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New insights into the interaction of ribosomal protein L1 with RNA.
J Mol Biol. 2006 Jan 27; 355(4):747-59.JM

Abstract

The RNA-binding ability of ribosomal protein L1 is of profound interest, since L1 has a dual function as a ribosomal structural protein that binds rRNA and as a translational repressor that binds its own mRNA. Here, we report the crystal structure at 2.6 A resolution of ribosomal protein L1 from the bacterium Thermus thermophilus in complex with a 38 nt fragment of L1 mRNA from Methanoccocus vannielii. The conformation of RNA-bound T.thermophilus L1 differs dramatically from that of the isolated protein. Analysis of four copies of the L1-mRNA complex in the crystal has shown that domain II of the protein does not contribute to mRNA-specific binding. A detailed comparison of the protein-RNA interactions in the L1-mRNA and L1-rRNA complexes identified amino acid residues of L1 crucial for recognition of its specific targets on the both RNAs. Incorporation of the structure of bacterial L1 into a model of the Escherichia coli ribosome revealed two additional contact regions for L1 on the 23S rRNA that were not identified in previous ribosome models.

Authors+Show Affiliations

Institute of Protein Research, Russian Academy of Sciences, 142290 Pushchino, Moscow region, Russian Federation.No affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info available

Pub Type(s)

Journal Article
Research Support, N.I.H., Extramural
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

16330048

Citation

Nevskaya, Natalia, et al. "New Insights Into the Interaction of Ribosomal Protein L1 With RNA." Journal of Molecular Biology, vol. 355, no. 4, 2006, pp. 747-59.
Nevskaya N, Tishchenko S, Volchkov S, et al. New insights into the interaction of ribosomal protein L1 with RNA. J Mol Biol. 2006;355(4):747-59.
Nevskaya, N., Tishchenko, S., Volchkov, S., Kljashtorny, V., Nikonova, E., Nikonov, O., Nikulin, A., Köhrer, C., Piendl, W., Zimmermann, R., Stockley, P., Garber, M., & Nikonov, S. (2006). New insights into the interaction of ribosomal protein L1 with RNA. Journal of Molecular Biology, 355(4), 747-59.
Nevskaya N, et al. New Insights Into the Interaction of Ribosomal Protein L1 With RNA. J Mol Biol. 2006 Jan 27;355(4):747-59. PubMed PMID: 16330048.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - New insights into the interaction of ribosomal protein L1 with RNA. AU - Nevskaya,Natalia, AU - Tishchenko,Svetlana, AU - Volchkov,Sergey, AU - Kljashtorny,Vladislav, AU - Nikonova,Ekaterina, AU - Nikonov,Oleg, AU - Nikulin,Alexei, AU - Köhrer,Caroline, AU - Piendl,Wolfgang, AU - Zimmermann,Robert, AU - Stockley,Peter, AU - Garber,Maria, AU - Nikonov,Stanislav, Y1 - 2005/11/17/ PY - 2005/07/25/received PY - 2005/10/31/revised PY - 2005/10/31/accepted PY - 2005/12/7/pubmed PY - 2006/2/28/medline PY - 2005/12/7/entrez SP - 747 EP - 59 JF - Journal of molecular biology JO - J Mol Biol VL - 355 IS - 4 N2 - The RNA-binding ability of ribosomal protein L1 is of profound interest, since L1 has a dual function as a ribosomal structural protein that binds rRNA and as a translational repressor that binds its own mRNA. Here, we report the crystal structure at 2.6 A resolution of ribosomal protein L1 from the bacterium Thermus thermophilus in complex with a 38 nt fragment of L1 mRNA from Methanoccocus vannielii. The conformation of RNA-bound T.thermophilus L1 differs dramatically from that of the isolated protein. Analysis of four copies of the L1-mRNA complex in the crystal has shown that domain II of the protein does not contribute to mRNA-specific binding. A detailed comparison of the protein-RNA interactions in the L1-mRNA and L1-rRNA complexes identified amino acid residues of L1 crucial for recognition of its specific targets on the both RNAs. Incorporation of the structure of bacterial L1 into a model of the Escherichia coli ribosome revealed two additional contact regions for L1 on the 23S rRNA that were not identified in previous ribosome models. SN - 0022-2836 UR - https://www.unboundmedicine.com/medline/citation/16330048/New_insights_into_the_interaction_of_ribosomal_protein_L1_with_RNA_ DB - PRIME DP - Unbound Medicine ER -