Of linkers and autochaperones: an unambiguous nomenclature to identify common and uncommon themes for autotransporter secretion.

I. Drobnak, E. Braselmann, J.L. Chaney, D.L. Leyton, H.D. Bernstein, T. Lithgow, S. Luirink, J.P. Nataro, P.L. Clark

Research output: Contribution to JournalArticleAcademicpeer-review

Abstract

Autotransporter (AT) proteins provide a diverse array of important virulence functions to Gram-negative bacterial pathogens, and have also been adapted for protein surface display applications. The 'autotransporter' moniker refers to early models that depicted these proteins facilitating their own translocation across the bacterial outer membrane. Although translocation is less autonomous than originally proposed, AT protein segments upstream of the C-terminal transmembrane β-barrel have nevertheless consistently been found to contribute to efficient translocation and/or folding of the N-terminal virulence region (the 'passenger'). However, defining the precise secretion functions of these AT regions has been complicated by the use of multiple overlapping and ambiguous terms to define AT sequence, structural, and functional features, including 'autochaperone', 'linker' and 'junction'. Moreover, the precise definitions and boundaries of these features vary among ATs and even among research groups, leading to an overall murky picture of the contributions of specific features to translocation. Here we propose a unified, unambiguous nomenclature for AT structural, functional and conserved sequence features, based on explicit criteria. Applied to 16 well-studied AT proteins, this nomenclature reveals new commonalities for translocation but also highlights that the autochaperone function is less closely associated with a conserved sequence element than previously believed.
Original languageEnglish
Article number1
Pages (from-to)1-16
JournalMolecular Microbiology
Volume95
Issue number1
DOIs
Publication statusPublished - 2015

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Terminology
Conserved Sequence
Virulence
Proteins
Bacterial Translocation
Type V Secretion Systems
Membrane Proteins
Membranes
Research

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Drobnak, I., Braselmann, E., Chaney, J. L., Leyton, D. L., Bernstein, H. D., Lithgow, T., ... Clark, P. L. (2015). Of linkers and autochaperones: an unambiguous nomenclature to identify common and uncommon themes for autotransporter secretion. Molecular Microbiology, 95(1), 1-16. [1]. https://doi.org/10.1111/mmi.12838
Drobnak, I. ; Braselmann, E. ; Chaney, J.L. ; Leyton, D.L. ; Bernstein, H.D. ; Lithgow, T. ; Luirink, S. ; Nataro, J.P. ; Clark, P.L. / Of linkers and autochaperones: an unambiguous nomenclature to identify common and uncommon themes for autotransporter secretion. In: Molecular Microbiology. 2015 ; Vol. 95, No. 1. pp. 1-16.
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Drobnak, I, Braselmann, E, Chaney, JL, Leyton, DL, Bernstein, HD, Lithgow, T, Luirink, S, Nataro, JP & Clark, PL 2015, 'Of linkers and autochaperones: an unambiguous nomenclature to identify common and uncommon themes for autotransporter secretion.' Molecular Microbiology, vol. 95, no. 1, 1, pp. 1-16. https://doi.org/10.1111/mmi.12838

Of linkers and autochaperones: an unambiguous nomenclature to identify common and uncommon themes for autotransporter secretion. / Drobnak, I.; Braselmann, E.; Chaney, J.L.; Leyton, D.L.; Bernstein, H.D.; Lithgow, T.; Luirink, S.; Nataro, J.P.; Clark, P.L.

In: Molecular Microbiology, Vol. 95, No. 1, 1, 2015, p. 1-16.

Research output: Contribution to JournalArticleAcademicpeer-review

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AU - Drobnak, I.

AU - Braselmann, E.

AU - Chaney, J.L.

AU - Leyton, D.L.

AU - Bernstein, H.D.

AU - Lithgow, T.

AU - Luirink, S.

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AU - Clark, P.L.

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AB - Autotransporter (AT) proteins provide a diverse array of important virulence functions to Gram-negative bacterial pathogens, and have also been adapted for protein surface display applications. The 'autotransporter' moniker refers to early models that depicted these proteins facilitating their own translocation across the bacterial outer membrane. Although translocation is less autonomous than originally proposed, AT protein segments upstream of the C-terminal transmembrane β-barrel have nevertheless consistently been found to contribute to efficient translocation and/or folding of the N-terminal virulence region (the 'passenger'). However, defining the precise secretion functions of these AT regions has been complicated by the use of multiple overlapping and ambiguous terms to define AT sequence, structural, and functional features, including 'autochaperone', 'linker' and 'junction'. Moreover, the precise definitions and boundaries of these features vary among ATs and even among research groups, leading to an overall murky picture of the contributions of specific features to translocation. Here we propose a unified, unambiguous nomenclature for AT structural, functional and conserved sequence features, based on explicit criteria. Applied to 16 well-studied AT proteins, this nomenclature reveals new commonalities for translocation but also highlights that the autochaperone function is less closely associated with a conserved sequence element than previously believed.

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