Hamacher, Kay ; Trylska, J. ; McCammon, J. A. (2006)
Dependency map of proteins in the small ribosomal subunit.
In: PLoS Comp. Biol., 2 (2)
doi: 10.1371/journal.pcbi.0020010
Artikel, Bibliographie
Kurzbeschreibung (Abstract)
The assembly of the ribosome has recently become an interesting target for antibiotics in several bacteria. In this work, we extended an analytical procedure to determine native state fluctuations and contact breaking to investigate the protein stability dependence in the 30S small ribosomal subunit of Thermus thermophilus. We determined the causal influence of the presence and absence of proteins in the 30S complex on the binding free energies of other proteins. The predicted dependencies are in overall agreement with the experimentally determined assembly map for another organism, Escherichia coli. We found that the causal influences result from two distinct mechanisms: one is pure internal energy change, the other originates from the entropy change. We discuss the implications on how to target the ribosomal assembly most effectively by suggesting six proteins as targets for mutations or other hindering of their binding. Our results show that by blocking one out of this set of proteins, the association of other proteins is eventually reduced, thus reducing the translation efficiency even more. We could additionally determine the binding dependency of THX peptide not present in the ribosome of E. coli and suggest its assembly path.
| Typ des Eintrags: | Artikel |
|---|---|
| Erschienen: | 2006 |
| Autor(en): | Hamacher, Kay ; Trylska, J. ; McCammon, J. A. |
| Art des Eintrags: | Bibliographie |
| Titel: | Dependency map of proteins in the small ribosomal subunit |
| Sprache: | Englisch |
| Publikationsjahr: | 2006 |
| Titel der Zeitschrift, Zeitung oder Schriftenreihe: | PLoS Comp. Biol. |
| Jahrgang/Volume einer Zeitschrift: | 2 |
| (Heft-)Nummer: | 2 |
| DOI: | 10.1371/journal.pcbi.0020010 |
| Kurzbeschreibung (Abstract): | The assembly of the ribosome has recently become an interesting target for antibiotics in several bacteria. In this work, we extended an analytical procedure to determine native state fluctuations and contact breaking to investigate the protein stability dependence in the 30S small ribosomal subunit of Thermus thermophilus. We determined the causal influence of the presence and absence of proteins in the 30S complex on the binding free energies of other proteins. The predicted dependencies are in overall agreement with the experimentally determined assembly map for another organism, Escherichia coli. We found that the causal influences result from two distinct mechanisms: one is pure internal energy change, the other originates from the entropy change. We discuss the implications on how to target the ribosomal assembly most effectively by suggesting six proteins as targets for mutations or other hindering of their binding. Our results show that by blocking one out of this set of proteins, the association of other proteins is eventually reduced, thus reducing the translation efficiency even more. We could additionally determine the binding dependency of THX peptide not present in the ribosome of E. coli and suggest its assembly path. |
| Freie Schlagworte: | Bioinformatik |
| Fachbereich(e)/-gebiet(e): | 10 Fachbereich Biologie ?? fb10_mikrobiologie ?? 10 Fachbereich Biologie > Computational Biology and Simulation 20 Fachbereich Informatik |
| Hinterlegungsdatum: | 27 Mai 2010 13:56 |
| Letzte Änderung: | 03 Jan 2019 14:01 |
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