de.mpg.escidoc.pubman.appbase.FacesBean
English
 
Help Guide Disclaimer Contact us Login
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT

Released

Journal Article

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

MPS-Authors
http://pubman.mpdl.mpg.de/cone/persons/resource/persons78832

Villa,  Elizabeth
Baumeister, Wolfgang / Molecular Structural Biology, Max Planck Institute of Biochemistry, Max Planck Society;

Locator
There are no locators available
Fulltext (public)

1284.full.pdf
(Any fulltext), 9MB

Supplementary Material (public)
There is no public supplementary material available
Citation

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.


Cite as: http://hdl.handle.net/11858/00-001M-0000-000E-DFA6-3
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.