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Significance During apoptosis, hundreds of intracellular proteins are cleaved by caspases. In addition to recognizing optimized motifs in the primary structure of its substrates, we show that caspase-7 possesses an exosite to enhance poly(ADP-ribose) polymerase 1 (PARP-1) recognition via the mutual binding of RNA. We also demonstrate that caspase-7 binds RNA and that PARP-1, via 2 RNA-binding domains, likely binds the same RNA molecule, bringing itself near caspase-7 for prompt inactivation. This mechanism is conserved in the mouse ortholog. We have also validated the use of RNA for the efficient cleavage of 6 other RNA-BPs, demonstrating that this distinctive mode of proteolysis enhancement by caspase-7 is an essential feature of substrate recognition during apoptosis.

Caspase-7 uses RNA to enhance proteolysis of poly(ADP-ribose) polymerase 1 and other RNA-binding proteins