Proteomics

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Cross-linking mass spectrometry of yeast mitochondria grown on different carbon sources reveal Ndi1, Min8 and Pet9 associated with the electron transport chain

ABSTRACT: Mitochondria derived from Saccharomyces cerevisiae grown on either a non-fermentable (glycerol) or a fermentable (glucose) carbon source were cross-linked with BS3. Additionally, by using a stable-isotope labelled quantitative cross-linking approach, we were able to quantify differences in protein-protein cross-links in mitochondria according to the growth condition. Furthermore, so far uncharacterized yeast proteins were put into biological context based on their cross-linking pattern.

INSTRUMENT(S): Orbitrap Fusion Lumos, Orbitrap Fusion, Q Exactive HF

ORGANISM(S): Saccharomyces Cerevisiae (baker's Yeast)

SUBMITTER: Andreas Linden  

LAB HEAD: Henning Urlaub

PROVIDER: PXD017620 | Pride | 2020-04-27

REPOSITORIES: Pride

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Publications

A Cross-linking Mass Spectrometry Approach Defines Protein Interactions in Yeast Mitochondria.

Linden Andreas A   Deckers Markus M   Parfentev Iwan I   Pflanz Ralf R   Homberg Bettina B   Neumann Piotr P   Ficner Ralf R   Rehling Peter P   Urlaub Henning H  

Molecular & cellular proteomics : MCP 20200424 7

Protein cross-linking and the analysis of cross-linked peptides by mass spectrometry is currently receiving much attention. Not only is this approach applied to isolated complexes to provide information about spatial arrangements of proteins, but it is also increasingly applied to entire cells and their organelles. As in quantitative proteomics, the application of isotopic labeling further makes it possible to monitor quantitative changes in the protein-protein interactions between different sta  ...[more]

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