Ribosomal protein L1 recognizes the same specific structural motif in its target sites on the autoregulatory mRNA and 23S rRNA.
The RNA-binding ability of ribosomal protein L1 is of profound interest since the protein has a dual function as a ribosomal protein binding rRNA and as a translational repressor binding its mRNA. Here, we report the crystal structure of ribosomal protein L1 in complex with a specific fragment of its mRNA and compare it with the structure of L1 in complex with a specific fragment of 23S rRNA determined earlier. In both complexes, a strongly conserved RNA structural motif is involved in L1 binding through a conserved network of RNA-protein H-bonds inaccessible to the solvent. These interactions should be responsible for specific recognition between the protein and RNA. A large number of additional non-conserved RNA-protein H-bonds stabilizes both complexes. The added contribution of these non-conserved H-bonds makes the ribosomal complex much more stable than the regulatory one.
Nevskaya
Natalia
N
Institute of Protein Research, Russian Academy of Sciences 142290 Pushchino, Moscow region, Russia.
Tishchenko
Svetlana
S
Gabdoulkhakov
Azat
A
Nikonova
Ekaterina
E
Nikonov
Oleg
O
Nikulin
Alexei
A
Platonova
Olga
O
Garber
Maria
M
Nikonov
Stanislav
S
Piendl
Wolfgang
W
D001665:Binding Sites; D006706:Homeostasis; D008958:Models, Molecular; D009690:Nucleic Acid Conformation; D019642:RNA, Archaeal / Q000737:chemistry / Q000378:metabolism; D012333:RNA, Messenger / Q000737:chemistry* / Q000378:metabolism; D012338:RNA, Ribosomal, 23S / Q000737:chemistry* / Q000378:metabolism; D016601:RNA-Binding Proteins / Q000737:chemistry* / Q000378:metabolism; D012269:Ribosomal Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism
D019642:RNA, Archaeal; D012333:RNA, Messenger; D012338:RNA, Ribosomal, 23S; D016601:RNA-Binding Proteins; D012269:Ribosomal Proteins; C028546:ribosomal protein L1