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

Abstract

Insertion of folded proteins into the outer membrane of Gram-negative bacteria is mediated by the essential β-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

Keywords

Bacterial Outer Membrane Proteins/chemistry
Binding Sites
Escherichia coli Proteins/chemistry
Magnetic Resonance Spectroscopy
Mutagenesis, Site-Directed
Mutant Proteins/chemistry
Periplasmic Proteins/chemistry
Phosphatidylglycerols/chemistry
Protein Binding
Protein Conformation
Recombinant Proteins/chemistry

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10.1038/embor.2010.202

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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 β-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 = "Bacterial Outer Membrane Proteins/chemistry, Binding Sites, Escherichia coli Proteins/chemistry, Magnetic Resonance Spectroscopy, Mutagenesis, Site-Directed, Mutant Proteins/chemistry, Periplasmic Proteins/chemistry, Phosphatidylglycerols/chemistry, Protein Binding, Protein Conformation, Recombinant Proteins/chemistry",

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",

year = "2011",

month = feb,

doi = "10.1038/embor.2010.202",

language = "English",

volume = "12",

pages = "123--128",

journal = "Embo Reports",

issn = "1469-221X",

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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

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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

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AB - Insertion of folded proteins into the outer membrane of Gram-negative bacteria is mediated by the essential β-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 - Bacterial Outer Membrane Proteins/chemistry

KW - Binding Sites

KW - Escherichia coli Proteins/chemistry

KW - Magnetic Resonance Spectroscopy

KW - Mutagenesis, Site-Directed

KW - Mutant Proteins/chemistry

KW - Periplasmic Proteins/chemistry

KW - Phosphatidylglycerols/chemistry

KW - Protein Binding

KW - Protein Conformation

KW - Recombinant Proteins/chemistry

UR - https://www.embopress.org/doi/full/10.1038/embor.2010.202

U2 - 10.1038/embor.2010.202

DO - 10.1038/embor.2010.202

M3 - Article

C2 - 21212804

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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