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

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...

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Autores principales: Pardo, Mercedes, Yu, Lu, Shen, Shihpei, Tate, Peri, Bode, Daniel, Letney, Blake L., Quelle, Dawn E., Skarnes, William, Choudhary, Jyoti S.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Nature Publishing Group UK 2017
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5557939/
https://www.ncbi.nlm.nih.gov/pubmed/28811661
http://dx.doi.org/10.1038/s41598-017-08456-2
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author Pardo, Mercedes
Yu, Lu
Shen, Shihpei
Tate, Peri
Bode, Daniel
Letney, Blake L.
Quelle, Dawn E.
Skarnes, William
Choudhary, Jyoti S.
author_facet Pardo, Mercedes
Yu, Lu
Shen, Shihpei
Tate, Peri
Bode, Daniel
Letney, Blake L.
Quelle, Dawn E.
Skarnes, William
Choudhary, Jyoti S.
author_sort Pardo, Mercedes
collection PubMed
description 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.
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spelling pubmed-55579392017-08-16 Myst2/Kat7 histone acetyltransferase interaction proteomics reveals tumour-suppressor Niam as a novel binding partner in embryonic stem cells Pardo, Mercedes Yu, Lu Shen, Shihpei Tate, Peri Bode, Daniel Letney, Blake L. Quelle, Dawn E. Skarnes, William Choudhary, Jyoti S. Sci Rep Article 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. Nature Publishing Group UK 2017-08-15 /pmc/articles/PMC5557939/ /pubmed/28811661 http://dx.doi.org/10.1038/s41598-017-08456-2 Text en © The Author(s) 2017 Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/.
spellingShingle Article
Pardo, Mercedes
Yu, Lu
Shen, Shihpei
Tate, Peri
Bode, Daniel
Letney, Blake L.
Quelle, Dawn E.
Skarnes, William
Choudhary, Jyoti S.
Myst2/Kat7 histone acetyltransferase interaction proteomics reveals tumour-suppressor Niam as a novel binding partner in embryonic stem cells
title Myst2/Kat7 histone acetyltransferase interaction proteomics reveals tumour-suppressor Niam as a novel binding partner in embryonic stem cells
title_full Myst2/Kat7 histone acetyltransferase interaction proteomics reveals tumour-suppressor Niam as a novel binding partner in embryonic stem cells
title_fullStr Myst2/Kat7 histone acetyltransferase interaction proteomics reveals tumour-suppressor Niam as a novel binding partner in embryonic stem cells
title_full_unstemmed Myst2/Kat7 histone acetyltransferase interaction proteomics reveals tumour-suppressor Niam as a novel binding partner in embryonic stem cells
title_short Myst2/Kat7 histone acetyltransferase interaction proteomics reveals tumour-suppressor Niam as a novel binding partner in embryonic stem cells
title_sort myst2/kat7 histone acetyltransferase interaction proteomics reveals tumour-suppressor niam as a novel binding partner in embryonic stem cells
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5557939/
https://www.ncbi.nlm.nih.gov/pubmed/28811661
http://dx.doi.org/10.1038/s41598-017-08456-2
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