Slowing Translation between Protein Domains by Increasing Affinity between mRNAs and the Ribosomal Anti-Shine–Dalgarno Sequence Improves Solubility-Reference-Cited by-同舟云学术

Slowing Translation between Protein Domains by Increasing Affinity between mRNAs and the Ribosomal Anti-Shine–Dalgarno Sequence Improves Solubility

Published:2015-12-16 Issue:2 Volume:5 Page:133-145
ISSN:2161-5063
Container-title:ACS Synthetic Biology
language:en
Short-container-title:ACS Synth. Biol.

Author:

Vasquez Kevin A.¹,Hatridge Taylor A.¹,Curtis Nicholas C.¹,Contreras Lydia M.¹

Affiliation:

1. McKetta Department of Chemical Engineering, University of Texas at Austin, 200 East Dean Keeton Street, Stop C0400, Austin, Texas 78712, United States

Funder

Welch Foundation

U.S. Department of Defense

National Science Foundation

Publisher

American Chemical Society (ACS)

Subject

Biochemistry, Genetics and Molecular Biology (miscellaneous),Biomedical Engineering,General Medicine

Link

https://pubs.acs.org/doi/pdf/10.1021/acssynbio.5b00193

Reference32 articles.

1. The ribosome as a platform for co-translational processing, folding and targeting of newly synthesized proteins

2. Cotranslational folding — omnia mea mecum porto?

3. Structural insight into the role of the ribosomal tunnel in cellular regulation

4. Intraribosomal Regulation of Expression and Fate of Proteins

5. A model of the translational apparatus based on a three-dimensional reconstruction of theEscherichia coliribosome

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