Reading frame switch caused by base-pair formation between the 3′ end of 16S rRNA and the mRNA during elongation of protein synthesis in Escherichia coli
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Watson-Crick base pairing is shown to occur between the mRNA and nucleotides near the 3' end of 16S rRNA during the elongation phase of protein synthesis in Escherichia coli. This base-pairing is similar to the mRNA-rRNA interaction formed during initiation of protein synthesis between the Shine and Dalgarno (S-D) nucleotides of ribosome binding sites and their complements in the 1540-1535 region of 16S rRNA. mRNA-rRNA hybrid formation during elongation had been postulated to explain the dependence of an efficient ribosomal frameshift on S-D nucleotides precisely spaced 5' on the mRNA from the frameshift site. Here we show that disruption of the postulated base pairs by single nucleotide substitutions, either in the S-D sequence required for shifting or in nucleotide 1538 of 16S rRNA, decrease the amount of shifting, and that this defect is corrected by restoring complementary base pairing. This result implies that the 3' end of 16S rRNA scans the mRNA very close to the decoding sites during elongation.
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In many cases, misreading UGA stop codons in prokaryotes is associated with a +1 frameshift.
“However, in many cases, misreading UGA stop codons in prokaryotes is associated with a +1 frameshift [81,82,83,84].”
From Detailed Dissection and Critical Evaluation of the Pfizer/BioNTech and Moderna mRNA Vaccines (2021) · cites this paper as [83]
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- Noller,H.F., Asire,M., Barta,A., Douthwaite,S., Goldstein,T., Gutell,R.R., Moazed,D., Normanly,J., Prince,J.B., Stern,S., Triman,K., Turner,S., Van Stolk,B., Wheaton,V., Weiser,B. and Woese,C.R. (1986) In Hardes- ty,B. and Kramer,G. (eds), Structure, Function and Genetics of Ribosomes. Springer-Verlag, New York, pp. 143-163.
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- Weiss,R.B., Dunn,D.M., Atkins,J.F. and Gesteland,R.F. (1987) C.S.H.S.Q.B., 52, in press. Received on November 1987; revised on February 2, 1988 ,3-Galactosidase activity measurements Whole-cell assays were based on the procedure according to Miller (1972). Whole-cell assays were carried out in a final volume of 1.0 ml Z-buffer, the assays were started with the addition of 0.2 ml of 4 mg/ml O-nitro- phenyl-t3-D galactopyranoside and stopped with the addition of 0.5 ml of 1 M Na2CO3, pH 11. All reactions were run at 28°C. The assay tubes were centrifuged before reading the A420. The whole cell unit definition is 3-gal units = [1000(A420)]/[OD6W x time(min) x vol.(ml)]. Labelling and purification of protein Affl-galactosidase fusions Cells were grown in M9 minimal = 0.2% glucose + 18 amino acids (0.05 mg/ml, no met or cys) + 1 jig/ml thiamine, heat-shocked at 42°C and grown for two doublings with rapid aeration. Spectinomycin (Sigma) was added to a final concentration of 0.5 mg/ml; and after 5 min 0.1 mCi of
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Detailed Dissection and Critical Evaluation of the Pfizer/BioNTech and Moderna mRNA Vaccines
Xia, X. (2021) · Vaccines · doi:10.3390/vaccines9070734 · Cited by 201 · see citing works
- Authors
- Weiss, R. B., Dunn, D. M., Dahlberg, A. E., Atkins, J. F., & Gesteland, R. F.
- Affiliations
- University of Utah (US)
- Venue
- The EMBO Journal
- Published
- 1988-05-01
- Volume
- 7
- Issue
- 5
- Pages
- 1503-1507
- ISSN
- 0261-4189 (ISSN-L)
- 1460-2075
- PMC
- PMC458402
- OpenAlex
- W2418466522
- Cited by
- 230
- References
- 0
- Citations by year
- 2026: 2 · 2025: 2 · 2024: 1 · 2023: 4 · 2021: 2 · 2020: 1 · 2018: 8 · 2016: 4 · 2015: 3 · 2014: 5 · 2013: 3 · 2012: 7
- FWCI
- 7.93
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- The EMBO Journal (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Science Foundation (8408649)
- Howard Hughes Medical Institute
- Helen Hay Whitney Foundation
- National Institutes of Health
- National Institute of General Medical Sciences (GM19756)
- 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 modifications and cancer
- Keywords
- ribosomal frameshifting, 16S rRNA, protein synthesis elongation, Shine-Dalgarno sequence, ribosome binding site, Escherichia coli, decoding site, single nucleotide substitution, Watson-Crick base pairing
- MeSH terms
- Bacterial Proteins, Base Composition, Base Sequence, Escherichia coli, Peptide Chain Elongation, Translational, RNA, Bacterial, RNA, Messenger, RNA, Ribosomal
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