Proteolysis of mitochondria in reticulocytes during maturation is ubiquitin-dependent and is accompanied by a high rate of ATP hydrolysis
- 28 January 1985
- journal article
- Published by Wiley in FEBS Letters
- Vol. 180 (2), 249-252
- https://doi.org/10.1016/0014-5793(85)81080-2
Abstract
The ATP-dependent breakdown of mitochondria-containing stroma proceeds via the ubiquitin-requiring pathway. The proteolysis is linked to a large ATP-cleaved consumption amounting to 1 ATP per peptide bond or more. Proteins of mitochondria-containing stroma are much better substrates of ATP-ubiquitindependent proteolysis than heat-denatured ones. Hemin suppresses both proteolysis and ATP hydrolysisKeywords
This publication has 13 references indexed in Scilit:
- ATP-dependent degradation of ubiquitin-protein conjugates.Proceedings of the National Academy of Sciences of the United States of America, 1984
- Accounting for the ATP‐consuming processes in rabbit reticulocytesEuropean Journal of Biochemistry, 1984
- Ubiquitin: Roles in protein modification and breakdownCell, 1983
- ATP serves two distinct roles in protein degradation in reticulocytes, one requiring and one independent of ubiquitin.The Journal of cell biology, 1983
- Mechanisms of Intracellular Protein BreakdownAnnual Review of Biochemistry, 1982
- Role for the Adenosine Triphosphate-Dependent Proteolytic Pathway in Reticulocyte MaturationScience, 1982
- Determination and Characteristics of Energy-Dependent Proteolysis in Rabbit ReticulocytesEuropean Journal of Biochemistry, 1980
- Nitrogen Economy and the Metabolism of Serine and Glycine in Reticulocytes of RabbitsEuropean Journal of Biochemistry, 1980
- A heat-stable polypeptide component of an ATP-dependent proteolytic system from reticulocytesBiochemical and Biophysical Research Communications, 1978
- A Method for the Colorimetric Determination of PhosphorusScience, 1944