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. 1991 May;3(5):497–505. doi: 10.1105/tpc.3.5.497

Increased expression of the maize immunoglobulin binding protein homolog b-70 in three zein regulatory mutants.

R S Boston 1, E B Fontes 1, B B Shank 1, R L Wrobel 1
PMCID: PMC160017  PMID: 1840924

Abstract

Plants carrying floury-2, Defective endosperm-B30, or Mucronate mutations overproduce b-70, a maize homolog of the mammalian immunoglobulin binding protein. During endosperm development in these mutants, levels of both b-70 protein and RNA increase dramatically between 14 days and 20 days after pollination. At later stages, b-70 RNA levels decline while protein levels remain high. The increase in b-70 RNA levels is endosperm specific and dependent on gene dosage in the floury-2 mutant. In all three mutants, the increases in b-70 RNA and protein levels are inversely proportional to changes in zein synthesis. Although b-70 polypeptides can be extracted from purified protein bodies, they carry a carboxy-terminal endoplasmic reticulum retention signal, HDEL. We propose that induction of b-70 in these mutants is a cellular response to abnormally folded or improperly assembled storage proteins and probably reflects its role as a polypeptide chain binding protein.

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Selected References

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