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Combining native and 'omics' mass spectrometry to identify endogenous ligands bound to membrane proteins.

ABSTRACT: Ligands bound to protein assemblies provide critical information for function, yet are often difficult to capture and define. Here we develop a top-down method, 'nativeomics', unifying 'omics' (lipidomics, proteomics, metabolomics) analysis with native mass spectrometry to identify ligands bound to membrane protein assemblies. By maintaining the link between proteins and ligands, we define the lipidome/metabolome in contact with membrane porins and a mitochondrial translocator to discover potential regulators of protein function.

SUBMITTER: Gault J

PROVIDER: S-EPMC7332344 | biostudies-literature | 2020 May

REPOSITORIES: biostudies-literature

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Combining native and 'omics' mass spectrometry to identify endogenous ligands bound to membrane proteins.

Gault Joseph J Liko Idlir I Landreh Michael M Shutin Denis D Bolla Jani Reddy JR Jefferies Damien D Agasid Mark M Yen Hsin-Yung HY Ladds Marcus J G W MJGW Lane David P DP Khalid Syma S Mullen Christopher C Remes Philip M PM Huguet Romain R McAlister Graeme G Goodwin Michael M Viner Rosa R Syka John E P JEP Robinson Carol V CV

Nature methods 20200504 5

Ligands bound to protein assemblies provide critical information for function, yet are often difficult to capture and define. Here we develop a top-down method, 'nativeomics', unifying 'omics' (lipidomics, proteomics, metabolomics) analysis with native mass spectrometry to identify ligands bound to membrane protein assemblies. By maintaining the link between proteins and ligands, we define the lipidome/metabolome in contact with membrane porins and a mitochondrial translocator to discover potent ...[more]

PMID: 32371966

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