Abstract
Translation is a central biological process, that is catalysed by a machinery consisting of RNA and protein. In this thesis three different protein components of the bacterial protein synthesis system have been structurally studied. Ribosome recycling factor (RRF) is essential for the recycling step of the translation cycle, elongation factor SelB is a specialised elongation factor needed for co-translational selenocysteine incorporation, and ribosomal protein L1 is a primary binding protein in ribosome assembly.
The structure of RRF from <i>Thermotoga maritima</i> was solved by X-ray crystallography. RRF is an L-shaped molecule with size and shape very similar to tRNA. This similarity in combination with data from the literature suggests that RRF can bind similarly to a tRNA to the ribosomal A-site.
The structure of a C-terminal, mRNA binding, part of SelB (SelB-C) from <i>Moorella thermoacetica</i> was solved. SelB-C consists of four winged-helix domains arranged into an L-shaped structure. The RNA binding site could be located in the structure based on sequence conservation and data from the literature. Sterical requirements suggest that the L-shape of SelB-C may have to open during the functional interaction with the ribosome.
Binding studies were performed with L1 from <i>Thermus thermophilus</i> and a 61-nucleotide fragment of 23S RNA. This protein-RNA complex was crystallised.
The structure of RRF from <i>Thermotoga maritima</i> was solved by X-ray crystallography. RRF is an L-shaped molecule with size and shape very similar to tRNA. This similarity in combination with data from the literature suggests that RRF can bind similarly to a tRNA to the ribosomal A-site.
The structure of a C-terminal, mRNA binding, part of SelB (SelB-C) from <i>Moorella thermoacetica</i> was solved. SelB-C consists of four winged-helix domains arranged into an L-shaped structure. The RNA binding site could be located in the structure based on sequence conservation and data from the literature. Sterical requirements suggest that the L-shape of SelB-C may have to open during the functional interaction with the ribosome.
Binding studies were performed with L1 from <i>Thermus thermophilus</i> and a 61-nucleotide fragment of 23S RNA. This protein-RNA complex was crystallised.
| Original language | English |
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| Qualification | Doctor |
| Awarding Institution |
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| Supervisors/Advisors |
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| Award date | 2002 Feb 22 |
| Publisher | |
| ISBN (Print) | 91-7874-176-9 |
| Publication status | Published - 2002 |
Bibliographical note
Defence detailsDate: 2002-02-22
Time: 10:15
Place: Lecture hall B, Center for Chemistry and Chemical Engineering
External reviewer(s)
Name: Kjeldgaard, Morten
Title: Associate Professor
Affiliation: [unknown]
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Article: I "Ribosomal protein L1 forms a specific complex with a 61 nucleotide fragment of 23S RNA"Selmer, M. and Liljas, A.,manuscript
Article: II "Crystallization and preliminary X-ray analysis of Thermatoga maritima Ribosome Recycling factor" Selmer, M., Al-Karadaghi, S., Hirokawa, G., Kaji, A. and Liljas, A.Acta Cryst. D55:2049-2050 (1999).
Article: III "Crystal structure of Thermotoga maritima Ribosome recycling factor: a tRNA mimic" Selmer, M., Al-Karadaghi, S., Hirokawa, G., Kaji, A. and Liljas, A.Science 286:2349-2352 (1999)
Article: IV "Preparation of a crystallizable mRNA binding domain of Moorella thermoacetica elongation factor SelB" Selmer, M., Wilting, R., Holmlund, D. and Su, X-D.submitted
Article: V "Crystal structure of the mRNA binding domain of elongation factor SelB" Selmer, M. and Su, X-D.manuscript
Subject classification (UKÄ)
- Biological Sciences
Free keywords
- Molecular biophysics
- Molekylär biofysik
- crystallography
- mimicry
- translation factor
- L1
- SelB
- protein synthesis
- RRF