MifM-instructed translation arrest involves nascent chain interactions with the exterior as well as the interior of the ribosome
Author:
Funder
Ministry of Education, Culture, Sports, Science, and Technology
Japan Society for the Promotion of Science
Publisher
Springer Science and Business Media LLC
Subject
Multidisciplinary
Link
http://www.nature.com/articles/s41598-018-28628-y.pdf
Reference58 articles.
1. Ito, K. & Chiba, S. Arrest peptides: cis-acting modulators of translation. Annu. Rev. Biochem. 82, 171–202 (2013).
2. Chiba, S., Lamsa, A. & Pogliano, K. A ribosome-nascent chain sensor of membrane protein biogenesis in Bacillus subtilis. EMBO J. 28, 3461–3475 (2009).
3. Chiba, S. & Ito, K. MifM monitors total YidC activities of Bacillus subtilis, including that of YidC2, the target of regulation. J. Bacteriol. 197, 99–107 (2015).
4. Dalbey, R. E., Wang, P. & Kuhn, A. Assembly of bacterial inner membrane proteins. Annu. Rev. Biochem. 80, 161–187 (2011).
5. Wang, P. & Dalbey, R. E. Inserting membrane proteins: the YidC/Oxa1/Alb3 machinery in bacteria, mitochondria, and chloroplasts. Biochim. Biophys. Acta 1808, 866–875 (2011).
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1. Nonspecific N-terminal tetrapeptide insertions disrupt the translation arrest induced by ribosome-arresting peptide sequences;Journal of Biological Chemistry;2024-06
2. Patchy and widespread distribution of bacterial translation arrest peptides associated with the protein localization machinery;Nature Communications;2024-04-02
3. Functional domains of a ribosome arresting peptide are affected by surrounding nonconserved residues;Journal of Biological Chemistry;2024-03
4. Patchy and widespread distribution of bacterial translation arrest peptides associated with the protein localization machinery;2023-09-02
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