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Identifying and characterising Thrap3, Bclaf1 and Erh direct interactions using cross-linking mass spectrometry

ABSTRACT: Cross-linking mass spectrometry (XL-MS) is a powerful technology capable of yielding structural insights across the complex cellular protein interaction network. We performed XL-MS using MS-cleavable cross-linker disuccinimidyl sulfoxide (DSSO) on endogenous affinity-purified BAF complex. We identified numerous crosslinks between three BAF co-purifying proteins, namely Thrap3, Bclaf1 and Erh. Our data suggests that Bclaf1, Erh and Thrap3 interact closely and might represent a stable complex. The XL data allowed us to map interaction surfaces on Thrap3 and B, which overlap with the non-disordered portions of both proteins.

INSTRUMENT(S): Orbitrap Fusion Lumos

ORGANISM(S): Mus Musculus (mouse)

TISSUE(S): Cell Culture

SUBMITTER: James Wright

LAB HEAD: Jyoti Choudhary

PROVIDER: PXD027611 | Pride | 2021-09-24

REPOSITORIES: Pride

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			Action	DRS
	20200321_LS15.raw	Raw
	20200321_LS16.raw	Raw
	20200810_LS19_LMS03_F01.raw	Raw
	20200810_LS19_LMS03_F02.raw	Raw
	20200810_LS19_LMS03_F03.raw	Raw

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