Substrate-dependent arrangements of the subunits of the BAM complex determined by neutron reflectometry

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dc.contributor.authorChen, Xen_AU
dc.contributor.authorDing, Yen_AU
dc.contributor.authorBamert, RSen_AU
dc.contributor.authorLe Brun, APen_AU
dc.contributor.authorDuff, APen_AU
dc.contributor.authorWu, CMen_AU
dc.contributor.authorHsu, HYen_AU
dc.contributor.authorShiota, Ten_AU
dc.contributor.authorLithgow, Ten_AU
dc.contributor.authorShen, HHen_AU
dc.date.accessioned2024-12-19T21:12:58Zen_AU
dc.date.available2024-12-19T21:12:58Zen_AU
dc.date.issued2021-09-01en_AU
dc.date.statistics2024-11-28en_AU
dc.description.abstractIn Gram-negative bacteria, the β-barrel assembly machinery (BAM) complex catalyses the assembly of β-barrel proteins into the outer membrane, and is composed of five subunits: BamA, BamB, BamC, BamD and BamE. Once assembled, - β-barrel proteins can be involved in various functions including uptake of nutrients, export of toxins and mediating host-pathogen interactions, but the precise mechanism by which these ubiquitous and often essential β-barrel proteins are assembled is yet to be established. In order to determine the relative positions of BAM subunits in the membrane environment we reconstituted each subunit into a biomimetic membrane, characterizing their interaction and structural changes by Quartz Crystal Microbalance with Dissipation monitoring (QCM-D) and neutron reflectometry. Our results suggested that the binding of BamE, or a BamDE dimer, to BamA induced conformational changes in the polypeptide transported-associated (POTRA) domains of BamA, but that BamB or BamD alone did not promote any such changes. As monitored by neutron reflectometry, addition of an unfolded substrate protein extended the length of POTRA domains further away from the membrane interface as part of the mechanism whereby the substrate protein was folded into the membrane. © 2021 Published by Elsevier B.V.en_AU
dc.description.sponsorshipWe acknowledge the use of the Australian Nuclear Science and Technology Organisation for the allocation of neutron beam time (P4786). H.H.S. acknowledges Prof. Susan Buchanan and Prof. Nicholas Noinaj for the gift of the plasmid pHIS-BamB, pHIS-BamC, pHIS-BamD, and pHIS-BamE. H.H.S. is an Australian NHMRC Career Development Research Fellow (GNT1106798). T.S. is supported by the Japan Society for the Promotion of Science (JSPS) Grants-in-Aid for Scientific Research (KAKENHI) (19K16077 and 18KK0197), Institute for Fermentation Osaka, The Shinnihon Foundation of Advanced Medical Treatment Research, and The Sasakawa Scientific Research Grant, Japan.en_AU
dc.format.mediumPrint-Electronicen_AU
dc.identifier.articlenumber183587en_AU
dc.identifier.citationChen, X., Ding, Y., Bamert, R. S., Le Brun, A. P., Duff, A. P., Wu, C.-M., Hsu, H.-Y., Shiota, T., Lithgow, T., & Shen, H.-H. (2021). Substrate-dependent arrangements of the subunits of the BAM complex determined by neutron reflectometry. Biochimica et Biophysica Acta (BBA) - Biomembranes, 1863(9), 183587. doi:10.1016/j.bbamem.2021.183587en_AU
dc.identifier.issn0005-2736en_AU
dc.identifier.issn1879-2642en_AU
dc.identifier.issue9en_AU
dc.identifier.journaltitleBiochimica et Biophysica Acta (BBA) - Biomembranesen_AU
dc.identifier.urihttps://doi.org/10.1016/j.bbamem.2021.183587en_AU
dc.identifier.urihttps://apo.ansto.gov.au/handle/10238/15839en_AU
dc.identifier.volume1863en_AU
dc.languageEnglishen_AU
dc.language.isoenen_AU
dc.publisherElsevieren_AU
dc.subjectSubstratesen_AU
dc.subjectNeutron reflectorsen_AU
dc.subjectBacteriaen_AU
dc.subjectCell membranesen_AU
dc.subjectToxinsen_AU
dc.subjectPathogensen_AU
dc.subjectInteractionsen_AU
dc.subjectBiomimeticsen_AU
dc.subjectPolypeptidesen_AU
dc.subjectQuartzen_AU
dc.subjectCrystalsen_AU
dc.subjectMicrobalancesen_AU
dc.titleSubstrate-dependent arrangements of the subunits of the BAM complex determined by neutron reflectometryen_AU
dc.typeJournal Articleen_AU
dcterms.dateAccepted2021-02-17en_AU
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