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  Type V secretion: mechanism(s) of autotransport through the bacterial outer membrane

Leo, J., Grin, I., & Linke, D. (2012). Type V secretion: mechanism(s) of autotransport through the bacterial outer membrane. Philosophical Transactions of the Royal Society of London, Series B: Biological Sciences, 367(1592), 1088-1101. doi:10.1098/rstb.2011.0208.

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Leo, JC1, Author           
Grin, I1, Author           
Linke, D1, Author           
Affiliations:
1Department Protein Evolution, Max Planck Institute for Developmental Biology, Max Planck Society, ou_3375791              

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 Abstract: Autotransport in Gram-negative bacteria denotes the ability of surface-localized proteins to cross the outer membrane (OM) autonomously. Autotransporters perform this task with the help of a β-barrel transmembrane domain localized in the OM. Different classes of autotransporters have been investigated in detail in recent years; classical monomeric but also trimeric autotransporters comprise many important bacterial virulence factors. So do the two-partner secretion systems, which are a special case as the transported protein resides on a different polypeptide chain than the transporter. Despite the great interest in these proteins, the exact mechanism of the transport process remains elusive. Moreover, different periplasmic and OM factors have been identified that play a role in the translocation, making the term 'autotransport' debatable. In this review, we compile the wealth of details known on the mechanism of single autotransporters from different classes and organisms, and put them into a bigger perspective. We also discuss recently discovered or rediscovered classes of autotransporters.

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 Dates: 2012-04
 Publication Status: Issued
 Pages: -
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 Table of Contents: -
 Rev. Type: -
 Identifiers: DOI: 10.1098/rstb.2011.0208
PMID: 22411980
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Title: Philosophical Transactions of the Royal Society of London, Series B: Biological Sciences
  Other : Philosophical Transactions B
  Abbreviation : Phil. Trans. R. Soc. B
Source Genre: Journal
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Publ. Info: London : Royal Society
Pages: - Volume / Issue: 367 (1592) Sequence Number: - Start / End Page: 1088 - 1101 Identifier: ISSN: 0962-8436
CoNE: https://pure.mpg.de/cone/journals/resource/963017382021_1