A mortise–tenon joint in the transmembrane domain modulates autotransporter assembly into bacterial outer membranes

Denisse L. Leyton, Matthew D. Johnson, Rajiv Thapa, Gerard H.M. Huysmans, Rhys A. Dunstan, Nermin Celik, Hsin-Hui Shen, Dorothy Loo, Matthew J. Belousoff, Anthony W. Purcell, Ian R. Henderson, Travis Beddoe, Jamie Rossjohn, Lisandra L. Martin, Richard A. Strugnell and Trevor Lithgow ()
Additional contact information
Denisse L. Leyton: Monash University
Matthew D. Johnson: Monash University
Rajiv Thapa: Monash University
Gerard H.M. Huysmans: Institut Pasteur, Molecular Genetics Unit, rue du Dr Roux
Rhys A. Dunstan: Monash University
Nermin Celik: Monash University
Hsin-Hui Shen: Monash University
Dorothy Loo: Monash University
Matthew J. Belousoff: Monash University
Anthony W. Purcell: Monash University
Ian R. Henderson: School of Immunity and Infection, University of Birmingham
Travis Beddoe: Monash University
Jamie Rossjohn: Monash University
Lisandra L. Martin: School of Chemistry, Monash University
Richard A. Strugnell: The University of Melbourne
Trevor Lithgow: Monash University

Nature Communications, 2014, vol. 5, issue 1, 1-11

Abstract: Abstract Bacterial autotransporters comprise a 12-stranded membrane-embedded β-barrel domain, which must be folded in a process that entraps segments of an N-terminal passenger domain. This first stage of autotransporter folding determines whether subsequent translocation can deliver the N-terminal domain to its functional form on the bacterial cell surface. Here, paired glycine-aromatic ‘mortise and tenon’ motifs are shown to join neighbouring β-strands in the C-terminal barrel domain, and mutations within these motifs slow the rate and extent of passenger domain translocation to the surface of bacterial cells. In line with this, biophysical studies of the autotransporter Pet show that the conserved residues significantly quicken completion of the folding reaction and promote stability of the autotransporter barrel domain. Comparative genomics demonstrate conservation of glycine-aromatic residue pairings through evolution as a previously unrecognized feature of all autotransporter proteins.

Date: 2014
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DOI: 10.1038/ncomms5239

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