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Three-dimensional structures of translating ribosomes by Cryo-EM

MPG-Autoren
http://pubman.mpdl.mpg.de/cone/persons/resource/persons50160

Fucini,  Paola
Ribosomes, Max Planck Institute for Molecular Genetics, Max Planck Society;

http://pubman.mpdl.mpg.de/cone/persons/resource/persons50126

Connell,  Sean
Dept. of Vertebrate Genomics (Head: Hans Lehrach), Max Planck Institute for Molecular Genetics, Max Planck Society;

http://pubman.mpdl.mpg.de/cone/persons/resource/persons50444

Nierhaus,  Knud H.
Ribosomes, Max Planck Institute for Molecular Genetics, Max Planck Society;

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Zitation

Gilbert, R. J. C., Fucini, P., Connell, S., Fuller, S. D., Nierhaus, K. H., Robinson, C. V., et al. (2004). Three-dimensional structures of translating ribosomes by Cryo-EM. Molecular Cell, 14(1), 57-66. doi:10.1016/S1097-2765(04)00163-7.


Zitierlink: http://hdl.handle.net/11858/00-001M-0000-0010-8870-4
Zusammenfassung
Cryo-electron microscopy and image reconstruction techniques have been used to obtain three-dimensional maps for E. coli ribosomes stalled following translation of three representative proteins. Comparisons of these electron density maps, at resolutions of between 13 and 16 Å, with that of a nontranslating ribosome pinpoint specific structural differences in stalled ribosomes and identify additional material, including tRNAs and mRNA. In addition, the tunnel through the large subunit, the anticipated exit route of newly synthesized proteins, is partially occluded in all the stalled ribosome structures. This observation suggests that significant segments of the nascent polypeptide chains examined here could be located within an expanded tunnel, perhaps in a rudimentary globular conformation. Such behavior could be an important aspect of the folding of at least some proteins in the cellular environment.