Abstract
The reader of this book will appreciate the significant progress that has been achieved in this field in less than a decade. Since the discovery of the involvement of ubiquitin (Ub) in protein breakdown in 19781 and of its covalent ligation to proteins in 1980,2 many of the enzymatic reactions in the formation and breakdown of Ub-protein conjugates have been elucidated. Techniques that have been developed to study the roles of Ub in intact cells include the use of specific antibodies, microinjection methods, a mammalian cell mutant, and cloned genes. Results obtained with such experimental techniques have confirmed the widespread occurrence and major physiological functions of the Ub proteolytic system (reviewed in refs. 3–5).
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References
Ciechanover, A., Hod, Y., and Hershko, A., 1978, A heat-stable polypeptide component of an ATP-dependent proteolytic system from reticulocytes, Biochem. Biophys. Res. Commun. 81: 1100–1105.
Hershko, A., Ciechanover, A., Heller, H., Haas, A. L., and Rose, I. A., 1980, Proposed role of ATP in protein breakdown: Conjugation of proteins with multiple chains of the polypeptide of ATP-dependent proteolysis, Proc. Natl. Acad. Sci. U.S.A. 77: 1783–1786.
Hershko, A., and Ciechanover, A., 1982, Mechanisms of intracellular protein breakdown, Annu. Rev. Biochem. 51: 335–364.
Finley, D., and Varshavsky, A., 1985, The ubiquitin system: Functions and mechanisms, TIBS 10: 343–347.
Hershko, A., and Ciechanover, A., 1986, The ubiquitin pathway for the degradation of intracellular proteins, Prog. Nucleic Acid Res. Mol. Biol. 33: 19–56.
Hershko, A., Leshinksy, E., Ganoth, D., and Heller, H., 1984, ATP-dependent degradation of ubiquitin-protein conjugates, Proc. Natl. Acad. Sci. U.S.A. 81: 1619–1623.
Hough, R., Pratt, G., and Rechsteiner, M., 1986, Ubiquitin-lysozyme conjugates. Identification and characterization of an ATP-dependent protease from rabbit reticulocyte lysates, J. Biol. Chem. 261: 2400–2408.
Hershko, A., Heller, H., Eytan, E., Kaklij, G., and Rose, I. A., 1984, Role of the α-amino group of protein in ubiquitin-mediated protein breakdown, Proc. Natl. Acad. Sci. U.S.A. 81: 7021–7025.
Ciechanover, A., Wolin, S. L., Steitz, J. A., and Lodish, H. F., 1985, Transfer RNA is an essential component of the ubiquitin-and ATP-dependent proteolytic system, Proc. Natl. Acad. Sci. U.S.A. 82: 1341–1345.
Ferber, S., and Ciechanover, A., 1986, Transfer RNA is required for conjugation of ubiquitin to selective substrates of the ubiquitin-and ATP-dependent proteolytic system, J. Biol. Chem. 261: 3128–3134.
Ferber, S., and Ciechanover, A., 1987, Role of arginine-tRNA in protein degradation by the ubiquitin pathway, Nature 326: 808–810.
Bachmair, A., Finley, D., and Varshavsky, A., 1986, In vivo half-life of a protein is a function of its amino-terminal residue, Science 234: 179–186.
Rogers, S., Wells, R., and Rechsteiner, M., 1986, Amino acid sequences common to rapidly degraded proteins: The PEST hypothesis, Science 234: 364–368.
Hershko, A., Heller, H., Eytan, E., and Reiss, Y., 1986, The protein substrate binding site of the ubiquitin-protein ligase system, J. Biol. Chem. 261: 11992–11999.
Fucci, L., Oliver, C. N., Coon, M. J., and Stadtman, E. R., 1983, Inactivation of key metabolic enzymes by mixed-function oxidation reactions: Possible implication in protein turnover and aging, Proc. Natl. Acad. Sci. U.S.A. 80: 1521–1528.
Levine, R. L., 1983, Oxidative modification of glutamine synthetase. Inactivation is due to loss of one histidine residue, J. Biol. Chem. 258: 11823–11827.
Evans, A. C., Jr., and Wilkinson, K. D., 1985, Ubiquitin-dependent proteolysis of native and alkylated bovine serum albumin: Effects of protein structure and ATP concentration on selectivity, Biochemistry 24: 2915–2923.
Katznelson, R., and Kulka, R. G., 1985, Effects of denaturation and methylation on the degradation of proteins in cultured hepatoma cells and in reticulocyte cell-free systems, Eur. J. Biochem. 146: 437–442.
Rote, K. V., and Rechsteiner, M., 1986, Degradation of proteins microinjected into HeLa cells: The role of substrate flexibility, J. Biol. Chem. 261: 15430–15436.
Hershko, A., Heller, H., Elias, S., and Ciechanover, A., 1983, Components of ubiquitin-protein ligase system. Resolution, affinity purification and role in protein breakdown, J. Biol. Chem. 258: 8206–8214.
Breslow, E., Daniel, R., Ohba, R., and Tate, S., 1986, Inhibition of ubiquitin-dependent proteolysis by non-ubiquitinable proteins, J. Biol. Chem. 261: 6530–6535.
Reiss, Y., Kaim, D., and Hershko, A., 1988, J. Biol. Chem. (in press).
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© 1988 Springer Science+Business Media New York
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Hershko, A. (1988). Selectivity of Ubiquitin-Mediated Protein Breakdown. In: Rechsteiner, M. (eds) Ubiquitin. Springer, Boston, MA. https://doi.org/10.1007/978-1-4899-2049-2_13
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DOI: https://doi.org/10.1007/978-1-4899-2049-2_13
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