title: New insights into the interaction of ribosomal protein L1 with RNA.
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.affiliation: Institute of Protein Research, Russian Academy of Sciences, 142290 Pushchino, Moscow region, Russian Federation.
authors.forename: Natalia
authors.initials: N
authors.lastname: Nevskaya
authors.forename: Svetlana
authors.initials: S
authors.lastname: Tishchenko
authors.forename: Sergey
authors.initials: S
authors.lastname: Volchkov
authors.forename: Vladislav
authors.initials: V
authors.lastname: Kljashtorny
authors.forename: Ekaterina
authors.initials: E
authors.lastname: Nikonova
authors.forename: Oleg
authors.initials: O
authors.lastname: Nikonov
authors.forename: Alexei
authors.initials: A
authors.lastname: Nikulin
authors.forename: Caroline
authors.initials: C
authors.lastname: Köhrer
authors.forename: Wolfgang
authors.initials: W
authors.lastname: Piendl
authors.forename: Robert
authors.initials: R
authors.lastname: Zimmermann
authors.forename: Peter
authors.initials: P
authors.lastname: Stockley
authors.forename: Maria
authors.initials: M
authors.lastname: Garber
authors.forename: Stanislav
authors.initials: S
authors.lastname: Nikonov
mesh_terms: D000595:Amino Acid Sequence; D006860:Hydrogen Bonding; D007700:Kinetics; D017017:Methanococcus / Q000235:genetics; D008969:Molecular Sequence Data; D009690:Nucleic Acid Conformation; D011485:Protein Binding; D017434:Protein Structure, Tertiary; D012329:RNA, Bacterial / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D012333:RNA, Messenger / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D012335:RNA, Ribosomal / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D012269:Ribosomal Proteins / Q000737:chemistry* / Q000378:metabolism*; D016415:Sequence Alignment; D020349:Surface Plasmon Resonance; D016963:Thermus thermophilus
chemical_list: D012329:RNA, Bacterial; D012333:RNA, Messenger; D012335:RNA, Ribosomal; D012269:Ribosomal Proteins; C028546:ribosomal protein L1