Journal Article

Protein Disulfide Isomerase Like 1-1 Participates in the Maturation of Proglutelin Within the Endoplasmic Reticulum in Rice Endosperm

Mio Satoh-Cruz, Andrew J. Crofts, Yoko Takemoto-Kuno, Aya Sugino, Haruhiko Washida, Naoko Crofts, Thomas W. Okita, Masahiro Ogawa, Hikaru Satoh and Toshihiro Kumamaru

in Plant and Cell Physiology

Published on behalf of Japanese Society of Plant Physiologists

Volume 51, issue 9, pages 1581-1593
Published in print September 2010 | ISSN: 0032-0781
Published online July 2010 | e-ISSN: 1471-9053 | DOI: http://dx.doi.org/10.1093/pcp/pcq098
Protein Disulfide Isomerase Like 1-1 Participates in the Maturation of Proglutelin Within the Endoplasmic Reticulum in Rice Endosperm

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The rice esp2 mutation was previously characterized by the abnormal accumulation of elevated levels of proglutelin and the absence of an endosperm-specific protein disulfide isomerase like (PDIL1-1). Here we show that Esp2 is the structural gene for PDIL1-1 and that this lumenal chaperone is asymmetrically distributed within the cortical endoplasmic reticulum (ER) and largely restricted to the cisternal ER. Temporal studies indicate that PDIL1-1 is essential for the maturation of proglutelin only when its rate of synthesis significantly exceeds its export from the ER, a condition resulting in its build up in the ER lumen and the induction of ER quality control processes which lower glutelin levels as well as those of the other storage proteins. As proglutelin is initially synthesized on the cisternal ER, its deposition within prolamine protein bodies in esp2 suggests that PDIL1-1 helps retain proglutelin in the cisternal ER lumen until it attains competence for ER export and, thereby, indirectly preventing heterotypic interactions with prolamine polypeptides.

Keywords: Endoplasmic reticulum; Endosperm; Oryza sativa; Protein body; Protein disulfide isomerase; Storage protein

Journal Article.  6836 words.  Illustrated.

Subjects: Biochemistry ; Molecular and Cell Biology ; Plant Sciences and Forestry

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