Dataset Information

Exonuclease-1 interactome and phosphorylation sites

ABSTRACT: To help shedding light on regulatory aspects of DNA repair and remodeling pathways in which EXO1 participates and to help revealing novel cellular processes in which EXO1 is involved, we set out to identify proteins interacting with EXO1. Both a small-scale approach and a comprehensive analysis of the EXO1 interactome allowed identifying novel protein partners that are involved in RNA processing or that are the causative agents of rare X-linked disorders. Follow-up biochemical studies allowed validating the direct interaction with selected proteins. Extensive coverage of EXO1 sequence (>85%) allowed conducting an in-depth analysis of its phosphorylation sites, with the identification of 26 residues that are differentially modified in untreated conditions or upon induction of DNA damage.

INSTRUMENT(S):

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Cell Culture

SUBMITTER: Daniel Hess

LAB HEAD: Daniel Hess

PROVIDER: PXD002780 | Pride | 2019-01-31

REPOSITORIES: Pride

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The human Exonuclease-1 interactome and phosphorylation sites.

Eid Wassim W Hess Daniel D König Christiane C Gentili Christian C Ferrari Stefano S

Biochemical and biophysical research communications 20190502 3

Error-free repair of DNA double-strand breaks is orchestrated by homologous recombination (HR) pathways and requires the concerted action of several factors. Among these, Exonulcease-1 (EXO1) and DNA2/BLM execute extensive resection of DNA ends to produce 3'-overhangs, which are key intermediates for downstream steps of HR. To help shedding light on regulatory aspects of DNA repair pathways in which EXO1 participates, we set out to identify proteins interacting with EXO1. Affinity purification o ...[more]

PMID: 31056253

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