期刊
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY
卷 133, 期 12, 页码 4567-4579出版社
AMER CHEMICAL SOC
DOI: 10.1021/ja110725d
关键词
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资金
- Ministry of Education, Culture, Sports, Science and Technology, Japan [20241051, 22121510]
- MEXT [21370047, 22121517]
- JST-SENTAN
- Naito Foundation
- YCU-AMRC
- CPLCEP-IAE-KU
- Grants-in-Aid for Scientific Research [23657072, 21370047, 22121517, 20241051, 22121510] Funding Source: KAKEN
A modular structure of ribonucleopeptide (RNP) affords a framework to construct macromolecular receptors and fluorescent sensors. We have isolated ATP-binding RNP with the minimum of nucleotides for ATP binding, in which the RNA consensus sequence is different from those reported for RNA aptamers against the ATP analogues. The three-dimensional structure of the substrate-binding complex of RNP was studied to understand the ATP-binding mechanism of RNP. A combination of NMR measurements, enzymatic and chemical mapping, and nucleotide mutation studies of the RNP-adenosine complex show that MP interacts with the adenine ring of adenosine by forming a U:A:U triple with two invariant U nucleotides. The observed recognition mode for the adenine ring is different from those of RNA aptamers for ATP derivatives reported previously. The RNP-adenosine complex is folded into a particular structure by formation of the U:A:U triple and a Hoogsteen type A:U base pair. This recognition mechanism was successfully utilized to convert the substrate-binding specificity of RNP from ATP- to GTP-binding with a C :G:C triple recognition mode.
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