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  Promiscuous behaviour of archaeal ribosomal proteins: Implications for eukaryotic ribosome evolution

Armache, J.-P., Anger, A. M., Marquez, V., Franckenberg, S., Froehlich, T., Villa, E., et al. (2013). Promiscuous behaviour of archaeal ribosomal proteins: Implications for eukaryotic ribosome evolution. NUCLEIC ACIDS RESEARCH, 41(2), 1284-1293. doi:10.1093/nar/gks1259.

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 Creators:
Armache, Jean-Paul1, Author
Anger, Andreas M.1, Author
Marquez, Viter1, Author
Franckenberg, Sibylle1, Author
Froehlich, Thomas1, Author
Villa, Elizabeth2, Author              
Berninghausen, Otto1, Author
Thomm, Michael1, Author
Arnold, Georg J.1, Author
Beckmann, Roland1, Author
Wilson, Daniel N.1, Author
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1external, ou_persistent22              
2Baumeister, Wolfgang / Molecular Structural Biology, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565142              

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Free keywords: INITIATION-FACTOR 6; CRYO-EM STRUCTURE; ELECTRON-MICROSCOPY; CRYSTAL-STRUCTURE; ANGSTROM RESOLUTION; TRANSFER-RNA; RIBONUCLEOPROTEIN PARTICLE; MOLECULAR-DYNAMICS; BACTERIAL RIBOSOME; ESCHERICHIA-COLI
 Abstract: In all living cells, protein synthesis occurs on ribonucleoprotein particles called ribosomes. Molecular models have been reported for complete bacterial 70S and eukaryotic 80S ribosomes; however, only molecular models of large 50S subunits have been reported for archaea. Here, we present a complete molecular model for the Pyrococcus furiosus 70S ribosome based on a 6.6 A cryo-electron microscopy map. Moreover, we have determined cryo-electron microscopy reconstructions of the Euryarchaeota Methanococcus igneus and Thermococcus kodakaraensis 70S ribosomes and Crenarchaeota Staphylothermus marinus 50S subunit. Examination of these structures reveals a surprising promiscuous behavior of archaeal ribosomal proteins: We observe intersubunit promiscuity of S24e and L8e (L7ae), the latter binding to the head of the small subunit, analogous to S12e in eukaryotes. Moreover, L8e and L14e exhibit intrasubunit promiscuity, being present in two copies per archaeal 50S subunit, with the additional binding site of L14e analogous to the related eukaryotic r-protein L27e. Collectively, these findings suggest insights into the evolution of eukaryotic ribosomal proteins through increased copy number and binding site promiscuity.

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Language(s): eng - English
 Dates: 2013-01
 Publication Status: Published in print
 Pages: 10
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: ISI: 000314121100055
DOI: 10.1093/nar/gks1259
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Title: NUCLEIC ACIDS RESEARCH
Source Genre: Journal
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Publ. Info: GREAT CLARENDON ST, OXFORD OX2 6DP, ENGLAND : OXFORD UNIV PRESS
Pages: - Volume / Issue: 41 (2) Sequence Number: - Start / End Page: 1284 - 1293 Identifier: ISSN: 0305-1048