Proteomics

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Characterisation of Myst2 and Niam interactomes in mouse embryonic stem cells


ABSTRACT: Here we undertake the characterisation of Myst2 protein interactions in mouse embryonic stem cells by affinity purification and mass spectrometry using a Myst2-FTAP tagged cell line. This protein interaction study confirms that in mouse embryonic stem cells Myst2 is part of H3 and H4 histone acetylation complexes similar to those described in somatic cells. We identify a novel Myst2- associated protein, the tumour suppressor protein Niam (Nuclear Interactor of Arf and Mdm2), and show that it also interacts with subunits of Myst2 H4 HAT complexes. Human NIAM is involved in chromosome segregation, p53 regulation and cell proliferation in somatic cells, but its role in embryonic stem cells is unknown. We describe the first Niam embryonic stem cell interactome, which includes proteins with roles in DNA replication and repair, transcription, splicing and ribosome biogenesis. Many of Myst2 and Niam binding partners are required for correct embryonic development, implicating Myst2 and NIAM in the cooperative regulation of this process and suggesting a novel role for Niam in embryonic biology. The data provides a useful resource for exploring Myst2 and Niam essential cellular functions and should contribute to deeper understanding of organism development and survival as well as the development of cancer.

INSTRUMENT(S): LTQ FT, LTQ Orbitrap Velos

ORGANISM(S): Mus Musculus (mouse)

TISSUE(S): Embryonic Stem Cell

SUBMITTER: James Wright  

LAB HEAD: Jyoti Choudhary

PROVIDER: PXD005987 | Pride | 2017-08-22

REPOSITORIES: Pride

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Publications

Myst2/Kat7 histone acetyltransferase interaction proteomics reveals tumour-suppressor Niam as a novel binding partner in embryonic stem cells.

Pardo Mercedes M   Yu Lu L   Shen Shihpei S   Tate Peri P   Bode Daniel D   Letney Blake L BL   Quelle Dawn E DE   Skarnes William W   Choudhary Jyoti S JS  

Scientific reports 20170815 1


MYST histone acetyltransferases have crucial functions in transcription, replication and DNA repair and are hence implicated in development and cancer. Here we characterise Myst2/Kat7/Hbo1 protein interactions in mouse embryonic stem cells by affinity purification coupled to mass spectrometry. This study confirms that in embryonic stem cells Myst2 is part of H3 and H4 histone acetylation complexes similar to those described in somatic cells. We identify a novel Myst2-associated protein, the tumo  ...[more]

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