PXD012425

PXD012425 is an original dataset announced via ProteomeXchange.

Title	Searching for new members of the SLX4 complex and for SLX4-complex members that are SUMOylated in vitro
Description	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.
HostingRepository	PRIDE
AnnounceDate	2020-03-05
AnnouncementXML	Submission_2020-05-27_06:08:06.xml
DigitalObjectIdentifier
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Unsupported dataset by repository
PrimarySubmitter	AUDEBERT Stephane
SpeciesList	scientific name: Homo sapiens (Human); NCBI TaxID: 9606;
ModificationList	monohydroxylated residue; iodoacetamide derivatized residue
Instrument	LTQ Orbitrap Velos

Revision	Datetime	Status	ChangeLog Entry
0	2019-01-18 03:11:40	ID requested
1	2020-03-05 05:01:04	announced
⏵ 2	2020-05-27 06:08:07	announced	2020-05-27: Updated publication reference for PubMed record(s): 32398829.

Takedachi A, Despras E, Scaglione S, Gu, é, rois R, Guervilly JH, Blin M, Audebert S, Camoin L, Hasanova Z, Schertzer M, Guille A, Churikov D, Callebaut I, Naim V, Chaffanet M, Borg JP, Bertucci F, Revy P, Birnbaum D, Londo, ñ, o-Vallejo A, Kannouche PL, Gaillard PHL, SLX4 interacts with RTEL1 to prevent transcription-mediated DNA replication perturbations. Nat Struct Mol Biol, 27(5):438-449(2020) [pubmed]

curator keyword: Biological

submitter keyword: SLX4 scaffold, protein SUMOylation, interactome

Marseille proteomics ; CRCM ; Gaillard PH lab
contact affiliation	Centre de Recherche en Cancérologie de Marseille, CRCM Inserm UMR1068, CNRS UMR7258, Aix Marseille Université U105, Institut Paoli Calmettes France
contact email	stephane.audebert@inserm.fr
lab head
AUDEBERT Stephane
contact affiliation	Pharmacology department
contact email	stephane.audebert@inserm.fr
dataset submitter

Dataset FTP location NOTE: Most web browsers have now discontinued native support for FTP access within the browser window. But you can usually install another FTP app (we recommend FileZilla) and configure your browser to launch the external application when you click on this FTP link. Or otherwise, launch an app that supports FTP (like FileZilla) and use this address: ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2020/03/PXD012425

PRIDE project URI

• PRIDE
  1. PXD012425
     1. Label: PRIDE project
     2. Name: Searching for new members of the SLX4 complex and for SLX4-complex members that are SUMOylated in vitro