Analysis of the nucleotide context of <Emphasis Type="Italic">Arabidopsis thaliana</Emphasis> mitochondrial mRNA editing sites |
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Authors: | O V Vishnevsky I I Titov Yu M Konstantinov |
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Institution: | (1) Institute of Protein Research, Pushchino, Moscow oblast, 142290, Russia;(2) Belozersky Institute of Physicochemical Biology and Faculty of Chemistry, Moscow State University, Vorob’evy gory, Moscow, 119899, Russia;(3) Bach Institute of Biochemistry, Russian Academy of Sciences, Leninskii pr. 33, Moscow, 119071, Russia;(4) Institute of Agricultural Biotechnology, Russian Academy of Agricultural Sciences, Moscow, 127550, Russia;(5) Institute of Molecular Biology and Biophysics, Siberian Division, Russian Academy of Medical Sciences, Novosibirsk, 630117, Russia;(6) Physics Laboratory, Kansai Medical University Uyamahigashi, Hirakata Osaka 573-1136, Japan;(7) Department of Biochemistry, Dokkyo University, Mibu, Tochigi 321-0200, Japan |
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Abstract: | The structure of native and modified uracil-DNA glycosylase from E. coli in solution was studied by synchrotron small-angle X-ray scattering. The modified enzyme (6His-uracil glycosylase) differs from the native one by the presence of an additional N-terminal 11-meric sequence of amino acid residues, including a block of six His residues. In contrast to minimal differences in the amino acid sequences and functional activity, conformations of native and 6His-uracil glycosylases in solution were found to differ substantially at moderate ionic strength (60 mM NaCl). The structure of uracil-DNA glycosylase in solution is close to that in crystal and shows a tendency toward association. The interaction of this enzyme with nonhydrolyzable analogues of DNA ligands causes partial dissociation of associates and compaction of protein structure. At the same time, 6His-uracil DNA glycosylase has a compact structure, intrinsically different from that in crystals. A decrease in the ionic strength of solution results in a partial destruction of the compact structure of the modified protein, keeping its functional activity unchanged. |
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Keywords: | uracil-DNA glycosylase synchrotron small-angle X-ray scattering DNA-protein interaction |
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