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Assembly Mapping of 30 S Ribosomal Proteins from Escherichia coli
Open accessAbstract
Further studies were performed on the sequence of addition of proteins to 16 S RNA during the in vitro reconstitution of 30 S ribosomal subunits from Escherichia coli. Direct binding of protein S17 to 16 S RNA was studied in detail, and the following results were obtained: (a) under reconstitution conditions, a maximum of approximately 1 mole of S17 is bound per mole of 16 S RNA, either alone, or in the presence of all other 30 S proteins; (b) S17 binds only to 16 S RNA and not to 23 S RNA; and (c) radioactive S17–16 S RNA complexes are directly converted (without dissociation) to 30 S subunits by the addition of excess unlabeled total 30 S proteins. From these results, we conclude that the binding of S17 to 16 S RNA is specific. We have also determined the positions of S15, S16, S17, and S12 in the assembly map and have clarified subsequent interactions depending on these proteins. A revised assembly map is presented which incorporates the additional information obtained from these experimental results.
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Cited by
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Wimberly, B. T., Brodersen, D. E., Clemons, W. M., Morgan-Warren, R. J., Carter, A. P., Vonrhein, C., Hartsch, T., & Ramakrishnan, V. (2000) · Nature · doi:10.1038/35030006 · Cited by 2,035
Crystal structures of complexes of the small ribosomal subunit with tetracycline, edeine and IF3
Pioletti, M., Schlünzen, F., Harms, J., Zarivach, R., Glühmann, M., Avila, H., Bashan, A., Bartels, H., Auerbach, T., Jacobi, C., et al. (2001) · The EMBO Journal · doi:10.1093/emboj/20.8.1829 · Cited by 527
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Crystal structure of the S15-rRNA complex.
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Chen, S. S., Sperling, E., Silverman, J. M., Davis, J. H., & Williamson, J. R. (2012) · Molecular BioSystems · doi:10.1039/c2mb25310k · Cited by 65
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Metadata
- Authors
- Held, W. A., Ballou, B., Mizushima, S., & Nomura, M.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 1974-05
- Volume
- 249
- Issue
- 10
- Pages
- 3103-3111
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W1492288245
- Cited by
- 424
- References
- 0
- FWCI
- 9.20
- Type
- journal article
- Language
- en
- Open access
- hybrid
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