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Specific protection of 16 S rRNA by translationalinitiation factors
Abstract
The binding of initiation factors to 30 S ribosomal subunits protects specific sets of nucleotides in 16 S rRNA from base-specific chemical probes. Initiation factor 3 (IF-3) protects residues G700, G703 and G791 from attack by kethoxal. These protected bases are close to those in 16 S rRNA that are protected by 50 S subunits, providing a structural basis for the subunit dissociation activity of IF-3. The IF-3-dependent protections also flank bases that are protected by P-site-bound tRNA, in keeping with the possibility that IF-3 may interact with initiator tRNA, or influence the properties of the 30 S P site during initiation. IF-1 protects G530, A1492 and A1493 and causes enhanced reactivity of A1408. These bases are precisely the ones that are protected by the binding of tRNA to the ribosomal A site. This suggests that IF-1 mimics A-site-bound tRNA, and could serve to prevent premature binding of aminoacyl tRNA by blocking the 30 S A site. We were unable to detect any effect of IF-2 on the reactivity pattern of 16 S rRNA, suggesting that this factor may interact primarily through protein-protein interactions.
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The parts of 16S RNA responsible for pactamycin binding (H23b and H24a) also contain bases that are protected by initiation factor 3 (IF3).
“It is also interesting to note that the parts of 16S RNA responsible for its binding (H23b and H24a) also contain bases that are protected by initiation factor 3 (IF3) (Moazed et al. 1995”
From The Structural Basis for the Action of the Antibiotics Tetracycline, Pactamycin, and Hygromycin B on the 30S Ribosomal Subunit (2000) · cites this paper as Moazed et al. 1995
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Research works printed but not linked: 13
- Boileau, 1983, Direct cross-links between initiation factors 1, 2, and 3 and ribosomal proteins promoted by 2-iminothiolane, Biochemistry, 22, 3162, 10.1021/bi00282a020 · DOI
- Chapman, 1977, Protection of specific sites in 16 S RNA from chemical modification by association of 30 S and 50 S ribosomes, J. Mol. Biol., 109, 131, 10.1016/S0022-2836(77)80049-1 · DOI
- Ehresmann, 1986, Cross-linking of initiation factor IF3 to Escherichia coli 30 S ribosomal subunit by transdiamminedichloroplatinum (II) characterization of twocross-linking sites in 16 S rRNA: A possible way of functioning of IF3, Nucl. Acids Res., 14, 4803, 10.1093/nar/14.12.4803 · DOI
- Grunberg-Manago, 1977, Initiation mechanisms of protein synthesis, Progr. Nucl. Acid Res. Mol. Biol., 20, 209, 10.1016/S0079-6603(08)60474-2 · DOI
- Gualerzi, 1990, Initiation of mRNA translation in prokaryotes, Biochemistry, 29, 5881, 10.1021/bi00477a001 · DOI
- Hartz, 1989, Selection of the initiator tRNA by Escherichia coli initiation factors, Genes Develop., 3, 1899, 10.1101/gad.3.12a.1899 · DOI
- Herr, 1979, Mechanism of ribosomal subunit association: Discrimination of specific sites in 16 S RNA essential for association activity, J. Mol. Biol., 130, 433, 10.1016/0022-2836(79)90433-9 · DOI
- Moazed, 1986, Transfer RNA shields specific nucleotides in 16 S ribosomal RNA from attack by chemical probes, Cell, 47, 985, 10.1016/0092-8674(86)90813-5 · DOI
- Moazed, 1990, Binding of tRNA to the ribosomal A and P sites protects two distinct sets of nucleotides in 16 S rRNA, J. Mol. Biol., 211, 135, 10.1016/0022-2836(90)90016-F · DOI
- Moazed, 1986, Rapid chemical probing of conformation in 16 S ribosomal RNA and 30 S ribosomal subunits using primer extension, J. Mol. Biol., 187, 399, 10.1016/0022-2836(86)90441-9 · DOI
- Muralikrishna, 1989, Escherichia coli initiation factor 3 protein binding to 30 S ribosomal subunits alters the accessibility of nucleotides within the conserved central region of 16 S rRNA, Biochemistry, 28, 7505, 10.1021/bi00445a002 · DOI
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Cited by
Sorted by citations
Brodersen, D. E., Clemons, W. M., Carter, A. P., Morgan-Warren, R. J., Wimberly, B. T., & Ramakrishnan, V. (2000) · Cell · doi:10.1016/s0092-8674(00)00216-6 · Cited by 950
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Beck, H. J., & Moll, I. (2018) · Microbiology Spectrum · doi:10.1128/microbiolspec.rwr-0016-2017 · Cited by 55
Metadata
- Authors
- Moazed, D., Samaha, R. R., Gualerzi, C., & Noller, H. F.
- Affiliations
- University of California, Santa Cruz (US)
- Università di Camerino (IT)
- Corresponding author
- Noller, Harry F.
- Venue
- Journal of Molecular Biology
- Publisher
- Elsevier BV
- Published
- 1995-01
- Volume
- 248
- Issue
- 2
- Pages
- 207-210
- ISSN
- 0022-2836 (ISSN-L)
- OpenAlex
- W2056365366
- Cited by
- 152
- References
- 0
- Citations by year
- 2025: 1 · 2024: 4 · 2023: 2 · 2022: 1 · 2021: 2 · 2020: 1 · 2019: 2 · 2018: 3 · 2016: 6 · 2015: 2 · 2014: 2 · 2013: 3 · 2012: 3
- FWCI
- 1.72
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Journal of Molecular Biology (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Institute of General Medical Sciences (GM-17129)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA and protein synthesis mechanisms
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA modifications and cancer
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Bacterial Genetics and Biotechnology
- Keywords
- 16S rRNA, initiation factor 3, initiation factor 2, 30S ribosomal subunit, 50S subunit, ribosomal P site, ribosomal A site, initiator tRNA, ribosome subunit dissociation, protein-protein interaction
- MeSH terms
- Aldehydes, Bacterial Proteins, Butanones, Escherichia coli, Peptide Initiation Factors, Protein Binding, RNA, Ribosomal, 16S, RNA, Transfer, Molecular Probes, Eukaryotic Initiation Factor-1, Prokaryotic Initiation Factor-3, Prokaryotic Initiation Factor-1
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