Proteome Organization in a Genome-Reduced Bacterium

Sebastian Kuehner, Vera van Noort, Matthew J. Betts, Alejandra Leo-Macias, Claire Batisse, Michaela Rode, Takuji Yamada, Tobias Maier, Samuel Bader, Pedro Beltran-Alvarez, Daniel Castano-Diez, Wei-Hua Chen, Damien Devos, Marc Gueell, Tomas Norambuena, Ines Racke, Vladimir Rybin, Alexander Schmidt, Eva Yus, Ruedi AebersoldRichard Herrmann, Bettina Boettcher, Achilleas S. Frangakis, Robert B. Russell, Luis Serrano, Peer Bork, Anne-Claude Gavin

Research output: Contribution to journalArticlepeer-review


The genome of Mycoplasma pneumoniae is among the smallest found in self-replicating organisms. To study the basic principles of bacterial proteome organization, we used tandem affinity purification-mass spectrometry (TAP-MS) in a proteome-wide screen. The analysis revealed 62 homomultimeric and 116 heteromultimeric soluble protein complexes, of which the majority are novel. About a third of the heteromultimeric complexes show higher levels of proteome organization, including assembly into larger, multiprotein complex entities, suggesting sequential steps in biological processes, and extensive sharing of components, implying protein multifunctionality. Incorporation of structural models for 484 proteins, single-particle electron microscopy, and cellular electron tomograms provided supporting structural details for this proteome organization. The data set provides a blueprint of the minimal cellular machinery required for life.

Original languageEnglish
Pages (from-to)1235-1240
Number of pages6
Issue number5957
Publication statusPublished - 27 Nov 2009


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