Journal
MOLECULAR MICROBIOLOGY
Volume 95, Issue 1, Pages 1-16Publisher
WILEY
DOI: 10.1111/mmi.12838
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Funding
- NIH [R01 GM097573]
- Chemistry-Biochemistry-Biology Interface Program [T32 GM075762]
- College of Science at the University of Notre Dame
- Clare Boothe Luce Graduate Fellowship
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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 -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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