Proteomics

Dataset Information

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Identification of the SS18-SSX interacting proteins


ABSTRACT: Using affinity purification determine changes in SS18 BAF complex upon fusion to SSX1. Using soluble nuclear fraction (nuclear extract NE) and nuclease digested chromatin fraction (CHR) we performed affinity capture of proteins bound to wild type SS18 and synovial sarcoma SS18-SSX1 fusion from NE and CHR of 293T cells.

INSTRUMENT(S): LTQ Orbitrap Elite

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Hek-293t Cell

SUBMITTER: Andrew D'Avino  

LAB HEAD: Cigall Kadoch

PROVIDER: PXD018715 | Pride | 2020-08-09

REPOSITORIES: Pride

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Publications


Interactions between chromatin-associated proteins and the histone landscape play major roles in dictating genome topology and gene expression. Cancer-specific fusion oncoproteins, which display unique chromatin localization patterns, often lack classical DNA-binding domains, presenting challenges in identifying mechanisms governing their site-specific chromatin targeting and function. Here we identify a minimal region of the human SS18-SSX fusion oncoprotein (the hallmark driver of synovial sar  ...[more]

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