In vivo crosslinking and effective 2D enrichment for proteome wide interactome studies

Abstract Cross-linking mass spectrometry has evolved as a powerful technique to study protein-protein interactions and to provide structural information. Low reaction efficiencies, and complex matrices lead to challenging system wide crosslink analysis. We improved and streamlined an Azide-A-DSBSO b...

Full description

Saved in:
Bibliographic Details
Main Authors: Philipp Bräuer, Laszlo Tirian, Fränze Müller, Karl Mechtler, Manuel Matzinger
Format: Article
Language:English
Published: Nature Portfolio 2025-08-01
Series:Communications Chemistry
Online Access:https://doi.org/10.1038/s42004-025-01644-6
Tags: Add Tag
No Tags, Be the first to tag this record!
_version_ 1849333209460899840
author Philipp Bräuer
Laszlo Tirian
Fränze Müller
Karl Mechtler
Manuel Matzinger
author_facet Philipp Bräuer
Laszlo Tirian
Fränze Müller
Karl Mechtler
Manuel Matzinger
author_sort Philipp Bräuer
collection DOAJ
description Abstract Cross-linking mass spectrometry has evolved as a powerful technique to study protein-protein interactions and to provide structural information. Low reaction efficiencies, and complex matrices lead to challenging system wide crosslink analysis. We improved and streamlined an Azide-A-DSBSO based in vivo crosslinking workflow employing two orthogonal effective enrichment steps: Affinity enrichment and size exclusion chromatography (SEC). Combined, they allow an effective enrichment of DSBSO containing peptides and remove the background of linear as well as mono-linked peptides. We found that the analysis of a single SEC fraction is effective to yield ~90% of all crosslinks, which is important whenever measurement time is limited, and sample throughput is crucial. Our workflow resulted in more than 5000 crosslinks from K562 cells and generated a comprehensive PPI network. From 393 PPI found within the nucleus, 56 are novel. We further show, that by applying DSBSO to nuclear extracts we yield more crosslinks on lower abundant proteins and showcase this on the DEAD-box RNA helicase DDX39B which is predominantly expressed in the nucleus. Our data indicates that DDX39B might be present in monomeric and dimeric forms together with DDX39A within the nuclear extracts analyzed.
format Article
id doaj-art-5d4fada6989340169ba173018a1e4b43
institution Kabale University
issn 2399-3669
language English
publishDate 2025-08-01
publisher Nature Portfolio
record_format Article
series Communications Chemistry
spelling doaj-art-5d4fada6989340169ba173018a1e4b432025-08-20T03:45:56ZengNature PortfolioCommunications Chemistry2399-36692025-08-018111310.1038/s42004-025-01644-6In vivo crosslinking and effective 2D enrichment for proteome wide interactome studiesPhilipp Bräuer0Laszlo Tirian1Fränze Müller2Karl Mechtler3Manuel Matzinger4Research Institute of Molecular Pathology (IMP), Vienna BioCenter (VBC)Institute of Molecular Biotechnology (IMBA), Austrian Academy of Sciences, Vienna BioCenter (VBC)Research Institute of Molecular Pathology (IMP), Vienna BioCenter (VBC)Research Institute of Molecular Pathology (IMP), Vienna BioCenter (VBC)Research Institute of Molecular Pathology (IMP), Vienna BioCenter (VBC)Abstract Cross-linking mass spectrometry has evolved as a powerful technique to study protein-protein interactions and to provide structural information. Low reaction efficiencies, and complex matrices lead to challenging system wide crosslink analysis. We improved and streamlined an Azide-A-DSBSO based in vivo crosslinking workflow employing two orthogonal effective enrichment steps: Affinity enrichment and size exclusion chromatography (SEC). Combined, they allow an effective enrichment of DSBSO containing peptides and remove the background of linear as well as mono-linked peptides. We found that the analysis of a single SEC fraction is effective to yield ~90% of all crosslinks, which is important whenever measurement time is limited, and sample throughput is crucial. Our workflow resulted in more than 5000 crosslinks from K562 cells and generated a comprehensive PPI network. From 393 PPI found within the nucleus, 56 are novel. We further show, that by applying DSBSO to nuclear extracts we yield more crosslinks on lower abundant proteins and showcase this on the DEAD-box RNA helicase DDX39B which is predominantly expressed in the nucleus. Our data indicates that DDX39B might be present in monomeric and dimeric forms together with DDX39A within the nuclear extracts analyzed.https://doi.org/10.1038/s42004-025-01644-6
spellingShingle Philipp Bräuer
Laszlo Tirian
Fränze Müller
Karl Mechtler
Manuel Matzinger
In vivo crosslinking and effective 2D enrichment for proteome wide interactome studies
Communications Chemistry
title In vivo crosslinking and effective 2D enrichment for proteome wide interactome studies
title_full In vivo crosslinking and effective 2D enrichment for proteome wide interactome studies
title_fullStr In vivo crosslinking and effective 2D enrichment for proteome wide interactome studies
title_full_unstemmed In vivo crosslinking and effective 2D enrichment for proteome wide interactome studies
title_short In vivo crosslinking and effective 2D enrichment for proteome wide interactome studies
title_sort in vivo crosslinking and effective 2d enrichment for proteome wide interactome studies
url https://doi.org/10.1038/s42004-025-01644-6
work_keys_str_mv AT philippbrauer invivocrosslinkingandeffective2denrichmentforproteomewideinteractomestudies
AT laszlotirian invivocrosslinkingandeffective2denrichmentforproteomewideinteractomestudies
AT franzemuller invivocrosslinkingandeffective2denrichmentforproteomewideinteractomestudies
AT karlmechtler invivocrosslinkingandeffective2denrichmentforproteomewideinteractomestudies
AT manuelmatzinger invivocrosslinkingandeffective2denrichmentforproteomewideinteractomestudies