Subcellular differences in post-translational modification of barley 14-3-3 proteins
article
Expression and post-translational modification of barley 14-3-3 isoforms, 14-3-3A, 14-3-3B and 14-3-3C, were investigated using isoform-specific antibodies. Although all three isoforms were shown to be present in the cytosolic, the nuclear and the microsomal cell fractions, differences in post-translational modification were identified for the different cell fractions. Germination-related modifications of 14-3-3 proteins were observed in the cytosol and the microsomal fraction, but not in the nucleus. In vitro proteolytic cleavage of 14-3-3 proteins using trypsin suggests that for 14-3-3A this change was caused by proteolytic cleavage of the unconserved C-terminal region. Copyright (C) 2000 Federation of European Biochemical Societies. Chemicals/CAS: 14-3-3 Proteins; Antibodies; Plant Proteins; Protein Isoforms; Proteins; Trypsin, EC 3.4.21.4; Tyrosine 3-Monooxygenase, EC 1.14.16.2
Topics
14-3-3 ProteinCell compartmentGerminationHordeum distichumPost-translational modificationisoproteinprotein antibodytrypsinvegetable proteinbarleycarboxy terminal sequencecell fractionationcell nucleuscontrolled studycytosolelectrophoresisgerminationmicrosomepriority journalprotein degradationprotein expressionprotein modificationprotein processingWestern blotting14-3-3 ProteinsAntibodiesBlotting, WesternElectrophoresis, Polyacrylamide GelHordeumPlant ProteinsProtein IsoformsProtein Processing, Post-TranslationalProteinsSeedsSubcellular FractionsTrypsinTyrosine 3-MonooxygenaseHordeumHordeum vulgare subsp. vulgareStaphylococcus phage 3A
TNO Identifier
280417
ISSN
00145793
Source
FEBS Letters, 473(3), pp. 292-296.
Pages
292-296