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Detailed analysis of RNA-protein interactions within the bacterial ribosomal protein L5/5S rRNA complex.
RNA. 2002 Dec; 8(12):1548-57.RNA

Abstract

The crystal structure of ribosomal protein L5 from Thermus thermophilus complexed with a 34-nt fragment comprising helix III and loop C of Escherichia coli 5S rRNA has been determined at 2.5 A resolution. The protein specifically interacts with the bulged nucleotides at the top of loop C of 5S rRNA. The rRNA and protein contact surfaces are strongly stabilized by intramolecular interactions. Charged and polar atoms forming the network of conserved intermolecular hydrogen bonds are located in two narrow planar parallel layers belonging to the protein and rRNA, respectively. The regions, including these atoms conserved in Bacteria and Archaea, can be considered an RNA-protein recognition module. Comparison of the T. thermophilus L5 structure in the RNA-bound form with the isolated Bacillus stearothermophilus L5 structure shows that the RNA-recognition module on the protein surface does not undergo significant changes upon RNA binding. In the crystal of the complex, the protein interacts with another RNA molecule in the asymmetric unit through the beta-sheet concave surface. This protein/RNA interface simulates the interaction of L5 with 23S rRNA observed in the Haloarcula marismortui 50S ribosomal subunit.

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Authors+Show Affiliations

Perederina A
Institute of Protein Research, Russian Academy of Sciences, 142290 Pushchino, Moscow region, Russia.
Nevskaya N
No affiliation info available
Nikonov O
No affiliation info available
Nikulin A
No affiliation info available
Dumas P
No affiliation info available
Yao M
No affiliation info available
Tanaka I
No affiliation info available
Garber M
No affiliation info available
Gongadze G
No affiliation info available
Nikonov S
No affiliation info available

MeSH

Amino Acid SequenceBacterial ProteinsBase SequenceBinding SitesEscherichia coliHydrogen BondingModels, MolecularMolecular Sequence DataNucleic Acid ConformationPeptide FragmentsProtein ConformationRNA, Ribosomal, 5SRibosomal Proteins

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

12515387

Citation

Perederina, Anna, et al. "Detailed Analysis of RNA-protein Interactions Within the Bacterial Ribosomal Protein L5/5S rRNA Complex." RNA (New York, N.Y.), vol. 8, no. 12, 2002, pp. 1548-57.
Perederina A, Nevskaya N, Nikonov O, et al. Detailed analysis of RNA-protein interactions within the bacterial ribosomal protein L5/5S rRNA complex. RNA. 2002;8(12):1548-57.
Perederina, A., Nevskaya, N., Nikonov, O., Nikulin, A., Dumas, P., Yao, M., Tanaka, I., Garber, M., Gongadze, G., & Nikonov, S. (2002). Detailed analysis of RNA-protein interactions within the bacterial ribosomal protein L5/5S rRNA complex. RNA (New York, N.Y.), 8(12), 1548-57.
Perederina A, et al. Detailed Analysis of RNA-protein Interactions Within the Bacterial Ribosomal Protein L5/5S rRNA Complex. RNA. 2002;8(12):1548-57. PubMed PMID: 12515387.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Detailed analysis of RNA-protein interactions within the bacterial ribosomal protein L5/5S rRNA complex. AU - Perederina,Anna, AU - Nevskaya,Natalia, AU - Nikonov,Oleg, AU - Nikulin,Alexei, AU - Dumas,Philippe, AU - Yao,Min, AU - Tanaka,Isao, AU - Garber,Maria, AU - Gongadze,George, AU - Nikonov,Stanislav, PY - 2003/1/8/pubmed PY - 2003/1/28/medline PY - 2003/1/8/entrez SP - 1548 EP - 57 JF - RNA (New York, N.Y.) JO - RNA VL - 8 IS - 12 N2 - The crystal structure of ribosomal protein L5 from Thermus thermophilus complexed with a 34-nt fragment comprising helix III and loop C of Escherichia coli 5S rRNA has been determined at 2.5 A resolution. The protein specifically interacts with the bulged nucleotides at the top of loop C of 5S rRNA. The rRNA and protein contact surfaces are strongly stabilized by intramolecular interactions. Charged and polar atoms forming the network of conserved intermolecular hydrogen bonds are located in two narrow planar parallel layers belonging to the protein and rRNA, respectively. The regions, including these atoms conserved in Bacteria and Archaea, can be considered an RNA-protein recognition module. Comparison of the T. thermophilus L5 structure in the RNA-bound form with the isolated Bacillus stearothermophilus L5 structure shows that the RNA-recognition module on the protein surface does not undergo significant changes upon RNA binding. In the crystal of the complex, the protein interacts with another RNA molecule in the asymmetric unit through the beta-sheet concave surface. This protein/RNA interface simulates the interaction of L5 with 23S rRNA observed in the Haloarcula marismortui 50S ribosomal subunit. SN - 1355-8382 UR - https://www.unboundmedicine.com/medline/citation/12515387/Detailed_analysis_of_RNA_protein_interactions_within_the_bacterial_ribosomal_protein_L5/5S_rRNA_complex_ DB - PRIME DP - Unbound Medicine ER -