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Proc Natl Acad Sci U S A. Jul 1979; 76(7): 3107–3110.
PMCID: PMC383772

Resolution of the ATP-dependent proteolytic system from reticulocytes: a component that interacts with ATP.


The ATP-dependent proteolytic cell-free system from reticulocytes has been resolved into three components, each of which is absolutely required for acid solubilization of 125I-labeled bovine serum albumin radioactivity. In addition to the previously reported heat-stable polypeptide [Ciechanover, A., Hod, Y. & Hershko, A. (1978) Biochem. Biophys. Res Commun. 81, 1100-1105], we now describe a protein of high molecular weight (approximately 450,000) that is labile at 42 degrees C. The extremely heat-labile factors is remarkably stabilized by ATP. GTP and CTP, which do not stimulate protolysis, do not stabilize this factor. Adenylate nucleotides such as ADP or the nonhydrolyzable beta,gamma imido or methylene analogues of ATP cause stabilization although they do not activate proteolysis. A third protein component of the protease system, stable at 42 degrees C, has been separated from the heat-labile species by salt precipitation. All three components are required with ATP for proteolytic activity, but thus far only the heat-labile factor has been shown to interact directly with ATP.

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Selected References

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  • Goldberg AL, St John AC. Intracellular protein degradation in mammalian and bacterial cells: Part 2. Annu Rev Biochem. 1976;45:747–803. [PubMed]
  • Hershko A, Tomkins GM. Studies on the degradation of tyrosine aminotransferase in hepatoma cells in culture. Influence of the composition of the medium and adenosine triphosphate dependence. J Biol Chem. 1971 Feb 10;246(3):710–714. [PubMed]
  • Etlinger JD, Goldberg AL. A soluble ATP-dependent proteolytic system responsible for the degradation of abnormal proteins in reticulocytes. Proc Natl Acad Sci U S A. 1977 Jan;74(1):54–58. [PMC free article] [PubMed]
  • Roberts JW, Roberts CW, Mount DW. Inactivation and proteolytic cleavage of phage lambda repressor in vitro in an ATP-dependent reaction. Proc Natl Acad Sci U S A. 1977 Jun;74(6):2283–2287. [PMC free article] [PubMed]
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  • Moore AT, Williams KE, Lloyd JB. The effect of chemical treatments of albumin and orosomucoid on rate of clearance from the rat bloodstream and rate of pinocytic capture of rat yolk sac cultured in vitro. Biochem J. 1977 Jun 15;164(3):607–616. [PMC free article] [PubMed]
  • Tao M. Further studies on the properties of the rabbit reticulocyte adenosine 3',5'-cyclic monophosphate-dependent protein kinase I. Arch Biochem Biophys. 1971 Mar;143(1):151–157. [PubMed]
  • Roberts JW, Roberts CW, Craig NL. Escherichia coli recA gene product inactivates phage lambda repressor. Proc Natl Acad Sci U S A. 1978 Oct;75(10):4714–4718. [PMC free article] [PubMed]

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