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Journal of Experimental Botany, Vol. 52, No. 365, pp. 2387-2388, December 1, 2001
© 2001 Oxford University Press

Gene Note

Expression patterns of genes encoding endomembrane proteins support a reduced function of the Golgi in wheat endosperm during the onset of storage protein deposition

Galia Shy1, Linda Ehler2, Eliot Herman2 and Gad Galili1,3

1 Department of Plant Sciences, the Weizmann Institute of Science, Rehovot, Israel
2 Soybean Genomics Improvement Laboratory, USDA, Beltsville MD, USA

Abstract

Wheat storage proteins are deposited in the vacuole of maturing endosperm cells by a novel pathway that is the result of protein body formation by the endoplasmic reticulum followed by autophagy into the central vacuole, bypassing the Golgi apparatus. This model predicts a reduced role of the Golgi in storage protein accumulation, which has been supported by electron microscopy observations. To study this issue further, wheat cDNAs encoding three distinct proteins of the endomembrane system were cloned and characterized. The proteins encoded were homologues (i) of the ER translocon component Sec61{alpha}, (ii) the vacuolar sorting receptor BP-80 which is located in the Golgi and clathrin-coated prevacuole vesicles (CCV), and (iii) the Golgi COPI coatomer component COP{alpha}. During endosperm development, the levels of all three mRNAs were highest in young stages, before the onset of storage protein synthesis, and declined with seed maturation. However, the relative mRNA levels of BP-80/Sec61{alpha} and the COP{alpha}/Sec61{alpha} were lower during the onset of storage protein synthesis than at earlier stages of endosperm development. These results support previous studies, suggesting a reduced function of the Golgi apparatus in wheat storage protein transport and deposition.

Key words: Wheat, storage proteins, endoplasmic reticulum, storage vacuoles, endomembrane system.


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[Abstract] [Full Text] [PDF]


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