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Comprehensive characterization of Minichromosome Maintenance Complex (MCM) protein interactions using affinity and proximity purifications coupled to mass spectrometry.

ABSTRACT: This project is the complete interactome of the Minichromosome Maintenance (MCM) complex by using AP-MS and BioID approaches for all the different MCM proteins. Overall, our analysis identified unique and shared interaction partners and proteins enriched for distinct biological processes including DNA replication, DNA repair and cell cycle regulation. Furthermore, we mapped the changes in protein interactions of the MCM complex in response to DNA damage, identifying a new role for this complex in DNA repair. In summary, we demonstrate the complementarity of these approaches for the characterization of protein interactions within the MCM complex.

INSTRUMENT(S): Q Exactive

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Fibroblast

DISEASE(S): Osteosarcoma

SUBMITTER: Francois-Michel Boisvert

LAB HEAD: Francois-Michel Boisvert

PROVIDER: PXD004089 | Pride | 2016-08-09

REPOSITORIES: Pride

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Comprehensive Characterization of Minichromosome Maintenance Complex (MCM) Protein Interactions Using Affinity and Proximity Purifications Coupled to Mass Spectrometry.

Dubois Marie-Line ML Bastin Charlotte C Lévesque Dominique D Boisvert François-Michel FM

Journal of proteome research 20160816 9

The extensive identification of protein-protein interactions under different conditions is an important challenge to understand the cellular functions of proteins. Here we use and compare different approaches including affinity purification and purification by proximity coupled to mass spectrometry to identify protein complexes. We explore the complete interactome of the minichromosome maintenance (MCM) complex by using both approaches for all of the different MCM proteins. Overall, our analysis ...[more]

PMID: 27494197

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Comprehensive characterization of Minichromosome Maintenance Complex (MCM) protein interactions using affinity and proximity purifications coupled to mass spectrometry.

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