PMID:1962196

Citation	Tobias, JW, Shrader, TE, Rocap, G and Varshavsky, A (1991) The N-end rule in bacteria. Science 254:1374-7
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.
Links	PubMed
Keywords	Amino Acid Sequence; Animals; Bacteria/metabolism; Bacterial Proteins/metabolism; Escherichia coli/enzymology; Escherichia coli/metabolism; Half-Life; Kinetics; Molecular Sequence Data; Rabbits; Reticulocytes/metabolism; Saccharomyces cerevisiae/enzymology; Saccharomyces cerevisiae/metabolism; Structure-Activity Relationship; beta-Galactosidase/metabolism
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