Journal
FEBS JOURNAL
Volume 287, Issue 12, Pages 2428-2439Publisher
WILEY
DOI: 10.1111/febs.15281
Keywords
Isc operon; FeS cluster; native mass spectrometry; proteins; structural biology
Categories
Funding
- INSTRUCT
- UK Dementia Research Institute - Medical Research Council [RE1 3556]
- Alzheimer UK
- Alzheimer Foundation
- FRISBI [ANR-10-INBS-05-02]
- GRAL, a project of the University Grenoble Alpes graduate school (Ecoles Universitaires de Recherche) CBH-EUR-GS [ANR-17-EURE-0003]
- EMBO
- Grenoble Instruct-ERIC Center (ISBG) [UMS 3518 CNRS-CEA-UGA-EMBL]
- BBSRC [BB/S001832/1] Funding Source: UKRI
- MRC [UKDRI-6002] Funding Source: UKRI
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Native mass spectrometry is an emerging technique in biology that gives the possibility to study noncovalently bound complexes with high sensitivity and accuracy. It thus allows the characterization of macromolecular assemblies, assessing their mass and stoichiometries and mapping the interacting surfaces. In this review, we discuss the application of native mass spectrometry to dynamic molecular machines based on multiple weak interactions. In the study of these machines, it is crucial to understand which and under which conditions various complexes form at any time point. We focus on the specific example of the iron-sulfur cluster biogenesis machine because this is an archetype of a dynamic machine that requires very specific and demanding experimental conditions, such as anaerobicity and the need of retaining the fold of marginally folded proteins. We describe the advantages, challenges and current limitations of the technique by providing examples from our own experience and suggesting possible future solutions.
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