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Substrate binding specificity of Mth212/D151N

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posted on 30.12.2011, 16:43 by Jens Georg, Lars Schomacher, James P. J. Chong, Alan I. Majerník, Monika Raabe, Henning Urlaub, Sabine Müller, Elena Ciirdaeva, Wilfried Kramer, Hans-Joachim Fritz

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Taken from "The ExoIII homologue Mth212 is a DNA uridine endonuclease"

Nucleic Acids Research 2006;34(18):5325-5336.

Published online 29 Sep 2006

PMCID:PMC1636421.

© 2006 The Author(s)

Electrophoretic mobility shift assays with Mth212/D151N and double-stranded oligonucleotides containing either an apyrimidinic site analog (AP, see ) opposite G () or a normal C/G base pair () were carried out as described in Materials and Methods. Mobilities of free substrates are shown in the leftmost lanes (AP/G and C/G, respectively). Amounts of competitor DNA are indicated as nucleotide equivalents relative to substrate oligonucleotides (Competitor was pET_B_001 with 5.4 kb). Positions of bands corresponding to competitor DNA, protein/substrate complexes and free dsDNA are indicated in the left margin.

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