Expression and post-translational modification of barley 14-3-3 isoforms, 1
4-3-3A, 14-3-3B and 14-3-3C, mere investigated using isoform-specific antib
odies. Although all three isoforms were shown to be present in the cytosoli
c, the nuclear and the microsomal cell fractions, differences in post-trans
lational modification were identified for the different cell fractions. Ger
mination-related modifications of 14-3-3 proteins mere observed in the cyto
sol and the microsomal fraction, but not in the nucleus. In vitro proteolyt
ic cleavage of 14-3-3 proteins using trypsin suggests that for 14-3-3A this
change mas caused by proteolytic cleavage of the unconserved C-terminal re
gion. (C) 2000 Federation of European Biochemical Societies.