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THE PLANT CELL, Vol 3, Issue 5 483-496, Copyright © 1991 by American Society of Plant Biologists
Characterization of an Immunoglobulin Binding Protein Homolog in the Maize floury-2 Endosperm Mutant
EBP. Fontes, B. B. Shank, R. L. Wrobel, S. P. Moose, G. R. OBrian, E. T. Wurtzel and R. S. Boston
Department of Botany, Box 7612, North Carolina State University, Raleigh, North Carolina 27695-7612
The maize b-70 protein is an endoplasmic reticulum protein overproduced in
the floury-2 (fl2) endosperm mutant. The increase in b-70 levels in fl2
plants occurs during seed maturation and is endosperm specific. We have
used amino acid sequence homology to identify b-70 as a homolog of
mammalian immunoglobulin binding protein (BiP). Purified b-70 fractions
contain two 75-kilodalton polypeptides with pl values of 5.3 and 5.4. Both
75-kilodalton polypeptides share several properties with BiP, including the
ability to bind ATP and localization within the lumen of the endoplasmic
reticulum. In addition, both b-70 polypeptides can be induced in maize cell
cultures with tunicamycin treatment. Like BiP, the pl 5.3 form of b-70 is
post-translationally modified by phosphorylation and ADP-ribosylation.
However, modification of the pl 5.4 species was not detected in vitro or in
vivo. Although the b-70 gene is unlinked to fl2, b-70 overproduction is
positively correlated with the fl2 gene and is regulated at the mRNA level.
In contrast, the fl2 allele negatively affects the accumulation of the
major endosperm storage proteins. The physical similarity of b-70 to BiP
and its association with abnormal protein accumulation in fl2 endoplasmic
reticulum may reflect a biological function to mediate protein folding and
assembly in maize endosperm.
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