Journal article
Myst2/Kat7 histone acetyltransferase interaction proteomics reveals tumour-suppressor Niam as a novel binding partner in embryonic stem cells
Scientific reports, Vol.7(1), pp.8157-14
08/15/2017
DOI: 10.1038/s41598-017-08456-2
PMCID: PMC5557939
PMID: 28811661
Abstract
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 tumour suppressor protein Niam (Nuclear Interactor of ARF and Mdm2). 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 early development and survival as well as cancer. Data are available via ProteomeXchange with identifier PXD005987.
Details
- Title: Subtitle
- Myst2/Kat7 histone acetyltransferase interaction proteomics reveals tumour-suppressor Niam as a novel binding partner in embryonic stem cells
- Creators
- Mercedes Pardo - Proteomic Mass Spectrometry, Wellcome Trust Sanger Institute, Wellcome Genome Campus, Hinxton, Cambridge, CB10 1SA, United Kingdom. mp3@sanger.ac.ukLu Yu - Proteomic Mass Spectrometry, Wellcome Trust Sanger Institute, Wellcome Genome Campus, Hinxton, Cambridge, CB10 1SA, United KingdomShihpei Shen - Cold Genesys Inc., Santa Ana, CA, USAPeri Tate - Stem Cell Engineering, Wellcome Trust Sanger Institute, Wellcome Genome Campus, Hinxton, Cambridge, CB10 1SA, United KingdomDaniel Bode - Wellcome Trust PhD Program, Cambridge Stem Cell Institute, Cambridge, Cambridgeshire, United KingdomBlake L Letney - Departments of Pharmacology and Pathology, The University of Iowa and Holden Comprehensive Cancer Center, Iowa City, IA, 52242, USADawn E Quelle - Departments of Pharmacology and Pathology, The University of Iowa and Holden Comprehensive Cancer Center, Iowa City, IA, 52242, USAWilliam Skarnes - Stem Cell Engineering, Wellcome Trust Sanger Institute, Wellcome Genome Campus, Hinxton, Cambridge, CB10 1SA, United KingdomJyoti S Choudhary - Proteomic Mass Spectrometry, Wellcome Trust Sanger Institute, Wellcome Genome Campus, Hinxton, Cambridge, CB10 1SA, United Kingdom
- Resource Type
- Journal article
- Publication Details
- Scientific reports, Vol.7(1), pp.8157-14
- Publisher
- England
- DOI
- 10.1038/s41598-017-08456-2
- PMID
- 28811661
- PMCID
- PMC5557939
- ISSN
- 2045-2322
- eISSN
- 2045-2322
- Grant note
- WT098051 / Wellcome Trust Wellcome Trust P30 CA086862 / NCI NIH HHS R01 CA090367 / NCI NIH HHS
- Language
- English
- Date published
- 08/15/2017
- Academic Unit
- Pathology; Neuroscience and Pharmacology
- Record Identifier
- 9984040234402771
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