First published online February 24, 2002; 10.1104/pp.010624
Plant Physiol, April 2002, Vol. 128, pp. 1212-1222
The Rice Mutant esp2 Greatly Accumulates the Glutelin
Precursor and Deletes the Protein Disulfide Isomerase1
Yoko
Takemoto,
Sean J.
Coughlan,
Thomas W.
Okita,
Hikaru
Satoh,
Masahiro
Ogawa, and
Toshihiro
Kumamaru*
Institute of Genetic Resources, Faculty of Agriculture, Kyushu
University, Hakozaki, Fukuoka 812-8581, Japan (Y.T., H.S., T.K.);
DuPont Agricultural Experimental Station, 402/4251, Wilmington,
Delaware 19880-0402 (S.J.C.); Institute of Biological Chemistry,
Washington State University, Pullman, Washington 99164-6340 (T.W.O.);
Department of Life Science, Yamaguchi Prefectural University,
Sakurabatake, Yamaguchi 753-8502, Japan (M.O.)
Rice (Oryza sativa) accumulates prolamins and
glutelins as storage proteins. The latter storage protein is
synthesized on the endoplasmic reticulum (ER) as a 57-kD
proglutelin precursor, which is then processed into acidic and basic
subunits in the protein storage vacuole. Three esp2
mutants, CM1787, EM44, and EM747, contain larger amounts of the 57-kD
polypeptide and corresponding lower levels of acidic and basic glutelin
subunits than normal. Electron microscopic observation revealed that
esp2 contained normal-appearing glutelin-containing
protein bodies (PB-II), but lacked the normal prolamin-containing PB
(PB-I). Instead, numerous small ER-derived PBs of uniform size (0.5 µm in diameter) and low electron density were readily observed.
Immunoblot analysis of purified subcellular fractions and
immunocytochemistry at the electron microscopy level showed that these
new PBs contained the 57-kD proglutelin precursor and prolamin
polypeptides. The 57-kD proglutelin was extracted with 1% (v/v)
lactic acid solution only after removal of cysteine-rich prolamin
polypeptides, suggesting that these proteins form glutelin-prolamin
aggregates via interchain disulfide bonds within the ER lumen. The
endosperm of esp2 mutants contains the lumenal
chaperones, binding protein and calnexin, but lacks protein
disulfide isomerase (PDI) at the protein and RNA levels. The transcript
of PDI was expressed in the seed only during the early stage of seed
development in the wild type. These results suggest that PDI plays an
essential role in the segregation of proglutelin and prolamin
polypeptides within the ER lumen.
1
This work was supported by the Ministry of
Education, Science and Culture of Japan (grant nos. 10660009 and
1213826) and by the National Science Foundation (grant no. IBN-9982483
to T.W.O.). This research study is part of Project 0590 of the
Agricultural Research Center, Washington State University.
*
Corresponding author; e-mail kumamaru{at}agr.kyushu-u.ac.jp; fax
81-92-642-3057.
© 2002 American Society of Plant Physiologists
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