Fig. 1: Structure and purification of DNMT3C catalytic domain proteins. | Communications Biology

Fig. 1: Structure and purification of DNMT3C catalytic domain proteins.

From: Specific DNMT3C flanking sequence preferences facilitate methylation of young murine retrotransposons

Fig. 1

a Domain composition of different DNMT3 enzymes. The murine DNMT3C protein (Uniprot entry P0DOY1) consists of 740 amino acids. See also Supplementary Fig. 1. b Structure of the heterotetrameric complex of DNMT3B catalytic domain and DNMT3L C-terminal domain19. DNMT3B is shown in orange and brown, DNMT3L in grey. Residues differing in DNMT3C and DNMT3B are colored pink in the orange DNMT3B subunit. DNA is shown in blue with the -1 flank base pair in cyan and the -2 flank base pair in yellow. c Purification of WT DNMT3C catalytic domain and mutants. Lane 1: WT DNMT3C, lane 2: C543N/V547A mutant, lane 3: C543N mutant, lane 4: V547A mutant, lane 5: E590K mutant. M: Protein size marker. d Zoom into the DNMT3B/3L structure focusing on the -2 and -1 flank region. Coloring is as described in panel (b). N656 (corresponding to C543 in DNMT3C), A660 (V547 in DNMT3C) and K703 (E590 in DNMT3C) are highlighted. There are no other amino acids differences between DNMT3C and DNMT3B near the DNA at the -2/-1 flank region.

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