Please use this identifier to cite or link to this item: https://doi.org/10.7554/eLife.19042
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dc.titleDefining key roles for auxiliary proteins in an ABC transporter that maintains bacterial outer membrane lipid asymmetry
dc.contributor.authorThong, Shuhua
dc.contributor.authorErcan, Bilge
dc.contributor.authorTorte, Federico
dc.contributor.authorFong, Zhen Yang
dc.contributor.authorWong, Hui Yi Alvina
dc.contributor.authorWenk, Markus R
dc.contributor.authorChng, Shu-Sin
dc.date.accessioned2020-06-22T03:35:45Z
dc.date.available2020-06-22T03:35:45Z
dc.date.issued2016
dc.identifier.citationThong, Shuhua, Ercan, Bilge, Torte, Federico, Fong, Zhen Yang, Wong, Hui Yi Alvina, Wenk, Markus R, Chng, Shu-Sin (2016). Defining key roles for auxiliary proteins in an ABC transporter that maintains bacterial outer membrane lipid asymmetry. ELIFE 5 (AUGUST). ScholarBank@NUS Repository. https://doi.org/10.7554/eLife.19042
dc.identifier.issn2050084X
dc.identifier.issn2050084X
dc.identifier.urihttps://scholarbank.nus.edu.sg/handle/10635/170492
dc.description.abstract© Thong et al. 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.
dc.language.isoen
dc.publisherELIFE SCIENCES PUBLICATIONS LTD
dc.sourceElements
dc.subjectScience & Technology
dc.subjectLife Sciences & Biomedicine
dc.subjectBiology
dc.subjectLife Sciences & Biomedicine - Other Topics
dc.subjectESCHERICHIA-COLI
dc.subjectSALMONELLA-TYPHIMURIUM
dc.subjectSULFATE TRANSPORTER
dc.subjectBINDING PROTEIN
dc.subjectSTAS DOMAIN
dc.subjectLIPOPOLYSACCHARIDE
dc.subjectCOMPLEX
dc.subjectBIOGENESIS
dc.subjectPHOSPHOLIPIDS
dc.subjectMECHANISMS
dc.typeArticle
dc.date.updated2020-06-17T04:38:11Z
dc.contributor.departmentBIOMED INST FOR GLOBAL HEALTH RES & TECH
dc.contributor.departmentDEPT OF BIOCHEMISTRY
dc.contributor.departmentDEPT OF CHEMISTRY
dc.description.doi10.7554/eLife.19042
dc.description.sourcetitleELIFE
dc.description.volume5
dc.description.issueAUGUST
dc.published.statePublished
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