New insights into the interaction of ribosomal protein L1 with RNA.
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.
Nevskaya
Natalia
N
Institute of Protein Research, Russian Academy of Sciences, 142290 Pushchino, Moscow region, Russian Federation.
Tishchenko
Svetlana
S
Volchkov
Sergey
S
Kljashtorny
Vladislav
V
Nikonova
Ekaterina
E
Nikonov
Oleg
O
Nikulin
Alexei
A
Köhrer
Caroline
C
Piendl
Wolfgang
W
Zimmermann
Robert
R
Stockley
Peter
P
Garber
Maria
M
Nikonov
Stanislav
S
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
D012329:RNA, Bacterial; D012333:RNA, Messenger; D012335:RNA, Ribosomal; D012269:Ribosomal Proteins; C028546:ribosomal protein L1