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

Research output: Contribution to journalArticle

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A mortise-tenon joint in the transmembrane domain modulates autotransporter assembly into bacterial outer membranes. / Leyton, Denisse L; Johnson, Matthew D; Thapa, Rajiv; Huysmans, Gerard H M; Dunstan, Rhys A; Celik, Nermin; Shen, Hsin-Hui; Loo, Dorothy; Belousoff, Matthew J; Purcell, Anthony W; Henderson, Ian R; Beddoe, Travis; Rossjohn, Jamie; Martin, Lisandra L; Strugnell, Richard A; Lithgow, Trevor.

In: Nature Communications, Vol. 5, 26.06.2014, p. 4239.

Research output: Contribution to journalArticle

Harvard

Leyton, DL, Johnson, MD, Thapa, R, Huysmans, GHM, Dunstan, RA, Celik, N, Shen, H-H, Loo, D, Belousoff, MJ, Purcell, AW, Henderson, IR, Beddoe, T, Rossjohn, J, Martin, LL, Strugnell, RA & Lithgow, T 2014, 'A mortise-tenon joint in the transmembrane domain modulates autotransporter assembly into bacterial outer membranes', Nature Communications, vol. 5, pp. 4239. https://doi.org/10.1038/ncomms5239

APA

Leyton, D. L., Johnson, M. D., Thapa, R., Huysmans, G. H. M., Dunstan, R. A., Celik, N., Shen, H-H., Loo, D., Belousoff, M. J., Purcell, A. W., Henderson, I. R., Beddoe, T., Rossjohn, J., Martin, L. L., Strugnell, R. A., & Lithgow, T. (2014). A mortise-tenon joint in the transmembrane domain modulates autotransporter assembly into bacterial outer membranes. Nature Communications, 5, 4239. https://doi.org/10.1038/ncomms5239

Vancouver

Author

Leyton, Denisse L ; Johnson, Matthew D ; Thapa, Rajiv ; Huysmans, Gerard H M ; Dunstan, Rhys A ; Celik, Nermin ; Shen, Hsin-Hui ; Loo, Dorothy ; Belousoff, Matthew J ; Purcell, Anthony W ; Henderson, Ian R ; Beddoe, Travis ; Rossjohn, Jamie ; Martin, Lisandra L ; Strugnell, Richard A ; Lithgow, Trevor. / A mortise-tenon joint in the transmembrane domain modulates autotransporter assembly into bacterial outer membranes. In: Nature Communications. 2014 ; Vol. 5. pp. 4239.

Bibtex

@article{d45fdd82f80e4304a74e0e75783ea41a,
title = "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.",
keywords = "Amino Acid Motifs, Amino Acid Sequence, Bacterial Outer Membrane Proteins, Bacterial Proteins, Bacterial Toxins, Carboxylic Ester Hydrolases, Carrier Proteins, Conserved Sequence, Enterotoxins, Escherichia coli Proteins, Models, Molecular, Protein Folding, Protein Structure, Secondary, Protein Structure, Tertiary, Protein Transport, Pseudomonas aeruginosa, Serine Endopeptidases",
author = "Leyton, {Denisse L} and Johnson, {Matthew D} and Rajiv Thapa and Huysmans, {Gerard H M} and Dunstan, {Rhys A} and Nermin Celik and Hsin-Hui Shen and Dorothy Loo and Belousoff, {Matthew J} and Purcell, {Anthony W} and Henderson, {Ian R} and Travis Beddoe and Jamie Rossjohn and Martin, {Lisandra L} and Strugnell, {Richard A} and Trevor Lithgow",
year = "2014",
month = jun,
day = "26",
doi = "10.1038/ncomms5239",
language = "English",
volume = "5",
pages = "4239",
journal = "Nature Communications",
issn = "2041-1723",
publisher = "Springer",

}

RIS

TY - JOUR

T1 - A mortise-tenon joint in the transmembrane domain modulates autotransporter assembly into bacterial outer membranes

AU - Leyton, Denisse L

AU - Johnson, Matthew D

AU - Thapa, Rajiv

AU - Huysmans, Gerard H M

AU - Dunstan, Rhys A

AU - Celik, Nermin

AU - Shen, Hsin-Hui

AU - Loo, Dorothy

AU - Belousoff, Matthew J

AU - Purcell, Anthony W

AU - Henderson, Ian R

AU - Beddoe, Travis

AU - Rossjohn, Jamie

AU - Martin, Lisandra L

AU - Strugnell, Richard A

AU - Lithgow, Trevor

PY - 2014/6/26

Y1 - 2014/6/26

N2 - 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.

AB - 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.

KW - Amino Acid Motifs

KW - Amino Acid Sequence

KW - Bacterial Outer Membrane Proteins

KW - Bacterial Proteins

KW - Bacterial Toxins

KW - Carboxylic Ester Hydrolases

KW - Carrier Proteins

KW - Conserved Sequence

KW - Enterotoxins

KW - Escherichia coli Proteins

KW - Models, Molecular

KW - Protein Folding

KW - Protein Structure, Secondary

KW - Protein Structure, Tertiary

KW - Protein Transport

KW - Pseudomonas aeruginosa

KW - Serine Endopeptidases

U2 - 10.1038/ncomms5239

DO - 10.1038/ncomms5239

M3 - Article

C2 - 24967730

VL - 5

SP - 4239

JO - Nature Communications

JF - Nature Communications

SN - 2041-1723

ER -