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Figure 1

From: Arabidopsis thaliana PrimPol is a primase and lesion bypass DNA polymerase with the biochemical characteristics to cope with DNA damage in the nucleus, mitochondria, and chloroplast

Figure 1

AtPrimPol (AtPPol) is an active DNA polymerase and template-dependent primase with conserved AEP structural organization. (A) Domain organization of AtPrimPol in comparison to human PrimPol. The conserved motifs in the AEP and Zn++ finger subdomains and the N-terminal targeting sequence are indicated. (B) Primer synthesis by AtPPol using rNTPs. Ribonucleotide synthesis by AtPPol (200 and 400 nM) on ssDNA template containing the recognition sequence 5′-CCTG. Primer synthesis is observed by AtPPol, while the mutant lacking the Zf domain (AtPPolΔZf) and a mutant of the DXE polymerization motif (AtPPolΔpol) are unable to carry out primer synthesis. Primer synthesis starts with a 5′-pAG-3′ dinucleotide that is elongated to an oligonucleotides of 33 base pairs (5′-pAGGA(30)-3′). The process of template recognition, dimer synthesis, and primer extension by AtPrimPol is depicted as a cartoon. The cyan sphere represents the Zn++ finger domain and the magenta sphere the APE domain. (C) AtPrimPol is an active DNA polymerase. Primer extension reaction using three concentrations of wild-type and variants of AtPrimPol. Primer extension is observed for AtPPol, and the PrimPol ∆ZnF mutant whereas the mutant in the DXE polymerization motif is inactive. Original data used to compose this figure is present in Fig. S8.

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