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Fig. 1 | Epigenetics & Chromatin

Fig. 1

From: Independent functions of DNMT1 and USP7 at replication foci

Fig. 1

Cell-cycle independent expression of DNMT1 and the characteristics of the (GK) repeats in DNMT1. a Pulse labeling of cycling mouse 3T3 cell with BrdU followed by fixation and staining with antibodies to BrdU and DNMT1 shows that DNMT1 is present in non-S phase cells (identified by lack of BrdU staining) at levels comparable to S phase cells as previously reported [30]. b Domain organization of mammalian DNMT1. NLS: nuclear localization sequence. RFTS: replication focus targeting sequence. CXXC: Zinc-containing domain that binds to unmethylated CpG sites in double stranded DNA. Autoinhibitory: An acidic linker interposed between DNA and the active site of DNMT1 when the CXXC domain is bound to unmethylated DNA. BAH1 and 2: Bromo-adjacent homology domains that are of unknown function in DNMT1 but are involved in binding to specific histone modifications in other proteins. (GK): The run of alternating glycine and lysine amino acids at the junction between the N-terminal regulatory and C-terminal catalytic domains of DNMT1. Methyltransferase domain: Catalytic domain related in sequence and structure to eukaryotic and prokaryotic DNA (cytosine-5) methyltransferases. c Alignment of (GK) repeats of DNMT1 homologs from mammals, insects, and plants, and with the N-terminal tails of histones H2A, H2AZ, and H4. GK dipeptides are outlined in red; the related AK dipeptides are outlined in blue. d Structure of autoinhibited form of human DNMT1 in complex with unmethylated DNA to show spatial relationships of domains diagrammed in (b). The protein shown was truncated just N-terminal of the CXXC domain prior to crystallization. The (GK) repeats were unstructured in all the crystallographic studies of DNMT1; they are shown here roughly to scale in an arbitrary position

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