Abstract
Escherichia coli can selectively degrade proteins with abnormal structures1–4. Certain mutant proteins are rapidly catabolized even though the normal gene products are stable3–5. Similarly, the incorporation of various amino-acid analogues or puromycin1,2 into cell proteins or frequent errors in translation2 lead to the rapid degradation of the resulting abnormal proteins. This degradation appears to involve a proteolytic mechanism distinct from that activated during starvation to provide starving cells with a source of amino-acids for protein synthesis6,7.
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PROUTY, W., GOLDBERG, A. Fate of Abnormal Proteins in E. coli Accumulation in Intracellular Granules before Catabolism. Nature New Biology 240, 147–150 (1972). https://doi.org/10.1038/newbio240147a0
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DOI: https://doi.org/10.1038/newbio240147a0
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