Figure 6 | Cell Discovery

Figure 6

From: Transcriptome-wide identification of the RNA-binding landscape of the chromatin-associated protein PARP1 reveals functions in RNA biogenesis

Figure 6

PARP1–RNA domain interactions. (a) Schematic structure of PARP1 showing the various functional domains important in PARP1 activation, localization, and activity. The first three N-terminal domains (residues 1–353) are zinc-finger DNA-binding domains with distinct functions in PARP1 DNA nick-mediated activation. The central, auto-modification region of PARP1 contains a BRCT domain (residues 389–487), as well as flanking residues that serve as sites of auto-ADP ribosylation. Adjacent to the BRCT domain is a WGR domain (residues 518–643) followed by the catalytic domain (residues 662–1 014), which possesses activities related to the ADP-ribose adduct formation, elongation, and branching activity. Below are the various PARP1 constructs created to test the RNA-binding activity of PARP1. (b) Coomassie gel staining of purified recombinant full-length PARP1 and the truncated PARP1 proteins. (c) Western blot analysis of PARP1 and truncated PARP1 proteins. (d) Gel shift assays showing the binding of RNA by various proteins, PARP1 full-length, and truncations.

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