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Dissecting ribosomal particles throughout the kingdoms of life using advanced hybrid mass spectrometry methods.
van de Waterbeemd, Michiel; Tamara, Sem; Fort, Kyle L; Damoc, Eugen; Franc, Vojtech; Bieri, Philipp; Itten, Martin; Makarov, Alexander; Ban, Nenad; Heck, Albert J R.
Afiliação
  • van de Waterbeemd M; Biomolecular Mass Spectrometry and Proteomics, Bijvoet Center for Biomolecular Research and Utrecht Institute for Pharmaceutical Sciences, Utrecht University, Utrecht, 3584CH, The Netherlands.
  • Tamara S; Netherlands Proteomics Center, 3584CH, Utrecht, The Netherlands.
  • Fort KL; Biomolecular Mass Spectrometry and Proteomics, Bijvoet Center for Biomolecular Research and Utrecht Institute for Pharmaceutical Sciences, Utrecht University, Utrecht, 3584CH, The Netherlands.
  • Damoc E; Netherlands Proteomics Center, 3584CH, Utrecht, The Netherlands.
  • Franc V; Biomolecular Mass Spectrometry and Proteomics, Bijvoet Center for Biomolecular Research and Utrecht Institute for Pharmaceutical Sciences, Utrecht University, Utrecht, 3584CH, The Netherlands.
  • Bieri P; Netherlands Proteomics Center, 3584CH, Utrecht, The Netherlands.
  • Itten M; Thermo Fisher Scientific, 28199, Bremen, Germany.
  • Makarov A; Thermo Fisher Scientific, 28199, Bremen, Germany.
  • Ban N; Biomolecular Mass Spectrometry and Proteomics, Bijvoet Center for Biomolecular Research and Utrecht Institute for Pharmaceutical Sciences, Utrecht University, Utrecht, 3584CH, The Netherlands.
  • Heck AJR; Netherlands Proteomics Center, 3584CH, Utrecht, The Netherlands.
Nat Commun ; 9(1): 2493, 2018 06 27.
Article em En | MEDLINE | ID: mdl-29950687
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.

Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Idioma: En Ano de publicação: 2018 Tipo de documento: Article

Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Idioma: En Ano de publicação: 2018 Tipo de documento: Article