Binding of SecB to ribosome-bound polypeptides has the same characteristics as binding to full-length, denatured proteins
Author:
Publisher
Proceedings of the National Academy of Sciences
Subject
Multidisciplinary
Reference26 articles.
1. High selectivity with low specificity: how SecB has solved the paradox of chaperone binding
2. Cytosolic factor purified from Escherichia coli is necessary and sufficient for the export of a preprotein and is a homotetramer of SecB.
3. High-affinity binding of Escherichia coli SecB to the signal sequence region of a presecretory protein.
4. The antifolding activity of SecB promotes the export of the E. coli maltose-binding protein
5. Physiological role during export for the retardation of folding by the leader peptide of maltose-binding protein.
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1. Selective ribosome profiling reveals a role for SecB in the co-translational inner membrane protein biogenesis;Cell Reports;2022-12
2. Ribosome profiling reveals multiple roles of SecA in cotranslational protein export;Nature Communications;2022-06-13
3. Codon Selection Affects Recruitment of Ribosome-Associating Factors during Translation;ACS Synthetic Biology;2019-11-26
4. Molecular Mimicry of SecA and Signal Recognition Particle Binding to the Bacterial Ribosome;mBio;2019-08-27
5. Mechanisms of Cotranslational Maturation of Newly Synthesized Proteins;Annual Review of Biochemistry;2019-06-20
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