Divergent stalling sequences sense and control cellular physiology.
Open accessAbstract
Recent studies have identified several amino acid sequences that interact with the ribosomal interior components and arrest their own elongation. Whereas stalling of the inducible class depends on specific low-molecular weight compounds, that of the intrinsic class is released when the nascent chain is transported across or inserted into the membrane. The stalled ribosome alters messenger RNA secondary structure and thereby contributes to regulation of the cis-located target gene expression at different levels. The stalling sequences are divergent but likely to utilize non-uniform nature of the peptide bond formation reactions and are recruited relatively recently to different biological systems, possibly including those to be identified in forthcoming studies.
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The regulation of SecA is achieved by the product of the upstream secM gene, which is co-transcribed with secA.
“This regulation is achieved by the product of the upstream secM gene, which is co-transcribed with secA.”
From The Dynamic SecYEG Translocon (2021) · cites this paper as Ito et al., 2010
A mechanism allows E. coli to tailor SecA levels to reduced translocation activity of the SecYEG translocon.
“This is different for SecA; here an intriguing mechanism has been identified that allows E. coli to tailor SecA-levels to reduced translocation activity of the SecYEG translocon (Ito et al., 2010; Ito and Chiba, 2013).”
From The Dynamic SecYEG Translocon (2021) · cites this paper as Ito et al., 2010
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References 58 · Cited by 107
- Authors
- Ito, K., Chiba, S., & Pogliano, K.
- Affiliations
- Kyoto Sangyo University (JP)
- Kyoto University (JP)
- University of California San Diego (US)
- Corresponding author
- Ito, Koreaki
- Venue
- Biochemical and Biophysical Research Communications
- Publisher
- Elsevier BV
- Published
- 2010-02
- Volume
- 393
- Issue
- 1
- Pages
- 1-5
- ISSN
- 0006-291X (ISSN-L)
- PMC
- PMC2885147
- OpenAlex
- W2061225259
- Cited by
- 107
- References
- 58
- Citations by year
- 2026: 1 · 2024: 1 · 2022: 2 · 2021: 2 · 2020: 3 · 2019: 3 · 2018: 6 · 2017: 5 · 2016: 9 · 2015: 12 · 2014: 13 · 2013: 12 · 2012: 16
- FWCI
- 1.40
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Biochemical and Biophysical Research Communications (publishedVersion)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- Funders
- Japan Society for the Promotion of Science (20247020)
- National Institute of General Medical Sciences (R01GM057045)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA and protein synthesis mechanisms
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Bacterial Genetics and Biotechnology
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA Research and Splicing
- Keywords
- ribosome stalling, translational arrest, mRNA secondary structure, peptide bond formation, ribosome-associated proteins, translational regulation
- MeSH terms
- Amino Acid Sequence, Anti-Bacterial Agents, Gene Expression Regulation, Nucleic Acid Conformation, Peptide Chain Elongation, Translational, Ribosomes, RNA, Messenger, Transcription Factors, Tryptophan, Directed Molecular Evolution, Protein Sorting Signals, Escherichia coli Proteins
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