Plant Cell Hybrigenics The Protein Interactions Experts
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THE PLANT CELL, Vol 3, Issue 5 483-496, Copyright © 1991 by American Society of Plant Biologists


RESEARCH ARTICLES

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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ASPB Publications THE PLANT CELL PLANT PHYSIOLOGY
Copyright © 1991 by the American Society of Plant Biologists