期刊
MOLECULAR & CELLULAR PROTEOMICS
卷 17, 期 10, 页码 2018-2033出版社
ELSEVIER
DOI: 10.1074/mcp.RA118.000924
关键词
Protein Cross-linking; Protein-Protein Interactions; Histones; Chromatin function or biology; Mass Spectrometry; Histone interaction network - PTM interplay; Histone variant specific interactions; Nuclear interactome
资金
- Proteins@Work, a program of the Netherlands Proteomics Centre - Netherlands Organisation for Scientific Research as part of the National Roadmap Large-Scale Research Facilities of the Netherlands [184.032.201]
- European Union's Horizon 2020 research and innovation program [686547]
Cells organize their actions partly through tightly controlled protein-protein interactions-collectively termed the interactome. Here we use crosslinking mass spectrometry (XL-MS) to chart the protein-protein interactions in intact human nuclei. Overall, we identified similar to 8,700 crosslinks, of which 2/3 represent links connecting distinct proteins. From these data, we gain insights on interactions involving histone proteins. We observed that core histones on the nucleosomes expose well-defined interaction hot spots. For several nucleosome-interacting proteins, such as USF3 and Ran GTPase, the data allowed us to build low-resolution models of their binding mode to the nucleosome. For HMGN2, the data guided the construction of a refined model of the interaction with the nucleosome, based on complementary NMR, XL-MS, and modeling. Excitingly, the analysis of crosslinks carrying posttranslational modifications allowed us to extract how specific modifications influence nucleosome interactions. Overall, our data depository will support future structural and functional analysis of cell nuclei, including the nucleoprotein assemblies they harbor.
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