Abstract
ATP-dependent Lon protease of E. coli (Ec-Lon) is a key enzyme of the quality control system of the cell proteome. The Ec-Lon subunit comprises N-terminal non-catalytic region, ATPase module and proteolytic domain (serine–lysine endopeptidase). A distinctive feature of the Ec-Lon is its ability to interact with DNA, however either DNA binding site(s) or the role of the complex Ec-Lon/DNA have not yet been characterized. Aptamers, small nucleic acids with high specificity to organic compounds of different natures, are known to be a promising tool for the study of molecular mechanisms of interaction between nucleic acids and protein ligands. Ec-Lon protease was found to form complexes with the previously obtained thrombin aptamers whose molecules comprise the duplex domains and G-quadruplex region. The aptamer affinities to the enzyme have been characterized. The synthesis of novel aptamers specific to Ec-Lon protease is planned for studying the mechanism of the enzyme-DNA complexation.
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Abbreviations
- Apt:
-
aptamer
- NA:
-
is nucleic acid
- CCM:
-
chemical cleavage of mismatch
- SELEX:
-
systematic evolution of ligands by exponential enrichment
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Original Russian Text © V.A. Spiridonova, A.M. Kudzhaev, A.V. Melnichuk, A.A. Gainutdinov, A.G. Andrianova, T.V. Rotanova, 2015, published in Bioorganicheskaya Khimiya, 2015, Vol. 41, No. 6, pp. 696–700.
The article has been adapted from the report presented at the VIIth All-Russian symposium “Proteins and Peptides”, Novosibirsk, 12–17 July, 2015.
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Spiridonova, V.A., Kudzhaev, A.M., Melnichuk, A.V. et al. Interaction of DNA aptamers with the ATP-dependent lon protease from Escherichia coli . Russ J Bioorg Chem 41, 626–630 (2015). https://doi.org/10.1134/S1068162015060151
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DOI: https://doi.org/10.1134/S1068162015060151