期刊
MOLECULAR BIOSYSTEMS
卷 11, 期 9, 页码 2441-2448出版社
ROYAL SOC CHEMISTRY
DOI: 10.1039/c5mb00184f
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资金
- Japan Society for the Promotion of Science (JSPS) [24750166]
- Grants-in-Aid for Scientific Research [25249115, 24000011, 24750166] Funding Source: KAKEN
Y-box binding protein 1 (YB-1) binds to both RNA and DNA to control transcription and translation for the regulation of various cellular systems. YB-1 is overexpressed in some cancer cells and is a potential target for treatment of cancer. Herein, we describe isothermal titration calorimetry analyses of the interaction between a number of recombinant YB-1 domains and nucleic acids to identify the RNA and DNA binding sites and their binding mechanisms. These results demonstrated that the C-terminal domain of the protein interacts with single-stranded DNA and RNA by exothermic and endothermic reactions, respectively. The highly conserved cold-shock domain (CSD) also bound to single-stranded RNA and DNA by exothermic and endothermic reactions, respectively. The specific binding manner for RNA is in the CSD, whereas DNA binds with the most affinity to the C-terminal region (amino acids 130-219). We found further that the C-terminal region (amino acids 220-324) regulates the binding stoichiometry of RNA. These quantitative thermodynamic results provide a preliminary indication on the molecular mechanism of binding of the multifunctional protein YB-1 to nucleic acids to regulate its biological function.
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