Proteome organization in a genome-reduced bacterium.


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.

DOI: 10.1126/science.1176343

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@article{Khner2009ProteomeOI, title={Proteome organization in a genome-reduced bacterium.}, author={Sebastian K{\"{u}hner and Vera van Noort and Matthew J. Betts and Alejandra Leo-Macias and Claire Batisse and Michaela Rode and Takuji Yamada and Tobias Maier and Samuel Bader and Pedro Beltran-Alvarez and Daniel Casta{\~n}o-D{\'i}ez and Wei-Hua Chen and Damien P Devos and Marc G{\"{u}ell and Tom{\'a}s Norambuena and Ines Racke and Vladimir Rybin and Alexander H. Schmidt and Eva Yus and Ruedi Aebersold and Richard Herrmann and Bettina B{\"{o}ttcher and Achilleas S. Frangakis and Robert B. Russell and Luis Serrano and Peer Bork and Anne-Claude Gavin}, journal={Science}, year={2009}, volume={326 5957}, pages={1235-40} }