The rice glup2 lines are characterized by their abnormally high levels of endosperm 57 kDa proglutelins and of the luminal chaperone binding protein (BiP), features characteristic of a defect within the endoplasmic reticulum (ER). To elucidate the underlying genetic basis, the glup2 locus was identified by map based cloning. DNA sequencing of the genomes of three glup2 alleles and wild type demonstrated that the underlying genetic basis was mutations in the Golgi transport 1 (GOT1B) coding sequence. This conclusion was further validated by restoration of normal proglutelin levels in a glup2 line complemented by a GOT1B gene. Microscopic analyses indicated the presence of proglutelin-α-globulin-containing intracisternal granules surrounded by prolamine inclusions within the ER lumen. As assessed by in situ reverse transcriptase polymerase chain reaction (RT-PCR) analysis of developing endosperm sections, prolamine and α-globulin RNAs were found to be mis-targeted from their usual sites on the protein body ER to the cisternal ER, the normal sites of proglutelin synthesis. Our results indicate that GLUP2/GOT1B has a dual role during rice endosperm development. It is required for localization of prolamine and α-globulin RNAs to the protein body ER and for efficient export of proglutelin and α-globulin proteins from the ER to the Golgi apparatus.
Keywords: Endoplasmic reticulum; Golgi transport; Intracellular transport; Proglutelin; Protein body; Storage protein.
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