Fidelity of Cotranslational Protein Targeting by the Signal Recognition Particle
- Creators
- Zhang, Xin
- Shan, Shu-ou
Abstract
Accurate folding, assembly, localization, and maturation of newly synthesized proteins are essential to all cells and require high fidelity in the protein biogenesis machineries that mediate these processes. Here, we review our current understanding of how high fidelity is achieved in one of these processes, the cotranslational targeting of nascent membrane and secretory proteins by the signal recognition particle (SRP). Recent biochemical, biophysical, and structural studies have elucidated how the correct substrates drive a series of elaborate conformational rearrangements in the SRP and SRP receptor GTPases; these rearrangements provide effective fidelity checkpoints to reject incorrect substrates and enhance the fidelity of this essential cellular pathway. The mechanisms used by SRP to ensure fidelity share important conceptual analogies with those used by cellular machineries involved in DNA replication, transcription, and translation, and these mechanisms likely represent general principles for other complex cellular pathways.
Additional Information
© 2014 Annual Reviews. The authors are not aware of any affiliations, memberships, funding, or financial holdings that might be perceived as affecting the objectivity of this review.Attached Files
Accepted Version - nihms689575.pdf
Files
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Additional details
- PMCID
- PMC4444370
- Eprint ID
- 46097
- Resolver ID
- CaltechAUTHORS:20140605-104144841
- Created
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2014-06-05Created from EPrint's datestamp field
- Updated
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2021-11-10Created from EPrint's last_modified field