dc.contributor.author | Weikum, Julia | |
dc.contributor.author | van Dyck, Jeroen F. | |
dc.contributor.author | Subramani, Saranya | |
dc.contributor.author | Klebl, David P. | |
dc.contributor.author | Storflor, Merete | |
dc.contributor.author | Muench, Stephen P. | |
dc.contributor.author | Abel, Sören | |
dc.contributor.author | Sobott, Frank | |
dc.contributor.author | Morth, Jens Preben | |
dc.date.accessioned | 2024-02-16T11:25:29Z | |
dc.date.available | 2024-02-16T11:25:29Z | |
dc.date.issued | 2023-10-23 | |
dc.description.abstract | The 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.citation | Weikum, 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.cristinID | FRIDAID 2234267 | |
dc.identifier.doi | 10.1016/j.bbamcr.2023.119614 | |
dc.identifier.issn | 0167-4889 | |
dc.identifier.issn | 1879-2596 | |
dc.identifier.uri | https://hdl.handle.net/10037/32948 | |
dc.language.iso | eng | en_US |
dc.publisher | Elsevier | en_US |
dc.relation.journal | BBA - Molecular Cell Research | |
dc.rights.accessRights | openAccess | en_US |
dc.rights.holder | Copyright 2023 The Author(s) | en_US |
dc.rights.uri | https://creativecommons.org/licenses/by/4.0 | en_US |
dc.rights | Attribution 4.0 International (CC BY 4.0) | en_US |
dc.title | The bacterial magnesium transporter MgtA reveals highly selective interaction with specific cardiolipin species | en_US |
dc.type.version | publishedVersion | en_US |
dc.type | Journal article | en_US |
dc.type | Tidsskriftartikkel | en_US |
dc.type | Peer reviewed | en_US |