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dc.contributor.authorWeikum, Julia
dc.contributor.authorvan Dyck, Jeroen F.
dc.contributor.authorSubramani, Saranya
dc.contributor.authorKlebl, David P.
dc.contributor.authorStorflor, Merete
dc.contributor.authorMuench, Stephen P.
dc.contributor.authorAbel, Sören
dc.contributor.authorSobott, Frank
dc.contributor.authorMorth, Jens Preben
dc.date.accessioned2024-02-16T11:25:29Z
dc.date.available2024-02-16T11:25:29Z
dc.date.issued2023-10-23
dc.description.abstractThe bacterial magnesium transporter A (MgtA) is a specialized P-type ATPase important for Mg<sup>2+</sup> import into the cytoplasm; disrupted magnesium homeostasis is linked to intrinsic ribosome instability and antibacterial resistance in Salmonella strains. Here, we show that MgtA has functional specificity for cardiolipin 18:1. Still, it reaches maximum activity only in combination with cardiolipin 16:0, equivalent to the major components of native cardiolipin found in E. coli membranes. Native mass spectrometry indicates the presence of two binding sites for cardiolipin, agreeing with the kinetic studies revealing that a cooperative relationship likely exists between the two cardiolipin variants. This is the first experimental evidence of cooperative effects between lipids of the same class, with only minor variations in their acyl chain composition, acting on a membrane protein. In summary, our results reveal that MgtA exhibits a highly complex interaction with one cardiolipin 18:1 and one cardiolipin 16:0, affecting protein activity and stability, contributing to our understanding of the particular interactions between lipid environment and membrane proteins. Further, a better understanding of Mg<sup>2+</sup> homeostasis in bacteria, due to its role as a virulence regulator, will provide further insights into the regulation and mechanism of bacterial infections.en_US
dc.identifier.citationWeikum, van Dyck, Subramani, Klebl, Storflor, Muench, Abel, Sobott, Morth. The bacterial magnesium transporter MgtA reveals highly selective interaction with specific cardiolipin species. BBA - Molecular Cell Research. 2023;1871(1)en_US
dc.identifier.cristinIDFRIDAID 2234267
dc.identifier.doi10.1016/j.bbamcr.2023.119614
dc.identifier.issn0167-4889
dc.identifier.issn1879-2596
dc.identifier.urihttps://hdl.handle.net/10037/32948
dc.language.isoengen_US
dc.publisherElsevieren_US
dc.relation.journalBBA - Molecular Cell Research
dc.rights.accessRightsopenAccessen_US
dc.rights.holderCopyright 2023 The Author(s)en_US
dc.rights.urihttps://creativecommons.org/licenses/by/4.0en_US
dc.rightsAttribution 4.0 International (CC BY 4.0)en_US
dc.titleThe bacterial magnesium transporter MgtA reveals highly selective interaction with specific cardiolipin speciesen_US
dc.type.versionpublishedVersionen_US
dc.typeJournal articleen_US
dc.typeTidsskriftartikkelen_US
dc.typePeer revieweden_US


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Attribution 4.0 International (CC BY 4.0)
Med mindre det står noe annet, er denne innførselens lisens beskrevet som Attribution 4.0 International (CC BY 4.0)