Plant and Cell Physiology, 1986, Vol. 27, No. 1 135-145
© 1986
Article |
The Site of Synthesis and Accumulation of Rice Storage Proteins
Department of Biochemistry, College of Agricultural Chemistry, Kyoto Prefectural University Shimogamo, Kyoto 606, Japan
Electron microscopy showed that the two types of protein bodies (PB) in starchy endosperms of rice were formed differently during the period of storage protein accumulation. Two routes for the transport of storage protein from the site of synthesis at the rough endoplasmic reticulum (RER) to the site of accumulation were also proposed. PB-I, bound by a single membrane to which ribosomes were attached, was thought to develop inside the cisternae of RER, while the PB-II membrane was thought to originate from the vacuole.
In the wheat germ cell-free translation system, storage protein-related polypeptides of developing rice endosperms, including a precursor of glutelin and putative precursors of prolamin, were directed by membrane-bound polysomes but not by free-polysomes. Immunoassay of the total translation products directed by a PB fraction showed that 46% were storage protein-related polypeptides.
Rice storage proteins (prolamin) that accumulate in PB-I appear to be synthesized by membrane-bound polysomes attached to PB-I or RER and to pass through the membrane into the lumen where they aggregate and are deposited. The proteins (glutelin and globulin) that accumulate in PB-II, however, seem to be synthesized by membrane-bound polysomes as a large precursor and to become sequestered into the cisternal space of RER, from where they are transferred to the vacuolar precursor of PB-II.
(Received August 6, 1985; Accepted November 6, 1985)
CiteULike 
Connotea 
Del.icio.us What's this?
This article has been cited by other articles:
|
|
 |
|
  T. Nochi, H. Takagi, Y. Yuki, L. Yang, T. Masumura, M. Mejima, U. Nakanishi, A. Matsumura, A. Uozumi, T. Hiroi, et al. From the Cover: Rice-based mucosal vaccine as a global strategy for cold-chain- and needle-free vaccination PNAS, June 26, 2007; 104(26): 10986 - 10991. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 H. Yasuda, Y. Hayashi, T. Jomori, and F. Takaiwa The Correlation between Expression and Localization of a Foreign Gene Product in Rice Endosperm Plant Cell Physiol., June 1, 2006; 47(6): 756 - 763. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 Y. Kawagoe, K. Suzuki, M. Tasaki, H. Yasuda, K. Akagi, E. Katoh, N. K. Nishizawa, M. Ogawa, and F. Takaiwa The Critical Role of Disulfide Bond Formation in Protein Sorting in the Endosperm of Rice PLANT CELL, April 1, 2005; 17(4): 1141 - 1153. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 P. R. Shewry and N. G. Halford Cereal seed storage proteins: structures, properties and role in grain utilization J. Exp. Bot., April 15, 2002; 53(370): 947 - 958. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 T. Katsube, N. Kurisaka, M. Ogawa, N. Maruyama, R. Ohtsuka, S. Utsumi, and F. Takaiwa Accumulation of Soybean Glycinin and Its Assembly with the Glutelins in Rice Plant Physiology, August 1, 1999; 120(4): 1063 - 1074. [Abstract] [Full Text]
|
|
|
|
 |
|
 X Li, Y Wu, D. Zhang, J. Gillikin, R. Boston, V. Franceschi, and T. Okita Rice prolamine protein body biogenesis: a BiP-mediated process Science, November 12, 1993; 262(5136): 1054 - 1056. [Abstract] [PDF]
|
|
|
|
|
|
Y. Takemoto, S. J. Coughlan, T. W. Okita, H. Satoh, M. Ogawa, and T. Kumamaru The Rice Mutant esp2 Greatly Accumulates the Glutelin Precursor and Deletes the Protein Disulfide Isomerase Plant Physiology, April 1, 2002; 128(4): 1212 - 1222. [Abstract] [Full Text] [PDF]
|
|