Structure and function of BamE within the outer membrane and the β-barrel assembly machine

Timothy J. Knowles; Douglas F. Browning; Mark Jeeves; Riyaz Maderbocus; Sandya Rajesh; Pooja Sridhar; Eleni Manoli; Danielle Emery; Ulf Sommer; Ashley Spencer; Denisse L. Leyton; Derrick Squire; Roy R. Chaudhuri; Mark R. Viant; Adam F. Cunningham; Ian R. Henderson; Michael Overduin

doi:10.1038/embor.2010.202

Structure and function of BamE within the outer membrane and the β-barrel assembly machine

Timothy J. Knowles, Douglas F. Browning, Mark Jeeves, Riyaz Maderbocus, Sandya Rajesh, Pooja Sridhar, Eleni Manoli, Danielle Emery, Ulf Sommer, Ashley Spencer, Denisse L. Leyton, Derrick Squire, Roy R. Chaudhuri, Mark R. Viant, Adam F. Cunningham, Ian R. Henderson, Michael Overduin

Research output: Contribution to journal › Article › peer-review

78 Citations (Scopus)

Abstract

Insertion of folded proteins into the outer membrane of Gram-negative bacteria is mediated by the essential β2-barrel assembly machine (Bam). Here, we report the native structure and mechanism of a core component of this complex, BamE, and show that it is exclusively monomeric in its native environment of the periplasm, but is able to adopt a distinct dimeric conformation in the cytoplasm. BamE is shown to bind specifically to phosphatidylglycerol, and comprehensive mutagenesis and interaction studies have mapped key determinants for complex binding, outer membrane integrity and cell viability, as well as revealing the role of BamE within the Bam complex.

Original language	English
Pages (from-to)	123-128
Number of pages	6
Journal	EMBO Reports
Volume	12
Issue number	2
DOIs	https://doi.org/10.1038/embor.2010.202
Publication status	Published - Feb 2011
Externally published	Yes

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Knowles, T. J., Browning, D. F., Jeeves, M., Maderbocus, R., Rajesh, S., Sridhar, P., Manoli, E., Emery, D., Sommer, U., Spencer, A., Leyton, D. L., Squire, D., Chaudhuri, R. R., Viant, M. R., Cunningham, A. F., Henderson, I. R., & Overduin, M. (2011). Structure and function of BamE within the outer membrane and the β-barrel assembly machine. EMBO Reports, 12(2), 123-128. https://doi.org/10.1038/embor.2010.202

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title = "Structure and function of BamE within the outer membrane and the β-barrel assembly machine",

abstract = "Insertion of folded proteins into the outer membrane of Gram-negative bacteria is mediated by the essential β2-barrel assembly machine (Bam). Here, we report the native structure and mechanism of a core component of this complex, BamE, and show that it is exclusively monomeric in its native environment of the periplasm, but is able to adopt a distinct dimeric conformation in the cytoplasm. BamE is shown to bind specifically to phosphatidylglycerol, and comprehensive mutagenesis and interaction studies have mapped key determinants for complex binding, outer membrane integrity and cell viability, as well as revealing the role of BamE within the Bam complex.",

keywords = "Bam complex, BamE, Omp85, SmpA, outer membrane biogenesis",

author = "Knowles, {Timothy J.} and Browning, {Douglas F.} and Mark Jeeves and Riyaz Maderbocus and Sandya Rajesh and Pooja Sridhar and Eleni Manoli and Danielle Emery and Ulf Sommer and Ashley Spencer and Leyton, {Denisse L.} and Derrick Squire and Chaudhuri, {Roy R.} and Viant, {Mark R.} and Cunningham, {Adam F.} and Henderson, {Ian R.} and Michael Overduin",

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doi = "10.1038/embor.2010.202",

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Knowles, TJ, Browning, DF, Jeeves, M, Maderbocus, R, Rajesh, S, Sridhar, P, Manoli, E, Emery, D, Sommer, U, Spencer, A, Leyton, DL, Squire, D, Chaudhuri, RR, Viant, MR, Cunningham, AF, Henderson, IR & Overduin, M 2011, 'Structure and function of BamE within the outer membrane and the β-barrel assembly machine', EMBO Reports, vol. 12, no. 2, pp. 123-128. https://doi.org/10.1038/embor.2010.202

TY - JOUR

T1 - Structure and function of BamE within the outer membrane and the β-barrel assembly machine

AU - Knowles, Timothy J.

AU - Browning, Douglas F.

AU - Jeeves, Mark

AU - Maderbocus, Riyaz

AU - Rajesh, Sandya

AU - Sridhar, Pooja

AU - Manoli, Eleni

AU - Emery, Danielle

AU - Sommer, Ulf

AU - Spencer, Ashley

AU - Leyton, Denisse L.

AU - Squire, Derrick

AU - Chaudhuri, Roy R.

AU - Viant, Mark R.

AU - Cunningham, Adam F.

AU - Henderson, Ian R.

AU - Overduin, Michael

PY - 2011/2

Y1 - 2011/2

N2 - Insertion of folded proteins into the outer membrane of Gram-negative bacteria is mediated by the essential β2-barrel assembly machine (Bam). Here, we report the native structure and mechanism of a core component of this complex, BamE, and show that it is exclusively monomeric in its native environment of the periplasm, but is able to adopt a distinct dimeric conformation in the cytoplasm. BamE is shown to bind specifically to phosphatidylglycerol, and comprehensive mutagenesis and interaction studies have mapped key determinants for complex binding, outer membrane integrity and cell viability, as well as revealing the role of BamE within the Bam complex.

AB - Insertion of folded proteins into the outer membrane of Gram-negative bacteria is mediated by the essential β2-barrel assembly machine (Bam). Here, we report the native structure and mechanism of a core component of this complex, BamE, and show that it is exclusively monomeric in its native environment of the periplasm, but is able to adopt a distinct dimeric conformation in the cytoplasm. BamE is shown to bind specifically to phosphatidylglycerol, and comprehensive mutagenesis and interaction studies have mapped key determinants for complex binding, outer membrane integrity and cell viability, as well as revealing the role of BamE within the Bam complex.

KW - Bam complex

KW - BamE

KW - Omp85

KW - SmpA

KW - outer membrane biogenesis

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U2 - 10.1038/embor.2010.202

DO - 10.1038/embor.2010.202

M3 - Article

SN - 1469-221X

VL - 12

SP - 123

EP - 128

JO - EMBO Reports

JF - EMBO Reports

IS - 2

ER -

Structure and function of BamE within the outer membrane and the β-barrel assembly machine

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