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dc.contributor.authorPardo, M
dc.contributor.authorYu, L
dc.contributor.authorShen, S
dc.contributor.authorTate, P
dc.contributor.authorBode, D
dc.contributor.authorLetney, BL
dc.contributor.authorQuelle, DE
dc.contributor.authorSkarnes, W
dc.contributor.authorChoudhary, JS
dc.date.accessioned2020-10-15T15:28:07Z
dc.date.issued2017-08-15
dc.identifier.citationScientific reports, 2017, 7 (1), pp. 8157 - ?
dc.identifier.issn2045-2322
dc.identifier.urihttps://repository.icr.ac.uk/handle/internal/4160
dc.identifier.eissn2045-2322
dc.identifier.doi10.1038/s41598-017-08456-2
dc.description.abstractMYST 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.
dc.formatElectronic
dc.format.extent8157 - ?
dc.languageeng
dc.language.isoeng
dc.publisherNATURE PUBLISHING GROUP
dc.rights.urihttps://creativecommons.org/licenses/by/4.0
dc.subjectPluripotent Stem Cells
dc.subjectAnimals
dc.subjectMice, Knockout
dc.subjectMice
dc.subjectCarrier Proteins
dc.subjectDNA-Binding Proteins
dc.subjectProteome
dc.subjectProteomics
dc.subjectComputational Biology
dc.subjectCell Proliferation
dc.subjectChromatin Assembly and Disassembly
dc.subjectProtein Binding
dc.subjectAcetylation
dc.subjectAlleles
dc.subjectFemale
dc.subjectMale
dc.subjectHistone Acetyltransferases
dc.subjectMass Spectrometry
dc.subjectEmbryonic Stem Cells
dc.subjectGene Regulatory Networks
dc.titleMyst2/Kat7 histone acetyltransferase interaction proteomics reveals tumour-suppressor Niam as a novel binding partner in embryonic stem cells.
dc.typeJournal Article
dcterms.dateAccepted2017-07-10
rioxxterms.versionofrecord10.1038/s41598-017-08456-2
rioxxterms.licenseref.urihttps://creativecommons.org/licenses/by/4.0
rioxxterms.licenseref.startdate2017-08-15
rioxxterms.typeJournal Article/Review
dc.relation.isPartOfScientific reports
pubs.issue1
pubs.notesNot known
pubs.organisational-group/ICR
pubs.organisational-group/ICR/Primary Group
pubs.organisational-group/ICR/Primary Group/ICR Divisions
pubs.organisational-group/ICR/Primary Group/ICR Divisions/Cancer Biology
pubs.organisational-group/ICR/Primary Group/ICR Divisions/Cancer Biology/Functional Proteomics Group
pubs.organisational-group/ICR
pubs.organisational-group/ICR/Primary Group
pubs.organisational-group/ICR/Primary Group/ICR Divisions
pubs.organisational-group/ICR/Primary Group/ICR Divisions/Cancer Biology
pubs.organisational-group/ICR/Primary Group/ICR Divisions/Cancer Biology/Functional Proteomics Group
pubs.publication-statusPublished
pubs.volume7
pubs.embargo.termsNot known
icr.researchteamFunctional Proteomics Group
dc.contributor.icrauthorPardo Calvo, Maria Mercedes
dc.contributor.icrauthorChoudhary, Jyoti


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