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- W161459905 abstract "Pokeweed antiviral protein (PAP) is a single chain (type I) ribosome-inactivating protein (RIP), which depurinates ribosomes at the a-sarcin/ricin loop of the large rRNA, resulting in inhibition of translation. Unlike the type II RIPs, which have an active and a binding moiety, PAP has only the active moiety. The mechanism by which toxins without a binding moiety enter cells is not known. We recently showed that PAP enters the cytosol from the endoplasmic reticulum (ER) in yeast and exhibits unusual stability in the cytosol. Using a series of PAP mutants, we identified the signal for this retrotranslocation event. Our results demonstrate that processing of the C-terminal signal is critical for transport of the mature form into the cytosol. Sequential deletion of amino acids from the C-terminus led to a gradual reduction in retrotranslocation, which was lost upon deletion of the last 13 amino acids. Single mutations in this sequence delayed retrotranslocation, indicating that the C-terminal hydrophobic peptide is critical for ER export. This peptide showed sequence similarity to ribosome inactivating AB-toxins that retrotranslocate. This is the first demonstration that a conserved C-terminal sequence mediates retrotranslocation of a type I RIP and suggests that type I and type II RIPs may use a common signal to enter the cytosol. This work is supported by NSF MCB 0348299." @default.
- W161459905 created "2016-06-24" @default.
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- W161459905 date "2006-03-01" @default.
- W161459905 modified "2023-09-26" @default.
- W161459905 title "C‐terminal processing and C‐terminus of the mature pokeweed antiviral protein are required for its retrotranslocation from the ER to the cytosol" @default.
- W161459905 doi "https://doi.org/10.1096/fasebj.20.5.a1353-d" @default.
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