Proteomics

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WDR76-SPIN1_SCAP-E2-XL_mzTab and mgf

ABSTRACT: SCAP-XL of Halo-WDR76 and SNAP-SPIN1 from stable cell line in WDR76 KO background. Serial Capture Affinity Purification (SCAP) was performed on whole cell extract of a stable cell line of 293FRT cells in WDR76 KO background. DSSO crosslinked in E2 sample. Data was acquired using a ms1/ms2/ms3 method. Data was searched using Proteomics Discoverer 2.4 with XlinkX.

INSTRUMENT(S): Orbitrap Fusion Lumos

ORGANISM(S): Homo Sapiens (ncbitaxon:9606)

SUBMITTER: Michael P. Washburn  

PROVIDER: MSV000086749 | MassIVE | Fri Jan 22 11:48:00 GMT 2021

REPOSITORIES: MassIVE

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An integrated structural model of the DNA damage-responsive H3K4me3 binding WDR76:SPIN1 complex with the nucleosome.

Liu Xingyu X   Zhang Ying Y   Wen Zhihui Z   Hao Yan Y   Banks Charles A S CAS   Cesare Joseph J   Bhattacharya Saikat S   Arvindekar Shreyas S   Lange Jeffrey J JJ   Xie Yixuan Y   Garcia Benjamin A BA   Slaughter Brian D BD   Unruh Jay R JR   Viswanath Shruthi S   Florens Laurence L   Workman Jerry L JL   Washburn Michael P MP  

Proceedings of the National Academy of Sciences of the United States of America 20240808 33

Serial capture affinity purification (SCAP) is a powerful method to isolate a specific protein complex. When combined with cross-linking mass spectrometry and computational approaches, one can build an integrated structural model of the isolated complex. Here, we applied SCAP to dissect a subpopulation of WDR76 in complex with SPIN1, a histone reader that recognizes trimethylated histone H3 lysine4 (H3K4me3). In contrast to a previous SCAP analysis of the SPIN1:SPINDOC complex, histones and the  ...[more]

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