Logo of plntphysLink to Publisher's site
Plant Physiol. 1982 Oct; 70(4): 1094–1100.
PMCID: PMC1065832

Biosynthesis of Storage Proteins in Developing Rice Seeds


Sodium dodecyl sulfate-polyacrylamide gel electrophoretic analysis of the starchy endosperm protein of rice (Oryza sativa L. Japonica cv Koshihikari) during seed development confirmed that storage protein begins to accumulate about 5 days after flowering. Two polypeptide groups, 22 to 23 and 37 to 39 kilodaltons, the components of glutelin, the major storage protein in rice seed, appeared 5 days after flowering. A 26-kilodalton polypeptide, the globulin component, also appeared 5 days after flowering. Smaller polypeptides (10- to 16-kilodaltons) including prolamin components, appeared about 10 days after flowering. In contrast, the levels of the 76- and 57-kilodalton polypeptides were fairly constant throughout seed development. Transmission electron microscopy and fractionation by sucrose density gradient centrifugation of the starchy endosperms at various stages of development showed that protein body type II, the accumulation site of glutelin and globulin, was formed faster than protein body type I, the accumulation site of prolamin.

The 57-kilodalton polypeptide but not the glutelin subunits was labeled in a 2-hour treatment with [14C]leucine given between 4 and 12 days after flowering to developing ears. In vivo pulse-chase labeling studies showed the 57-kilodalton polypeptide to be a precursor of the 22 to 23 and 37 to 39 kilodalton subunits. The 57-kilodalton polypeptide was salt-soluble, but the mature glutelin subunits were almost salt insoluble.

In vitro protein synthesis also showed that the mRNAs directly coding the 22 to 23 and 37 to 39 kilodalton components were absent in developing seeds and that the 57-kilodalton polypeptide was the major product. Thus, it was concluded that the two subunits of rice glutelin are formed through post-translational cleavage of the 57-kilodalton polypeptide.

Full text

Full text is available as a scanned copy of the original print version. Get a printable copy (PDF file) of the complete article (2.3M), or click on a page image below to browse page by page. Links to PubMed are also available for Selected References.

Images in this article

Selected References

These references are in PubMed. This may not be the complete list of references from this article.
  • Blobel G, Dobberstein B. Transfer of proteins across membranes. I. Presence of proteolytically processed and unprocessed nascent immunoglobulin light chains on membrane-bound ribosomes of murine myeloma. J Cell Biol. 1975 Dec;67(3):835–851. [PMC free article] [PubMed]
  • Bonner WM, Laskey RA. A film detection method for tritium-labelled proteins and nucleic acids in polyacrylamide gels. Eur J Biochem. 1974 Jul 1;46(1):83–88. [PubMed]
  • Greene FC. In Vitro Synthesis of Wheat (Triticum aestivum L.) Storage Proteins. Plant Physiol. 1981 Sep;68(3):778–783. [PMC free article] [PubMed]
  • Hall TC, Ma Y, Buchbinder BU, Pyne JW, Sun SM, Bliss FA. Messenger RNA for G1 protein of French bean seeds: Cell-free translation and product characterization. Proc Natl Acad Sci U S A. 1978 Jul;75(7):3196–3200. [PMC free article] [PubMed]
  • Joseph T, Higgins V, Spencer D. Precursor Forms of Pea Vicilin Subunits: MODIFICATION BY MICROSOMAL MEMBRANES DURING CELL-FREE TRANSLATION. Plant Physiol. 1981 Feb;67(2):205–211. [PMC free article] [PubMed]
  • Laemmli UK. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 1970 Aug 15;227(5259):680–685. [PubMed]
  • Larkins BA, Davies E. Polyribosomes from Peas: V. An Attempt to Characterize the Total Free and Membrane-bound Polysomal Population. Plant Physiol. 1975 Apr;55(4):749–756. [PMC free article] [PubMed]
  • Larkins BA, Hurkman WJ. Synthesis and deposition of zein in protein bodies of maize endosperm. Plant Physiol. 1978 Aug;62(2):256–263. [PMC free article] [PubMed]
  • Marcus A, Efron D, Weeks DP. The wheat embryo cell-free system. Methods Enzymol. 1974;30:749–754. [PubMed]
  • Tumer NE, Thanh VH, Nielsen NC. Purification and characterization of mRNA from soybean seeds. Identification of glycinin and beta-conglycinin precursors. J Biol Chem. 1981 Aug 25;256(16):8756–8760. [PubMed]

Articles from Plant Physiology are provided here courtesy of American Society of Plant Biologists


Related citations in PubMed

See reviews...See all...

Cited by other articles in PMC

See all...


Recent Activity

Your browsing activity is empty.

Activity recording is turned off.

Turn recording back on

See more...