Structural and biochemical analyses of hemimethylated DNA binding by t
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《核酸研究医学期刊》
Nucleic Acids Res. (2004) 32, 82–92
The authors would like to apologise for an error that appears in Figure 1D. The lane 3 label should read GmATG not GmACG. Please find herewith the corrected version of Figure 1. This change does not affect the Discussion or Conclusions.
Figure 1. SeqA71–181–DNA binding analyses. (A) The hemimethylated G-mA-T-C 14mer DNA used in the DNA binding analysis. The region corresponding to the hemimethylated G-mA-T-C 10mer DNA used in the crystallization of the SeqA71–181–DNA complex is colored, and is numbered. The recognition sequence of SeqA is colored blue in the box, and the hemimethylated mA:T base pair is colored red. ‘Me’ indicates the N6-methyl group. Numbers without asterisks indicate base positions from the 5' end of the methylated strand, and numbers with asterisks indicate base positions from the 3' end of the unmethylated strand. (B–D) Effect of base pair replacements at the G4:C4* (B), T6:A6* (C) and C7:G7* (D) base pairs. Replaced base pairs are indicated by white letters on the top of each panel. Lane 1 is a negative control experiment without protein, and lane 2 is a positive control. (E) Effect of mismatch replacements at the mA5:T5* position on the DNA binding. Lane 1 is a negative control experiment without protein, and lane 2 is a positive control. The T5* residue was replaced by G (lane 3), A (lane 4) and C (lane 5). Graphic representations of the DNA binding of the SeqA71–181 mutants are presented in the bottom panels (B–E). The amounts of complex formation relative to that accomplished by the wild-type SeqA71–181 protein are presented. Average and SD values from three independent experiments are presented.(Norie Fujikawa, Hitoshi Kurumizaka, Osam)
The authors would like to apologise for an error that appears in Figure 1D. The lane 3 label should read GmATG not GmACG. Please find herewith the corrected version of Figure 1. This change does not affect the Discussion or Conclusions.
Figure 1. SeqA71–181–DNA binding analyses. (A) The hemimethylated G-mA-T-C 14mer DNA used in the DNA binding analysis. The region corresponding to the hemimethylated G-mA-T-C 10mer DNA used in the crystallization of the SeqA71–181–DNA complex is colored, and is numbered. The recognition sequence of SeqA is colored blue in the box, and the hemimethylated mA:T base pair is colored red. ‘Me’ indicates the N6-methyl group. Numbers without asterisks indicate base positions from the 5' end of the methylated strand, and numbers with asterisks indicate base positions from the 3' end of the unmethylated strand. (B–D) Effect of base pair replacements at the G4:C4* (B), T6:A6* (C) and C7:G7* (D) base pairs. Replaced base pairs are indicated by white letters on the top of each panel. Lane 1 is a negative control experiment without protein, and lane 2 is a positive control. (E) Effect of mismatch replacements at the mA5:T5* position on the DNA binding. Lane 1 is a negative control experiment without protein, and lane 2 is a positive control. The T5* residue was replaced by G (lane 3), A (lane 4) and C (lane 5). Graphic representations of the DNA binding of the SeqA71–181 mutants are presented in the bottom panels (B–E). The amounts of complex formation relative to that accomplished by the wild-type SeqA71–181 protein are presented. Average and SD values from three independent experiments are presented.(Norie Fujikawa, Hitoshi Kurumizaka, Osam)