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Subcellular differences in post-translational modification of barley 14-3-3 proteins

Author: Zeijl, M.J. van · Testerink, C. · Kijne, J.W. · Wang, M.
Type:article
Date:2000
Source:FEBS Letters, 3, 473, 292-296
Identifier: 280417
doi: doi:10.1016/S0014-5793(00)01545-3
Keywords: 14-3-3 Protein · Cell compartment · Germination · Hordeum distichum · Post-translational modification · isoprotein · protein antibody · trypsin · vegetable protein · barley · carboxy terminal sequence · cell fractionation · cell nucleus · controlled study · cytosol · electrophoresis · germination · microsome · priority journal · protein degradation · protein expression · protein modification · protein processing · Western blotting · 14-3-3 Proteins · Antibodies · Blotting, Western · Electrophoresis, Polyacrylamide Gel · Hordeum · Plant Proteins · Protein Isoforms · Protein Processing, Post-Translational · Proteins · Seeds · Subcellular Fractions · Trypsin · Tyrosine 3-Monooxygenase · Hordeum · Hordeum vulgare subsp. vulgare · Staphylococcus phage 3A

Abstract

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