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CED-3 cleaves IFG-1 p170 at Aspartate 456.

By Vince Contreras (345152), Andrew J. Friday (345153), J. Kaitlin Morrison (345155), Enhui Hao (345156) and Brett D. Keiper (345157)

Abstract

<p>(A) Diagram of full length IFG-1 depicting the rCED-3 cleavage region between amino acids 420 and 686. No canonical caspase 3 recognition sites (DXXD) are present in this region. The positions of the non-canonical caspase cleavage sites (XXXD) are shown. (B) and (C) Aspartates 427 and 456 were mutated to alanines in the context of full length IFG-1 (1–1156). Radiolabeled IFG-1 (1–1156) was incubated with either (B) <i>C. elegans</i> rCED-3 or (C) human rCasp-3, resolved by SDS-PAGE, and visualized by phosphorimaging. The (*) indicates processed fragments and a carrot (<) represents the absence of a processed fragment. IFG-1 D456A was resistant to cleavage by rCED-3, and abolished one of the two cleavages by rCasp-3.</p

Topics: Biochemistry, Cell Biology, Physiology, cleaves, ifg-1, p170, aspartate
Year: 2013
DOI identifier: 10.1371/journal.pone.0024444.g005
OAI identifier: oai:figshare.com:article/411071
Provided by: FigShare
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