期刊
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY
卷 133, 期 12, 页码 4196-4199出版社
AMER CHEMICAL SOC
DOI: 10.1021/ja110411m
关键词
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资金
- NIH [RR012255]
- NSF [PHY0216576]
Riboswitches are cis-acting RNA fragments that regulate gene expression by sensing cellular levels of the associated small metabolites. In bacteria, the class I preQ(1) riboswitch allows the fine-tuning of queuosine biosynthesis in response to the intracellular concentration of the queuosine anabolic intermediate preQ(1). When binding preQ(1) the aptamer domain undergoes a significant degree of secondary and tertiary structural rearrangement and folds into an H-type pseudoknot. Conformational switching of the riboswitch aptamer domain upon recognizing its cognate metabolite plays a key role in the regulatory mechanism of the preQ(1) riboswitch. We investigate the folding mechanism of the preQ(1) riboswitch aptamer domain using all-atom G (o) over bar -model simulations. The folding pathway of such a single domain is found to be cooperative and sequentially coordinated, as the folding proceeds in the 5' -> 3' direction. This kinetically efficient folding mechanism suggests a fast ligand-binding response in competition with RNA elongation.
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