PMID:16330048
| Citation |
Nevskaya, N, Tishchenko, S, Volchkov, S, Kljashtorny, V, Nikonova, E, Nikonov, O, Nikulin, A, Köhrer, C, Piendl, W, Zimmermann, R, Stockley, P, Garber, M and Nikonov, S (2006) New insights into the interaction of ribosomal protein L1 with RNA. J. Mol. Biol. 355:747-59 |
|---|---|
| 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. |
| Links |
PubMed Online version:10.1016/j.jmb.2005.10.084 |
| Keywords |
Amino Acid Sequence; Hydrogen Bonding; Kinetics; Methanococcus/genetics; Molecular Sequence Data; Nucleic Acid Conformation; Protein Binding; Protein Structure, Tertiary; RNA, Bacterial/chemistry; RNA, Bacterial/genetics; RNA, Bacterial/metabolism; RNA, Messenger/chemistry; RNA, Messenger/genetics; RNA, Messenger/metabolism; RNA, Ribosomal/chemistry; RNA, Ribosomal/genetics; RNA, Ribosomal/metabolism; Ribosomal Proteins/chemistry; Ribosomal Proteins/metabolism; Sequence Alignment; Surface Plasmon Resonance; Thermus thermophilus |
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