society, ou_3477392              
3Department Biochemistry, Max Planck Institute for Developmental Biology, Max Planck Society, Max-Planck-Ring 5, 72076 Tübingen, DE, ou_3375718              
4Conservation of Protein Structure and Function Group, Department Protein Evolution, Max Planck Institute for Developmental Biology, Max Planck Society, ou_3477389              

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 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.

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 Dates: 2014-03
 Publication Status: Issued
 Pages: -
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 Table of Contents: -
 Rev. Type: -
 Identifiers: DOI: 10.1074/jbc.M113.513275
PMID: 24369174
 Degree: -

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Title: The Journal of Biological Chemistry
  Other : JBC
  Abbreviation : J. Biol. Chem.
Source Genre: Journal
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Publ. Info: Baltimore, etc. : American Society for Biochemistry and Molecular Biology [etc.]
Pages: - Volume / Issue: 289 (11) Sequence Number: - Start / End Page: 3788 - 3798 Identifier: ISSN: 0021-9258
CoNE: https://pure.mpg.de/cone/journals/resource/954925410826_1