Proteomics

Dataset Information

0

Searching for new members of the SLX4 complex and for SLX4-complex members that are SUMOylated in vitro

ABSTRACT: The project was initially aimed at identifying new members of the SLX4 complex as well as members of the complex that are SUMOylated in vitro. The project was also aimed at assessing whether SUMOylation may change the compositon of the complex by reducing complex association of SUMOylated partners. YFP-SLX4 complexes were immunopurified from Hela Flp-In TRex cells producing full length YFP-SLX4 using a GFP nanobody. The YFP-SLX4 pull down was used in an ex vivo/in vitro SUMO-ligation assay as described in Guervilly et al. 2015. After the SUMO-ligation reaction, beads were washed 5 times with 50 mM Tris-HCl [pH 8.0] buffer, allowing for the removal of SUMOylated proteins that associate less efficiently with SLX4, or other members of the complex. SLX4 and proteins remaining associated with SLX4 after the successive washes were eluted directly in NuPAGE LDS sample buffer (Invitrogen) for 5 min at 95˚C.

INSTRUMENT(S): LTQ Orbitrap Velos

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Epithelial Cell

SUBMITTER: AUDEBERT Stephane  

LAB HEAD: Marseille proteomics ; CRCM ; Gaillard PH lab

PROVIDER: PXD012425 | Pride | 2020-03-05

REPOSITORIES: Pride

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Dataset's files

Source:
Action DRS
FIT0_ATP_Run1.msf Msf
FIT0_ATP_Run1.raw Raw
FIT0_ATP_Run2.msf Msf
FIT0_ATP_Run2.raw Raw
FIT0_noATP_Run1.msf Msf
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Publications

The SLX4 tumor suppressor is a scaffold that plays a pivotal role in several aspects of genome protection, including homologous recombination, interstrand DNA crosslink repair and the maintenance of common fragile sites and telomeres. Here, we unravel an unexpected direct interaction between SLX4 and the DNA helicase RTEL1, which, until now, were viewed as having independent and antagonistic functions. We identify cancer and Hoyeraal-Hreidarsson syndrome-associated mutations in SLX4 and RTEL1, r  ...[more]

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