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 Communjournal_title
Nature communicationsauthors
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 Tdoi
10.1038/ncomms5239subject
Has Abstractpub_date
2014-06-26 00:00:00pages
4239issn
2041-1723pii
ncomms5239journal_volume
5pub_type
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