alpha-Sarcin catalytic activity is not required for cytotoxicity |
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| Authors: | Spencer C Alford Joel D Pearson Amanda Carette Robert J Ingham Perry L Howard |
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| Institution: | (1) Centre for Biomedical Research, University of Victoria, PO Box 3020, Station CSC Victoria, British Columbia, V8W 3N5, Canada;(2) Department of Biochemistry and Microbiology, University of Victoria, PO Box 3055, Station CSC Victoria, British Columbia, V8W 3P6, Canada;(3) Department of Biology, University of Victoria, PO Box 3020, Station CSC Victoria, British Columbia, V8W 3N5, Canada;(4) Department of Medical Microbiology and Immunology, University of Alberta, Edmonton, Alberta, T6G 2H7, Canada |
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| Abstract: | Background α-Sarcin is a protein toxin produced by Aspergillus giganteus. It belongs to a family of cytotoxic ribonucleases that inactivate the ribosome and inhibit protein synthesis. α-Sarcin cleaves
a single phosphodiester bond within the RNA backbone of the large ribosomal subunit, which makes the ribosome unrecognizable
to elongation factors and, in turn, blocks protein synthesis. Although it is widely held that the protein synthesis inhibition
caused by the toxin leads to cell death, it has not been directly shown that catalytically inactive mutants of α-sarcin are
non-toxic when expressed directly within the cytoplasm of cells. This is important since recent studies have cast doubt on
whether protein synthesis inhibition is sufficient to initiate apoptosis. |
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