Abstract
A NONSENSE mutation in a bacterial gene leads to the synthesis of two kinds of incomplete polypeptides1–4. These are the termination, or T, fragments extending from the normal N terminus to the site of mutation, and the reinitiation, or R, fragments initiating distal to the end of the T fragment and continuing to the normal C terminus. Both the T and the R fragments produced by nonsense mutations in the β-galactosidase gene of Escherichia coli (z gene) are rapidly and selectively degraded in vivo5–7. This contrasts strongly with the wild-type β-galactosidase, which is stable5,7. The degradation of mutant polypeptides implies the existence of proteolytic systems which can distinguish these unstable proteins from the stable ones.
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APTE, B., RHODES, H. & ZIPSER, D. Mutation blocking the specific degradation of reinitiation polypeptides in E. coli. Nature 257, 329–331 (1975). https://doi.org/10.1038/257329a0
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DOI: https://doi.org/10.1038/257329a0
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