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  Evolution of the protein stoichiometry in the L12 stalk of bacterial and organellar ribosomes.

Davydov, I., Wohlgemuth, I., Artamonova, I. I., Urlaub, H., Tonevitzky, A. G., & Rodnina, M. V. (2013). Evolution of the protein stoichiometry in the L12 stalk of bacterial and organellar ribosomes. Nature Communications, 4: 1387. doi:10.1038/ncomms2373.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-000E-70EC-4 Version Permalink: http://hdl.handle.net/11858/00-001M-0000-0028-3DA1-A
Genre: Journal Article

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 Creators:
Davydov, I., Author
Wohlgemuth, I.1, Author              
Artamonova, I. I., Author
Urlaub, H.2, Author              
Tonevitzky, A. G., Author
Rodnina, M. V.1, Author              
Affiliations:
1Department of Physical Biochemistry, MPI for biophysical chemistry, Max Planck Society, ou_578598              
2Research Group of Bioanalytical Mass Spectrometry, MPI for biophysical chemistry, Max Planck Society, ou_578613              

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 Abstract: The emergence of ribosomes and translation factors is central for understanding the origin of life. Recruitment of translation factors to bacterial ribosomes is mediated by the L12 stalk composed of protein L10 and several copies of protein L12, the only multi-copy protein of the ribosome. Here we predict stoichiometries of L12 stalk for >1,200 bacteria, mitochondria and chloroplasts by a computational analysis, and validate the predictions by quantitative mass spectrometry. The majority of bacteria have L12 stalks allowing for binding of four or six copies of L12, largely independent of the taxonomic group or living conditions of the bacteria, whereas some cyanobacteria have eight copies. Mitochondrial and chloroplast ribosomes can accommodate six copies of L12. The last universal common ancestor probably had six molecules of L12 molecules bound to L10. Changes of the stalk composition provide a unique possibility to trace the evolution of protein components of the ribosome.

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Language(s): eng - English
 Dates: 2013-01-22
 Publication Status: Published online
 Pages: 10
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 Rev. Method: Peer
 Identifiers: DOI: 10.1038/ncomms2373
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Title: Nature Communications
Source Genre: Journal
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Pages: - Volume / Issue: 4 Sequence Number: 1387 Start / End Page: - Identifier: -