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Science 10 October 1986:
Vol. 234. no. 4773, pp. 179 - 186
DOI: 10.1126/science.3018930
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Articles

Science, Vol 234, Issue 4773, 179-186
Copyright © 1986 by American Association for the Advancement of Science

articles

In vivo half-life of a protein is a function of its amino-terminal residue

A Bachmair, D Finley, and A Varshavsky

When a chimeric gene encoding a ubiquitin-beta-galactosidase fusion protein is expressed in the yeast Saccharomyces cerevisiae, ubiquitin is cleaved off the nascent fusion protein, yielding a deubiquitinated beta-galactosidase (beta gal). With one exception, this cleavage takes place regardless of the nature of the amino acid residue of beta gal at the ubiquitin-beta gal junction, thereby making it possible to expose different residues at the amino-termini of the otherwise identical beta gal proteins. The beta gal proteins thus designed have strikingly different half-lives in vivo, from more than 20 hours to less than 3 minutes, depending on the nature of the amino acid at the amino-terminus of beta gal. The set of individual amino acids can thus be ordered with respect to the half-lives that they confer on beta gal when present at its amino-terminus (the "N-end rule"). The currently known amino-terminal residues in long-lived, noncompartmentalized intracellular proteins from both prokaryotes and eukaryotes belong exclusively to the stabilizing class as predicted by the N-end rule. The function of the previously described posttranslational addition of single amino acids to protein amino-termini may also be accounted for by the N-end rule. Thus the recognition of an amino-terminal residue in a protein may mediate both the metabolic stability of the protein and the potential for regulation of its stability.


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Mol. Cell. Biol. 21, 8007-8021
   Abstract »    Full Text »    PDF »
Kinetic Analysis of the Conjugation of Ubiquitin to Picornavirus 3C Proteases Catalyzed by the Mammalian Ubiquitin-protein Ligase E3alpha.
T. G. Lawson, M. E. Sweep, P. E. Schlax, R. N. Bohnsack, and A. L. Haas (2001)
J. Biol. Chem. 276, 39629-39637
   Abstract »    Full Text »    PDF »
N-end Rule Specificity within the Ubiquitin/Proteasome Pathway Is Not an Affinity Effect.
O. V. Baboshina, R. Crinelli, T. J. Siepmann, and A. L. Haas (2001)
J. Biol. Chem. 276, 39428-39437
   Abstract »    Full Text »    PDF »
Two-hybrid analysis of the Saccharomyces cerevisiae 26S proteasome.
G. CAGNEY, P. UETZ, and S. FIELDS (2001)
Physiol Genomics 7, 27-34
   Abstract »    Full Text »    PDF »
Upc2p and Ecm22p, Dual Regulators of Sterol Biosynthesis in Saccharomyces cerevisiae.
A. Vik and J. Rine (2001)
Mol. Cell. Biol. 21, 6395-6405
   Abstract »    Full Text »    PDF »
Xylulokinase Overexpression in Two Strains of Saccharomyces cerevisiae Also Expressing Xylose Reductase and Xylitol Dehydrogenase and Its Effect on Fermentation of Xylose and Lignocellulosic Hydrolysate.
B. Johansson, C. Christensson, T. Hobley, and B. Hahn-Hagerdal (2001)
Appl. Envir. Microbiol. 67, 4249-4255
   Abstract »    Full Text »    PDF »
Sequence Architecture Downstream of the Initiator Codon Enhances Gene Expression and Protein Stability in Plants.
S. V. Sawant, K. Kiran, P. K. Singh, and R. Tuli (2001)
Plant Physiology 126, 1630-1636
   Abstract »    Full Text »    PDF »
Reconstruction of Ligand-Dependent Transactivation of Choristoneura fumiferana Ecdysone Receptor in Yeast.
H. T. Tran, H. B. Askari, S. Shaaban, L. Price, S. R. Palli, T. S. Dhadialla, G. R. Carlson, and T. R. Butt (2001)
Mol. Endocrinol. 15, 1140-1153
   Abstract »    Full Text »    PDF »
Degradation Signals Recognized by the Ubc6p-Ubc7p Ubiquitin-Conjugating Enzyme Pair.
T. Gilon, O. Chomsky, and R. G. Kulka (2000)
Mol. Cell. Biol. 20, 7214-7219
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The Doa4 Deubiquitinating Enzyme Is Functionally Linked to the Vacuolar Protein-sorting and Endocytic Pathways.
A. Y. Amerik, J. Nowak, S. Swaminathan, and M. Hochstrasser (2000)
Mol. Biol. Cell 11, 3365-3380
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Detecting and Measuring Cotranslational Protein Degradation in.
G. Turner and Varshavsky (2000)
Science 289, 2117-2120
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Varying Intertrial Interval Reveals Temporally Defined Memory Deficits and Enhancements in NTAN1-Deficient Mice.
S. A. Balogh, Y. T. Kwon, and V. H. Denenberg (2000)
Learn. Mem. 7, 279-286
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Evidence for Separable Functions of Srp1p, the Yeast Homolog of Importin alpha (Karyopherin alpha ): Role for Srp1p and Sts1p in Protein Degradation.
M. M. Tabb, P. Tongaonkar, L. Vu, and M. Nomura (2000)
Mol. Cell. Biol. 20, 6062-6073
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Evidence for an Interaction between Ubiquitin-Conjugating Enzymes and the 26S Proteasome.
P. Tongaonkar, L. Chen, D. Lambertson, B. Ko, and K. Madura (2000)
Mol. Cell. Biol. 20, 4691-4698
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Isolation and Characterization of HRT1 Using a Genetic Screen for Mutants Unable to Degrade Gic2p in Saccharomyces cerevisiae.
M. Blondel, J.-M. Galan, and M. Peter (2000)
Genetics 155, 1033-1044
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Altered Activity, Social Behavior, and Spatial Memory in Mice Lacking the NTAN1p Amidase and the Asparagine Branch of the N-End Rule Pathway.
Y. T. Kwon, S. A. Balogh, I. V. Davydov, A. S. Kashina, J. K. Yoon, Y. Xie, A. Gaur, L. Hyde, V. H. Denenberg, and A. Varshavsky (2000)
Mol. Cell. Biol. 20, 4135-4148
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Stable High-Level Expression of Heterologous Genes In Vitro and In Vivo by Noncytopathic DNA-Based Kunjin Virus Replicon Vectors.
A. N. Varnavski, P. R. Young, and A. A. Khromykh (2000)
J. Virol. 74, 4394-4403
   Abstract »    Full Text »


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