Summary
A maize 75 kDa protein recently has been identified as a plant homolog of the mammalian binding protein (BiP). To better understand the function of BiP in protein body formation in maize endosperm, immunomicroscopy studies were conducted on three maize endosperm mutants, floury-2, Mucronate, and Defective endosperm-B 30, in which the level of BiP is highly elevated. Our results showed that protein body morphology in all three mutants was altered. In addition, BiP was localized in both the ER and peripheral regions of the abnormal protein bodies. The degree to which protein body morphology differed from normal was positively correlated with increased amounts of BiP. In addition, the accumulation of BiP in abnormal protein bodies increased with protein body maturation. In the three endosperm mutants, the arrangement of zeins within protein bodies had been perturbed, yet none of the specific zein subclasses exhibited the staining pattern found for BiP. The association of BiP with abnormal packaging of proteins in protein bodies may reflect a biological function to mediate protein folding and assembly in maize endosperm.
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Abbreviations
- BiP:
-
binding protein
- BSA:
-
bovine serum albumin
- De*-B 30:
-
Defective endosperm B 30
- DAP:
-
day after pollination
- ER:
-
endoplasmic reticulum
- fl 2:
-
floury-2
- hsp 70:
-
70 kDa heat shock protein
- Mc:
-
Mucronate
- TBST:
-
20mM Tris-HCl, pH8.2 at 20°C, 500mM NaCl, 0.3% Tween 20
- TBST-B:
-
TBST with 1% (w/v) BSA
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Zhang, F., Boston, R.S. Increases in binding protein (BiP) accompany changes in protein body morphology in three high-lysine mutants of maize. Protoplasma 171, 142–152 (1992). https://doi.org/10.1007/BF01403729
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DOI: https://doi.org/10.1007/BF01403729