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

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.

journal_name

Nat Commun

journal_title

Nature communications

authors

Leyton DL,Johnson MD,Thapa R,Huysmans GH,Dunstan RA,Celik N,Shen HH,Loo D,Belousoff MJ,Purcell AW,Henderson IR,Beddoe T,Rossjohn J,Martin LL,Strugnell RA,Lithgow T

doi

10.1038/ncomms5239

subject

Has Abstract

pub_date

2014-06-26 00:00:00

pages

4239

issn

2041-1723

pii

ncomms5239

journal_volume

5

pub_type

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