Proteomic data on the nuclear interactome of human MCM9

Abstract

We present data relating to the interactome of MCM9 from the nuclei of human cells. MCM9 belongs to the AAA+ superfamily, and contains an MCM domain and motifs that may confer DNA helicase activity. MCM9 has been shown to bind MCM8, and has been implicated in DNA replication and homologous recombination. However, the mechanistic basis of MCM9’s role in DNA repair is poorly understood, and proteins with which it interacts were hitherto unknown. We performed tandem affinity purification of MCM9 and its interacting proteins from nuclear extracts of human cells, followed by proteomic analysis, thereby generating a set of mass spectrometry data corresponding to the MCM9 interactome [1]. The proteomic data set comprises 29 mass spectrometry RAW files, deposited to the ProteomeXchange Consortium, and freely available from the PRIDE partner repository with the data set identifier PXD000212. A set of 22 interacting proteins identified from the proteomic data was used to create an MCM9-centered interactive network diagram, using the Cytoscape program. These data allow the scientific community to access, mine and explore the human nuclear MCM9 interactome.

Molecular functions of MCM8 and MCM9 and their associated pathologies

“…As MCM9 co-immunoprecipitates with multiple MMR initiation proteins, including MSH2, MSH3, MLH1 and PMS1 (OMIM 600258 ), it was hypothesized that MCM9 plays a role in MMR. 21 , 65 This hypothesis gained traction when Traver et al. 21 reported that MCM9 KO cells display MMR deficiency and MSI.…”

Mechanism of DNA unwinding by hexameric MCM8-9 in complex with HROB

“…They are missing in fungi and nematodes, but present in most plants and vertebrates, while Drosophila only contains an MCM8 homologue [16][17][18] . The MCM8 and MCM9 proteins associate together (MCM8-9) and are similarly thought to form hexamers [19][20][21] , yet the oligomeric state of the fulllength human proteins remains uncharacterized. While MCM8 has the standard domain structure, MCM9 contains an unusual C-terminal extension downstream of the AAA+ ATPase site 22 .…”