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• W2051107122 abstract "In order to investigate whether the 2-amino group of guanine, which lies in the minor groove of theB-form helix, can directly influence DNA flexibility and major groove rcognition by proteins we have examined the properties of DNA molecules containing inosine and/or 2,6-diaminopurine (DAP) residues. Appropriately substitutedtyrT(A93) DNA fragments were prepared by the polymerase chain reaction. Their mobility in non-denaturing gels was affected, consistent with changed anisotropic flexibility leading to increased curvature due to G→I substitution and decreased curvature due to replacement of adenine with DAP. Band-shift assays of FIS protein binding revealed facilitated interaction with inosine-containing DNA and markedly reduced binding to DAP-containing DNA, attributable to altered bendability. DNase footprinting experiments confirmed that fewer sites would bind FIS in DAP-containing DNA at a given protein concentration, whereas higher levels of binding occurred with inosine-containing molecules. Thus base substitutions which affect the placement and presence of the purine 2-amino group in the mirror groove can affect both the intrinsic curvature and the bendability of DNA." @default.
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• W2051107122 date "1995-10-01" @default.
• W2051107122 modified "2023-10-11" @default.
• W2051107122 title "Effects of Base Substitutions on the Binding of a DNA-bending Protein" @default.
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• W2051107122 doi "https://doi.org/10.1006/jmbi.1995.0530" @default.
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