Protein synthesis elongation factor EF-1α is an isopeptidase essential for ubiquitin-dependent degradation of certain proteolytic substrates

Advances in Experimental Medicine and Biology

Volumn 389, Issue , 1996, Pages 209-219

  Gonen, Hedva ^a   Dickman, Dalia ^a   Schwartz, Alan L ^b   Ciechanover, Aaron ^a  

^a TECHNION ISRAEL INSTITUTE OF TECHNOLOGY   (Israel)

^b WASHINGTON UNIVERSITY SCHOOL OF MEDICINE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIA (MICROORGANISMS);

AMINO TERMINAL SEQUENCE; CONFERENCE PAPER; ENZYME ACTIVITY; ENZYME ANALYSIS; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN DEGRADATION; PROTEIN SYNTHESIS; RNA TRANSLATION; SIGNAL TRANSDUCTION; AMINO ACID SEQUENCE; ANIMAL; ARTICLE; CHEMISTRY; ENZYME SPECIFICITY; METABOLISM; MOLECULAR GENETICS; RABBIT; RETICULOCYTE; SACCHAROMYCES CEREVISIAE; SEQUENCE HOMOLOGY;

BIOLOGICAL FACTOR; DRUG DERIVATIVE; ELONGATION FACTOR; ELONGATION FACTOR 1; ISOPEPTIDASE; LYASE; TRANSFER RNA; UBIQUITIN; UBIQUITIN ALDEHYDE; UBIQUITIN-ALDEHYDE;

AMINO ACID SEQUENCE; ANIMALS; BIOLOGICAL FACTORS; CARBON-NITROGEN LYASES; LYASES; MOLECULAR SEQUENCE DATA; PEPTIDE ELONGATION FACTOR 1; PEPTIDE ELONGATION FACTORS; RABBITS; RETICULOCYTES; RNA, TRANSFER; SACCHAROMYCES CEREVISIAE; SEQUENCE HOMOLOGY, AMINO ACID; SUBSTRATE SPECIFICITY; UBIQUITINS;

EID: 0030330024     PISSN: 00652598     EISSN: None     Source Type: Book Series    
DOI: 10.1007/978-1-4613-0335-0_26     Document Type: Article

References (14)

1. Ciechanover, A. (1994). The ubiquitin-proteasome pathway. Cell 79, 13-21.
2. Gonen, H., Schwartz, A.L., and Ciechanover, A. (1991). Purification and characterization of a novel protein that is required tor the degradation of N-α- acetylated poteins by the uiquitin sstem. J. Biol. Chem. 266, 19221-19231.
3. Gonen, H., Smith, C. E., Siegel, N. R., Merrick, W. C., Kahana, C., Chakraburtty, K., Schwartz, A. L., and Ciechanover, A. (1994). Protein Synthesis elongation factor EF-1α is essential for ubiquitin-dependent degradation of N- α-acetylated proteins and may be substituted for by the bacterial elongation factor EF-Tu. Proc. Natl. Acad. Sci. USA 91, 7648-7652.
4. Hershko, A. and Ciechanover, A. (1992). The ubiquitin-mediated proteolytic Pathway. Annu. Rev. Biochem. 61, 761-807.
5. Hershko, A. and Rose, I. A. (1987). Ubiquitin-aldehyde: A general inhibitor of ubiquitin recycling processes. Proc. Natl. Acad. Sci. USA 84, 1829-1833
6. Jap, B., Puhler, G., Lucke, H., Typke, D., Lowe, J., Stock, D., Huber, R., and Baumeister, W. (1993). Preliminary X-ray crystallographic study of the proteasome from Thermoplasma acidophilum. J. Mol. Biol. 234, 881-884.
7. Louie, A., Ribeiro, N. S., Reid, R. B., and Jurnak, F. (1984). Relative affinities of all Escherichia coli aminoacyl-tRNAs for elongation factor Tu-GTP. J. Biol. Chem. 259, 5010-5016.
8. Merrick, W. C., Dever, T. E., Kinzy, T. G., Conroy, S. C., Cavallius, J., and Owens, C. L. (1990). Characterization of protein synthesis factors from rabbit reticulocytes. Biochim. Biophys. Acta 1050, 235-240.
9. Shiina, N., Gotoh, Y., Kubomura, N., Iwamatsu, A., and Nishida, E. (1994). Microtubule severeing by elongation factor 1α. Science 266, 282-285.
10. Tischler, M.E., DeSautels, M., and Goldberg, A.L. (1982). Does leucine, leucyl-tRNA, or some metabolite of leucine regulate protein synthesis and degradation in skeletal and cardiac muscle? J. Biol. Chem. 257, 1613-1621.
11. Tobias, J. W., Shrader, T. E., Rocap, G., and Varshavsky, A. (1991). The N-end rule in bacteria. Science 254, 1374-1377.
12. Varshavsky, A. 1992. The N-end rule. Cell 69, 725-735.
13. Wing, S.S. and Goldberg, A.L. (1993). Glucocorticoids activate the ATP- ubiquitin-dependent proteolytic system in skeletal muscle during fasting. Am. J. Physiol. 264, E668-E676.
14. Wolf, S., Lottspeich, and Baumeister, W. (1993). Ubiquitin found in the archaebacterium Themoplasma acidophilum. FEBS Lett. 326, 42-44.