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Science 29 November 1991:
Vol. 254. no. 5036, pp. 1374 - 1377
DOI: 10.1126/science.1962196
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Articles

Science, Vol 254, Issue 5036, 1374-1377
Copyright © 1991 by American Association for the Advancement of Science

articles

The N-end rule in bacteria

JW Tobias, TE Shrader, G Rocap, and A Varshavsky

Department of Biology, Massachusetts Institute of Technology, Cambridge 02139.

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.


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Proteases in Escherichia coli.
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   PDF »
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Science. ISSN 0036-8075 (print), 1095-9203 (online)