Rapid Degradation of Abnormal Proteins in Vacuoles from Acer pseudoplatanus L. Cells
- 1 June 1986
- journal article
- research article
- Published by Oxford University Press (OUP) in Plant Physiology
- Vol. 81 (2) , 460-463
- https://doi.org/10.1104/pp.81.2.460
Abstract
In Acer pseudoplatanus cells, the proteins synthesized in the presence of an amino acid analog ([14C]p-fluorophenylalanine), were degraded more rapidly than normal ones ([14C]phenylalanine as precursor). The degradation of an important part of these abnormal proteins occurred inside the vacuoles. The degradation process was not apparently associated to a specific proteolytic system but was related to a preferential transfer of these aberrant proteins from the cytoplasm to the vacuole.This publication has 18 references indexed in Scilit:
- Hydrolysis of Intracellular Proteins in Vacuoles Isolated from Acer pseudoplatanus L. CellsPlant Physiology, 1985
- Abnormal proteins of shortened length are preferentially degraded in the cytosol of cultured MRC5 fibroblastsFEBS Letters, 1984
- Structural and physical changes in lysosomes from isolated rat hepatocytes treated with methylamineBiochimica et Biophysica Acta (BBA) - Molecular Cell Research, 1983
- Control of ProteolysisAnnual Review of Biochemistry, 1980
- Hydrolytic Enzymes in the Central Vacuole of Plant CellsPlant Physiology, 1979
- Intracellular Protein Degradation in Mammalian and Bacterial Cells: Part 2Annual Review of Biochemistry, 1976
- Rapid degradation of puromycyl peptides in hepatoma cells and reticulocytesFEBS Letters, 1974
- p-Fluoropheiiylalanine and ‘Division-related Proteins’Nature, 1974
- Enzyme degradation in higher plants: PhosphoglucomutaseFEBS Letters, 1973
- Formation of a ribosomal lesion in rabbit reticulocytes by the lysine antagonist, S-(β-aminoethyl) cysteineBiochemical and Biophysical Research Communications, 1962