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Published on: October 4, 2018
Structural characterization of the ribosome maturation protein, RimM
Sakura Suzuki1, Ayako Tatsuguchi, Eiko Matsumoto
1RIKEN Genomic Sciences Center, Yokohama, Japan.
Abstract:
The RimM protein has been implicated in the maturation of the 30S ribosomal subunit. It binds to ribosomal protein S19, located in the head domain of the 30S subunit. Multiple sequence alignments predicted that RimM possesses two domains in its N- and C-terminal regions. In the present study, we have produced Thermus thermophilus RimM in both the full-length form (162 residues) and its N-terminal fragment, spanning residues 1 to 85, as soluble proteins in Escherichia coli and have performed structural analyses by nuclear magnetic resonance spectroscopy. Residues 1 to 80 of the RimM protein fold into a single structural domain adopting a six-stranded beta-barrel fold. On the other hand, the C-terminal region of RimM (residues 81 to 162) is partly folded in solution. Analyses of 1H-15N heteronuclear single quantum correlation spectra revealed that a wide range of residues in the C-terminal region, as well as the residues in the vicinity of a hydrophobic patch in the N-terminal domain, were dramatically affected upon complex formation with ribosomal protein S19.
Insights
The RimM protein, crucial for 30S ribosomal subunit maturation, features a stable N-terminal beta-barrel domain. Its interaction with ribosomal protein S19 significantly impacts both domains, influencing ribosome assembly.
Area of Science:
- Molecular Biology
- Structural Biology
- Biochemistry
Background:
- The RimM protein plays a role in the maturation of the 30S ribosomal subunit.
- RimM interacts with ribosomal protein S19, located in the 30S subunit's head domain.
- Sequence analysis suggests RimM has two domains: N-terminal and C-terminal.
Purpose of the Study:
- To characterize the structural properties of Thermus thermophilus RimM.
- To investigate the structural impact of RimM's interaction with ribosomal protein S19.
Main Methods:
- Production of full-length and N-terminal RimM fragments in Escherichia coli.
- Structural analysis using nuclear magnetic resonance (NMR) spectroscopy.
- Analysis of 1H-15N heteronuclear single quantum correlation spectra.
Main Results:
- The N-terminal region (residues 1-80) of RimM forms a stable six-stranded beta-barrel fold.
- The C-terminal region (residues 81-162) of RimM exhibits partial folding in solution.
- Complex formation with ribosomal protein S19 affected residues in the C-terminal region and a hydrophobic patch in the N-terminal domain.
Conclusions:
- Thermus thermophilus RimM possesses a well-defined N-terminal beta-barrel domain and a partially folded C-terminal domain.
- Ribosomal protein S19 binding induces significant conformational changes in both RimM domains, suggesting a role in regulating ribosome assembly.
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