Journal
NATURE COMMUNICATIONS
Volume 9, Issue -, Pages -Publisher
NATURE PORTFOLIO
DOI: 10.1038/s41467-018-04853-x
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Funding
- large-scale proteomics facility Proteins@Work [184.032.201]
- Netherlands Organization for Scientific Research (NWO)
- Spinoza Prize of NWO [SPI.2017.028]
- Fundamenteel Onderzoek der Materie (FOM) [12PR3303-2]
- European Union Horizon 2020 program FET-OPEN project MSmed [686547]
- Swiss National Science Foundation (SNSF)
- National Center of Competence in Research (NCCR) RNA and disease programme of the Swiss National Science Foundation (SNSF)
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Biomolecular mass spectrometry has matured strongly over the past decades and has now reached a stage where it can provide deep insights into the structure and composition of large cellular assemblies. Here, we describe a three-tiered hybrid mass spectrometry approach that enables the dissection of macromolecular complexes in order to complement structural studies. To demonstrate the capabilities of the approach, we investigate ribosomes, large ribonucleoprotein particles consisting of a multitude of protein and RNA subunits. We identify sites of sequence processing, protein post-translational modifications, and the assembly and stoichiometry of individual ribosomal proteins in four distinct ribosomal particles of bacterial, plant and human origin. Amongst others, we report extensive cysteine methylation in the zinc finger domain of the human S27 protein, the heptameric stoichiometry of the chloroplastic stalk complex, the heterogeneous composition of human 40S ribosomal subunits and their association to the CrPV, and HCV internal ribosome entry site RNAs.
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