Abstract

The N-end rule relates the in vivo half-life of a protein to the identity of its amino-terminal residue. Distinct versions of the N-end rule operate in all eukaryotes examined. It is shown that the bacterium Escherichia coli also has the N-end rule pathway. Amino-terminal arginine, lysine, leucine, phenylalanine, tyrosine, and tryptophan confer 2-minute half-lives on a test protein; the other amino-terminal residues confer greater than 10-hour half-lives on the same protein. Amino-terminal arginine and lysine are secondary destabilizing residues in E. coli because their activity depends on their conjugation to the primary destabilizing residues leucine or phenylalanine by leucine, phenylalanine-transfer RNA-protein transferase. The adenosine triphosphate-dependent protease Clp (Ti) is required for the degradation of N-end rule substrates in E. coli .

Keywords

PhenylalanineLeucineBiochemistryAmino acidArginineEscherichia coliTyrosineLysineTryptophanChemistryBiologyGene

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Publication Info

Year
1991
Type
article
Volume
254
Issue
5036
Pages
1374-1377
Citations
538
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Closed

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John W. Tobias, Thomas E. Shrader, Gabrielle Rocap et al. (1991). The N-End Rule in Bacteria. Science , 254 (5036) , 1374-1377. https://doi.org/10.1126/science.1962196

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DOI
10.1126/science.1962196