Subcellular differences in post-translational modification of barley 14-3-3 proteins.
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.
van Zeijl
M J
MJ
Center for Phytotechnology, Leiden University, The Netherlands Organization for Applied Scientific Research (UL/TNO), TNO Department of Applied Plant Sciences, Wassenaarseweg, AL Leiden, The Netherlands.
Testerink
C
C
Kijne
J W
JW
Wang
M
M
D048948:14-3-3 Proteins; D000906:Antibodies; D015153:Blotting, Western; D004591:Electrophoresis, Polyacrylamide Gel; D001467:Hordeum / Q000378:metabolism*; D010940:Plant Proteins / Q000378:metabolism; D020033:Protein Isoforms / Q000276:immunology / Q000378:metabolism; D011499:Protein Processing, Post-Translational; D011506:Proteins / Q000276:immunology / Q000378:metabolism*; D012639:Seeds / Q000737:chemistry / Q000378:metabolism; D013347:Subcellular Fractions / Q000378:metabolism; D014357:Trypsin / Q000494:pharmacology; D014446:Tyrosine 3-Monooxygenase
D048948:14-3-3 Proteins; D000906:Antibodies; D010940:Plant Proteins; D020033:Protein Isoforms; D011506:Proteins; D014446:Tyrosine 3-Monooxygenase; D014357:Trypsin