Structural aspects for the function of ATP-binding ribonucleopeptide receptors.
We describe here analyses of the secondary structure of ATP-binding ribonucleopeptide (RNP) receptors. Mapping of the RNA structure of ATP-binding RNP receptors by using hydrolytic enzymes, chemical probing with dimethyl sulfate (DMS), and in-line probing indicated that ATP-binding RNP receptors take the loop structure at the nucleotide position of the "variable region". In addition, it was evident that a part of the consensus region located next to the variable region directly participated in the binding to ATP. The completely preserved three U nucleotides were essential for the binding of RNP to ATP as revealed by the affinity evaluation and the secondary structure analyses of the U nucleotides mutants of the ATP-binding RNP receptor. Interestingly, two mutants with an adenosine introduced to either of the two U nucleotides showed similar secondary structures to the original ATP-binding RNP. These results imply the possibility that the adenine base introduced at the U position acts just like the substrate ATP, and suggest that the U nucleotides in these positions interact directly to ATP.
Nakano
Shun
S
Graduate School of Energy Science, Kyoto University, Institute of Advanced Energy, Kyoto University, Uji, Kyoto 611-0011, Japan.
Fukuda
Masatora
M
Mashima
Tsukasa
T
Katahira
Masato
M
Morii
Takashi
T
D000225:Adenine / Q000737:chemistry; D000255:Adenosine Triphosphate / Q000032:analysis*; D009154:Mutation; D010455:Peptides / Q000737:chemistry; D012313:RNA / Q000737:chemistry*
D010455:Peptides; D012313:RNA; D000255:Adenosine Triphosphate; D000225:Adenine