Defining key roles for auxiliary proteins in an ABC transporter that maintains bacterial outer membrane lipid asymmetry

In Gram-negative bacteria, lipid asymmetry is critical for the function of the outer membrane (OM) as a selective permeability barrier, but how it is established and maintained is poorly understood. Here, we characterize a non-canonical ATP-binding cassette (ABC) transporter in Escherichia coli that...
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Autor*in:	Shuhua Thong [verfasserIn] Bilge Ercan [verfasserIn] Federico Torta [verfasserIn] Zhen Yang Fong [verfasserIn] Hui Yi Alvina Wong [verfasserIn] Markus R Wenk [verfasserIn] Shu-Sin Chng [verfasserIn]

Format:	E-Artikel
Sprache:	Englisch

Erschienen:	2016

Schlagwörter:	phospholipid binding intermembrane lipid transport protein complex assembly mammalian cell entry (MCE) domain sulfate transport and anti-sigma factor antagonist (STAS) domain

Übergeordnetes Werk:	In: eLife - eLife Sciences Publications Ltd, 2013, 5(2016)
Übergeordnetes Werk:	volume:5 ; year:2016

Links:	Link aufrufen Link aufrufen Link aufrufen Journal toc

DOI / URN:	10.7554/eLife.19042

Katalog-ID:	DOAJ084227435

Internformat


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520			\|a In Gram-negative bacteria, lipid asymmetry is critical for the function of the outer membrane (OM) as a selective permeability barrier, but how it is established and maintained is poorly understood. Here, we characterize a non-canonical ATP-binding cassette (ABC) transporter in Escherichia coli that provides energy for maintaining OM lipid asymmetry via the transport of aberrantly localized phospholipids (PLs) from the OM to the inner membrane (IM). We establish that the transporter comprises canonical components, MlaF and MlaE, and auxiliary proteins, MlaD and MlaB, of previously unknown functions. We further demonstrate that MlaD forms extremely stable hexamers within the complex, functions in substrate binding with strong affinity for PLs, and modulates ATP hydrolytic activity. In addition, MlaB plays critical roles in both the assembly and activity of the transporter. Our work provides mechanistic insights into how the MlaFEDB complex participates in ensuring active retrograde PL transport to maintain OM lipid asymmetry.
650		4	\|a phospholipid binding
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allfields	10.7554/eLife.19042 doi (DE-627)DOAJ084227435 (DE-599)DOAJ87d1edefc7ac45a7a79c7381ce7c05fa DE-627 ger DE-627 rakwb eng QH301-705.5 Shuhua Thong verfasserin aut Defining key roles for auxiliary proteins in an ABC transporter that maintains bacterial outer membrane lipid asymmetry 2016 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier In Gram-negative bacteria, lipid asymmetry is critical for the function of the outer membrane (OM) as a selective permeability barrier, but how it is established and maintained is poorly understood. Here, we characterize a non-canonical ATP-binding cassette (ABC) transporter in Escherichia coli that provides energy for maintaining OM lipid asymmetry via the transport of aberrantly localized phospholipids (PLs) from the OM to the inner membrane (IM). We establish that the transporter comprises canonical components, MlaF and MlaE, and auxiliary proteins, MlaD and MlaB, of previously unknown functions. We further demonstrate that MlaD forms extremely stable hexamers within the complex, functions in substrate binding with strong affinity for PLs, and modulates ATP hydrolytic activity. In addition, MlaB plays critical roles in both the assembly and activity of the transporter. Our work provides mechanistic insights into how the MlaFEDB complex participates in ensuring active retrograde PL transport to maintain OM lipid asymmetry. phospholipid binding intermembrane lipid transport protein complex assembly mammalian cell entry (MCE) domain sulfate transport and anti-sigma factor antagonist (STAS) domain Medicine R Science Q Biology (General) Bilge Ercan verfasserin aut Federico Torta verfasserin aut Zhen Yang Fong verfasserin aut Hui Yi Alvina Wong verfasserin aut Markus R Wenk verfasserin aut Shu-Sin Chng verfasserin aut In eLife eLife Sciences Publications Ltd, 2013 5(2016) (DE-627)728518384 (DE-600)2687154-3 2050084X nnns volume:5 year:2016 https://doi.org/10.7554/eLife.19042 kostenfrei https://doaj.org/article/87d1edefc7ac45a7a79c7381ce7c05fa kostenfrei https://elifesciences.org/articles/19042 kostenfrei https://doaj.org/toc/2050-084X Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_171 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 GBV_ILN_602 GBV_ILN_2003 GBV_ILN_2014 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4335 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 5 2016
spelling	10.7554/eLife.19042 doi (DE-627)DOAJ084227435 (DE-599)DOAJ87d1edefc7ac45a7a79c7381ce7c05fa DE-627 ger DE-627 rakwb eng QH301-705.5 Shuhua Thong verfasserin aut Defining key roles for auxiliary proteins in an ABC transporter that maintains bacterial outer membrane lipid asymmetry 2016 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier In Gram-negative bacteria, lipid asymmetry is critical for the function of the outer membrane (OM) as a selective permeability barrier, but how it is established and maintained is poorly understood. Here, we characterize a non-canonical ATP-binding cassette (ABC) transporter in Escherichia coli that provides energy for maintaining OM lipid asymmetry via the transport of aberrantly localized phospholipids (PLs) from the OM to the inner membrane (IM). We establish that the transporter comprises canonical components, MlaF and MlaE, and auxiliary proteins, MlaD and MlaB, of previously unknown functions. We further demonstrate that MlaD forms extremely stable hexamers within the complex, functions in substrate binding with strong affinity for PLs, and modulates ATP hydrolytic activity. In addition, MlaB plays critical roles in both the assembly and activity of the transporter. Our work provides mechanistic insights into how the MlaFEDB complex participates in ensuring active retrograde PL transport to maintain OM lipid asymmetry. phospholipid binding intermembrane lipid transport protein complex assembly mammalian cell entry (MCE) domain sulfate transport and anti-sigma factor antagonist (STAS) domain Medicine R Science Q Biology (General) Bilge Ercan verfasserin aut Federico Torta verfasserin aut Zhen Yang Fong verfasserin aut Hui Yi Alvina Wong verfasserin aut Markus R Wenk verfasserin aut Shu-Sin Chng verfasserin aut In eLife eLife Sciences Publications Ltd, 2013 5(2016) (DE-627)728518384 (DE-600)2687154-3 2050084X nnns volume:5 year:2016 https://doi.org/10.7554/eLife.19042 kostenfrei https://doaj.org/article/87d1edefc7ac45a7a79c7381ce7c05fa kostenfrei https://elifesciences.org/articles/19042 kostenfrei https://doaj.org/toc/2050-084X Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_171 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 GBV_ILN_602 GBV_ILN_2003 GBV_ILN_2014 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4335 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 5 2016
allfields_unstemmed	10.7554/eLife.19042 doi (DE-627)DOAJ084227435 (DE-599)DOAJ87d1edefc7ac45a7a79c7381ce7c05fa DE-627 ger DE-627 rakwb eng QH301-705.5 Shuhua Thong verfasserin aut Defining key roles for auxiliary proteins in an ABC transporter that maintains bacterial outer membrane lipid asymmetry 2016 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier In Gram-negative bacteria, lipid asymmetry is critical for the function of the outer membrane (OM) as a selective permeability barrier, but how it is established and maintained is poorly understood. Here, we characterize a non-canonical ATP-binding cassette (ABC) transporter in Escherichia coli that provides energy for maintaining OM lipid asymmetry via the transport of aberrantly localized phospholipids (PLs) from the OM to the inner membrane (IM). We establish that the transporter comprises canonical components, MlaF and MlaE, and auxiliary proteins, MlaD and MlaB, of previously unknown functions. We further demonstrate that MlaD forms extremely stable hexamers within the complex, functions in substrate binding with strong affinity for PLs, and modulates ATP hydrolytic activity. In addition, MlaB plays critical roles in both the assembly and activity of the transporter. Our work provides mechanistic insights into how the MlaFEDB complex participates in ensuring active retrograde PL transport to maintain OM lipid asymmetry. phospholipid binding intermembrane lipid transport protein complex assembly mammalian cell entry (MCE) domain sulfate transport and anti-sigma factor antagonist (STAS) domain Medicine R Science Q Biology (General) Bilge Ercan verfasserin aut Federico Torta verfasserin aut Zhen Yang Fong verfasserin aut Hui Yi Alvina Wong verfasserin aut Markus R Wenk verfasserin aut Shu-Sin Chng verfasserin aut In eLife eLife Sciences Publications Ltd, 2013 5(2016) (DE-627)728518384 (DE-600)2687154-3 2050084X nnns volume:5 year:2016 https://doi.org/10.7554/eLife.19042 kostenfrei https://doaj.org/article/87d1edefc7ac45a7a79c7381ce7c05fa kostenfrei https://elifesciences.org/articles/19042 kostenfrei https://doaj.org/toc/2050-084X Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_171 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 GBV_ILN_602 GBV_ILN_2003 GBV_ILN_2014 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4335 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 5 2016
allfieldsGer	10.7554/eLife.19042 doi (DE-627)DOAJ084227435 (DE-599)DOAJ87d1edefc7ac45a7a79c7381ce7c05fa DE-627 ger DE-627 rakwb eng QH301-705.5 Shuhua Thong verfasserin aut Defining key roles for auxiliary proteins in an ABC transporter that maintains bacterial outer membrane lipid asymmetry 2016 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier In Gram-negative bacteria, lipid asymmetry is critical for the function of the outer membrane (OM) as a selective permeability barrier, but how it is established and maintained is poorly understood. Here, we characterize a non-canonical ATP-binding cassette (ABC) transporter in Escherichia coli that provides energy for maintaining OM lipid asymmetry via the transport of aberrantly localized phospholipids (PLs) from the OM to the inner membrane (IM). We establish that the transporter comprises canonical components, MlaF and MlaE, and auxiliary proteins, MlaD and MlaB, of previously unknown functions. We further demonstrate that MlaD forms extremely stable hexamers within the complex, functions in substrate binding with strong affinity for PLs, and modulates ATP hydrolytic activity. In addition, MlaB plays critical roles in both the assembly and activity of the transporter. Our work provides mechanistic insights into how the MlaFEDB complex participates in ensuring active retrograde PL transport to maintain OM lipid asymmetry. phospholipid binding intermembrane lipid transport protein complex assembly mammalian cell entry (MCE) domain sulfate transport and anti-sigma factor antagonist (STAS) domain Medicine R Science Q Biology (General) Bilge Ercan verfasserin aut Federico Torta verfasserin aut Zhen Yang Fong verfasserin aut Hui Yi Alvina Wong verfasserin aut Markus R Wenk verfasserin aut Shu-Sin Chng verfasserin aut In eLife eLife Sciences Publications Ltd, 2013 5(2016) (DE-627)728518384 (DE-600)2687154-3 2050084X nnns volume:5 year:2016 https://doi.org/10.7554/eLife.19042 kostenfrei https://doaj.org/article/87d1edefc7ac45a7a79c7381ce7c05fa kostenfrei https://elifesciences.org/articles/19042 kostenfrei https://doaj.org/toc/2050-084X Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_171 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 GBV_ILN_602 GBV_ILN_2003 GBV_ILN_2014 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4335 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 5 2016
allfieldsSound	10.7554/eLife.19042 doi (DE-627)DOAJ084227435 (DE-599)DOAJ87d1edefc7ac45a7a79c7381ce7c05fa DE-627 ger DE-627 rakwb eng QH301-705.5 Shuhua Thong verfasserin aut Defining key roles for auxiliary proteins in an ABC transporter that maintains bacterial outer membrane lipid asymmetry 2016 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier In Gram-negative bacteria, lipid asymmetry is critical for the function of the outer membrane (OM) as a selective permeability barrier, but how it is established and maintained is poorly understood. Here, we characterize a non-canonical ATP-binding cassette (ABC) transporter in Escherichia coli that provides energy for maintaining OM lipid asymmetry via the transport of aberrantly localized phospholipids (PLs) from the OM to the inner membrane (IM). We establish that the transporter comprises canonical components, MlaF and MlaE, and auxiliary proteins, MlaD and MlaB, of previously unknown functions. We further demonstrate that MlaD forms extremely stable hexamers within the complex, functions in substrate binding with strong affinity for PLs, and modulates ATP hydrolytic activity. In addition, MlaB plays critical roles in both the assembly and activity of the transporter. Our work provides mechanistic insights into how the MlaFEDB complex participates in ensuring active retrograde PL transport to maintain OM lipid asymmetry. phospholipid binding intermembrane lipid transport protein complex assembly mammalian cell entry (MCE) domain sulfate transport and anti-sigma factor antagonist (STAS) domain Medicine R Science Q Biology (General) Bilge Ercan verfasserin aut Federico Torta verfasserin aut Zhen Yang Fong verfasserin aut Hui Yi Alvina Wong verfasserin aut Markus R Wenk verfasserin aut Shu-Sin Chng verfasserin aut In eLife eLife Sciences Publications Ltd, 2013 5(2016) (DE-627)728518384 (DE-600)2687154-3 2050084X nnns volume:5 year:2016 https://doi.org/10.7554/eLife.19042 kostenfrei https://doaj.org/article/87d1edefc7ac45a7a79c7381ce7c05fa kostenfrei https://elifesciences.org/articles/19042 kostenfrei https://doaj.org/toc/2050-084X Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_171 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 GBV_ILN_602 GBV_ILN_2003 GBV_ILN_2014 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4335 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 5 2016
language	English
source	In eLife 5(2016) volume:5 year:2016
sourceStr	In eLife 5(2016) volume:5 year:2016
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institution	findex.gbv.de
topic_facet	phospholipid binding intermembrane lipid transport protein complex assembly mammalian cell entry (MCE) domain sulfate transport and anti-sigma factor antagonist (STAS) domain Medicine R Science Q Biology (General)
isfreeaccess_bool	true
container_title	eLife
authorswithroles_txt_mv	Shuhua Thong @@aut@@ Bilge Ercan @@aut@@ Federico Torta @@aut@@ Zhen Yang Fong @@aut@@ Hui Yi Alvina Wong @@aut@@ Markus R Wenk @@aut@@ Shu-Sin Chng @@aut@@
publishDateDaySort_date	2016-01-01T00:00:00Z
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callnumber-first	Q - Science
author	Shuhua Thong
spellingShingle	Shuhua Thong misc QH301-705.5 misc phospholipid binding misc intermembrane lipid transport misc protein complex assembly misc mammalian cell entry (MCE) domain misc sulfate transport and anti-sigma factor antagonist (STAS) domain misc Medicine misc R misc Science misc Q misc Biology (General) Defining key roles for auxiliary proteins in an ABC transporter that maintains bacterial outer membrane lipid asymmetry
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topic_title	QH301-705.5 Defining key roles for auxiliary proteins in an ABC transporter that maintains bacterial outer membrane lipid asymmetry phospholipid binding intermembrane lipid transport protein complex assembly mammalian cell entry (MCE) domain sulfate transport and anti-sigma factor antagonist (STAS) domain
topic	misc QH301-705.5 misc phospholipid binding misc intermembrane lipid transport misc protein complex assembly misc mammalian cell entry (MCE) domain misc sulfate transport and anti-sigma factor antagonist (STAS) domain misc Medicine misc R misc Science misc Q misc Biology (General)
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title	Defining key roles for auxiliary proteins in an ABC transporter that maintains bacterial outer membrane lipid asymmetry
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title_full	Defining key roles for auxiliary proteins in an ABC transporter that maintains bacterial outer membrane lipid asymmetry
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title_sort	defining key roles for auxiliary proteins in an abc transporter that maintains bacterial outer membrane lipid asymmetry
callnumber	QH301-705.5
title_auth	Defining key roles for auxiliary proteins in an ABC transporter that maintains bacterial outer membrane lipid asymmetry
abstract	In Gram-negative bacteria, lipid asymmetry is critical for the function of the outer membrane (OM) as a selective permeability barrier, but how it is established and maintained is poorly understood. Here, we characterize a non-canonical ATP-binding cassette (ABC) transporter in Escherichia coli that provides energy for maintaining OM lipid asymmetry via the transport of aberrantly localized phospholipids (PLs) from the OM to the inner membrane (IM). We establish that the transporter comprises canonical components, MlaF and MlaE, and auxiliary proteins, MlaD and MlaB, of previously unknown functions. We further demonstrate that MlaD forms extremely stable hexamers within the complex, functions in substrate binding with strong affinity for PLs, and modulates ATP hydrolytic activity. In addition, MlaB plays critical roles in both the assembly and activity of the transporter. Our work provides mechanistic insights into how the MlaFEDB complex participates in ensuring active retrograde PL transport to maintain OM lipid asymmetry.
abstractGer	In Gram-negative bacteria, lipid asymmetry is critical for the function of the outer membrane (OM) as a selective permeability barrier, but how it is established and maintained is poorly understood. Here, we characterize a non-canonical ATP-binding cassette (ABC) transporter in Escherichia coli that provides energy for maintaining OM lipid asymmetry via the transport of aberrantly localized phospholipids (PLs) from the OM to the inner membrane (IM). We establish that the transporter comprises canonical components, MlaF and MlaE, and auxiliary proteins, MlaD and MlaB, of previously unknown functions. We further demonstrate that MlaD forms extremely stable hexamers within the complex, functions in substrate binding with strong affinity for PLs, and modulates ATP hydrolytic activity. In addition, MlaB plays critical roles in both the assembly and activity of the transporter. Our work provides mechanistic insights into how the MlaFEDB complex participates in ensuring active retrograde PL transport to maintain OM lipid asymmetry.
abstract_unstemmed	In Gram-negative bacteria, lipid asymmetry is critical for the function of the outer membrane (OM) as a selective permeability barrier, but how it is established and maintained is poorly understood. Here, we characterize a non-canonical ATP-binding cassette (ABC) transporter in Escherichia coli that provides energy for maintaining OM lipid asymmetry via the transport of aberrantly localized phospholipids (PLs) from the OM to the inner membrane (IM). We establish that the transporter comprises canonical components, MlaF and MlaE, and auxiliary proteins, MlaD and MlaB, of previously unknown functions. We further demonstrate that MlaD forms extremely stable hexamers within the complex, functions in substrate binding with strong affinity for PLs, and modulates ATP hydrolytic activity. In addition, MlaB plays critical roles in both the assembly and activity of the transporter. Our work provides mechanistic insights into how the MlaFEDB complex participates in ensuring active retrograde PL transport to maintain OM lipid asymmetry.
collection_details	GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_171 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 GBV_ILN_602 GBV_ILN_2003 GBV_ILN_2014 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4335 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700
title_short	Defining key roles for auxiliary proteins in an ABC transporter that maintains bacterial outer membrane lipid asymmetry
url	https://doi.org/10.7554/eLife.19042 https://doaj.org/article/87d1edefc7ac45a7a79c7381ce7c05fa https://elifesciences.org/articles/19042 https://doaj.org/toc/2050-084X
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author2	Bilge Ercan Federico Torta Zhen Yang Fong Hui Yi Alvina Wong Markus R Wenk Shu-Sin Chng
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up_date	2024-07-03T21:52:46.818Z
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Defining key roles for auxiliary proteins in an ABC transporter that maintains bacterial outer membrane lipid asymmetry

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