Journal Article FZJ-2013-05183

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Energy barriers and driving forces in tRNA translocation through the ribosome

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2013
Nature Publishing Group London [u.a.]

Nature structural & molecular biology 2690, 1-8 () [10.1038/nsmb.2690]

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Abstract: During protein synthesis, tRNAs move from the ribosome's aminoacyl to peptidyl to exit sites. Here we investigate conformational motions during spontaneous translocation, using molecular dynamics simulations of 13 intermediate-translocation-state models obtained by combining Escherichia coli ribosome crystal structures with cryo-EM data. Resolving fast transitions between states, we find that tRNA motions govern the transition rates within the pre- and post-translocation states. Intersubunit rotations and L1-stalk motion exhibit fast intrinsic submicrosecond dynamics. The L1 stalk drives the tRNA from the peptidyl site and links intersubunit rotation to translocation. Displacement of tRNAs is controlled by 'sliding' and 'stepping' mechanisms involving conserved L16, L5 and L1 residues, thus ensuring binding to the ribosome despite large-scale tRNA movement. Our results complement structural data with a time axis, intrinsic transition rates and molecular forces, revealing correlated functional motions inaccessible by other means.

Classification:

Contributing Institute(s):
  1. Strukturbiochemie (ICS-6)
Research Program(s):
  1. 452 - Structural Biology (POF2-452) (POF2-452)

Appears in the scientific report 2013
Database coverage:
Medline ; BIOSIS Previews ; Current Contents - Life Sciences ; JCR ; NCBI Molecular Biology Database ; NationallizenzNationallizenz ; SCOPUS ; Science Citation Index ; Science Citation Index Expanded ; Thomson Reuters Master Journal List ; Web of Science Core Collection
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 Record created 2013-11-13, last modified 2021-01-29


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