Activation of the heat-stable polypeptide of the ATP-dependent proteolytic system.
- 1 February 1981
- journal article
- research article
- Published by Proceedings of the National Academy of Sciences in Proceedings of the National Academy of Sciences
- Vol. 78 (2) , 761-765
- https://doi.org/10.1073/pnas.78.2.761
Abstract
It had been shown previously that the heat-stable polypeptide of the ATP-dependent proteolytic system of reticulocytes, designated APF-1, forms covalent conjugates with protein substrates in an ATP-requiring process. We now describe an enzyme that carries out the activation by ATP of the polypeptide with pyrophosphate displacement. The formation of AMP-polypeptide and transfer of the polypeptide to a secondary acceptor are suggested by an APF-1 requirement for ATP-PPi and ATP-AMP exchange reactions, respectively. With radiolabeled polypeptide, an ATP-dependent labeling of the enzyme was shown to be by a linkage that is acid stable but is labile to treatment with mild alkali, hydroxylamine, borohydride, or mercuric salts. It therefore appears that the AMP-polypeptide undergoes attack by an -SH group of the enzyme to form a thiolester.This publication has 24 references indexed in Scilit:
- Characterization of the heat-stable polypeptide of the ATP-dependent proteolytic system from reticulocytes.Journal of Biological Chemistry, 1980
- Proposed role of ATP in protein breakdown: conjugation of protein with multiple chains of the polypeptide of ATP-dependent proteolysis.Proceedings of the National Academy of Sciences, 1980
- Hybrid troponin reconstituted from vertebrate and arthropod subunitsNature, 1975
- Attempts to Map a Process Evolution of Peptide BiosynthesisScience, 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
- PEPTIDYL TRANSFERS IN GRAMICIDIN S BIOSYNTHESIS FROM ENZYME-BOUND THIOESTER INTERMEDIATESProceedings of the National Academy of Sciences, 1969
- 5'-ADENYLYL-O-TYROSINE - NOVEL PHOSPHODIESTER RESIDUE OF ADENYLYLATED GLUTAMINE SYNTHETASE FROM ESCHERICHIA COLI1968
- An improved method for isolation of crystalline pyrophosphatase from baker's yeastArchives of Biochemistry and Biophysics, 1961
- Observations on intracellular protein catabolism studied in vitroArchives of Biochemistry and Biophysics, 1956
- THE RELEASE OF LABELED AMINO ACIDS FROM THE PROTEINS OF RAT LIVER SLICESJournal of Biological Chemistry, 1953