Resolution of the ATP-dependent proteolytic system from reticulocytes: a component that interacts with ATP.
- 1 July 1979
- journal article
- research article
- Published by Proceedings of the National Academy of Sciences in Proceedings of the National Academy of Sciences
- Vol. 76 (7) , 3107-3110
- https://doi.org/10.1073/pnas.76.7.3107
Abstract
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.This publication has 8 references indexed in Scilit:
- Escherichia coli recA gene product inactivates phage lambda repressor.Proceedings of the National Academy of Sciences, 1978
- A heat-stable polypeptide component of an ATP-dependent proteolytic system from reticulocytesBiochemical and Biophysical Research Communications, 1978
- 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 vitroBiochemical Journal, 1977
- Inactivation and proteolytic cleavage of phage lambda repressor in vitro in an ATP-dependent reaction.Proceedings of the National Academy of Sciences, 1977
- A soluble ATP-dependent proteolytic system responsible for the degradation of abnormal proteins in reticulocytes.Proceedings of the National Academy of Sciences, 1977
- Intracellular Protein Degradation in Mammalian and Bacterial Cells: Part 2Annual Review of Biochemistry, 1976
- Further studies on the properties of the rabbit reticulocyte adenosine 3′,5′-cyclic monophosphate-dependent protein kinaseArchives of Biochemistry and Biophysics, 1971
- Studies on the degradation of tyrosine aminotransferase in hepatoma cells in culture. Influence of the composition of the medium and adenosine triphosphate dependence.1971