This Article Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via CrossRef Citing Articles via Google Scholar Google Scholar Articles by Larkins, B. A. Articles by Hurkman, W. J. Search for Related Content PubMed PubMed Citation Articles by Larkins, B. A. Articles by Hurkman, W. J. Agricola Articles by Larkins, B. A. Articles by Hurkman, W. J.

Articles

Synthesis and Deposition of Zein in Protein Bodies of Maize Endosperm ¹

Department of Botany and Plant Pathology, Purdue University, West Lafayette, Indiana 47907

The origin of protein bodies in maize (Zea mays L.) endosperm was investigated to determine whether they are formed as highly differentiated organelles or as protein deposits within the rough endoplasmic reticulum. Electron microscopy of developing maize endosperm cells showed that membranes surrounding protein bodies were continuous with rough endoplasmic reticulum membranes. Membranes of protein bodies and rough endoplasmic reticulum both contained cytochrome c reductase activity indicating a similarity between these membranes. Furthermore, the proportion of alcohol-soluble protein synthesized by polyribosomes isolated from protein body or rough endoplasmic reticulum membranes was similar, and the alcohol-soluble or -insoluble proteins showed identical [¹⁴C]leucine labeling. These results demonstrated that protein bodies form simply as deposits within the rough endoplasmic reticulum.

Messenger RNA that directed synthesis of only the smaller molecular weight zein subunit was separated from mRNA that synthesized both subunits by sucrose gradient centrifugation. This result demonstrated that separate but similar sized mRNAs synthesize the major zein components. In vitro translation products of purified mRNAs or polyribosomes were approximately 2,000 daltons larger than native zein proteins, suggesting that the proteins are synthesized as zein precursors. When intact rough endoplasmic reticulum was placed in the in vitro protein synthesis system, proteins corresponding in molecular weight to the native zein proteins were obtained.

This article has been cited by other articles:

				I. Hara-Nishimura, R. Matsushima, T. Shimada, and M. Nishimura Diversity and Formation of Endoplasmic Reticulum-Derived Compartments in Plants. Are These Compartments Specific to Plant Cells? Plant Physiology, November 1, 2004; 136(3): 3435 - 3439. [Full Text] [PDF]

				T. Shimada, K. Fuji, K. Tamura, M. Kondo, M. Nishimura, and I. Hara-Nishimura Vacuolar sorting receptor for seed storage proteins in Arabidopsis thaliana PNAS, December 23, 2003; 100(26): 16095 - 16100. [Abstract] [Full Text] [PDF]

				B. G. Hunter, M. K. Beatty, G. W. Singletary, B. R. Hamaker, B. P. Dilkes, B. A. Larkins, and R. Jung Maize Opaque Endosperm Mutations Create Extensive Changes in Patterns of Gene Expression PLANT CELL, October 1, 2002; 14(10): 2591 - 2612. [Abstract] [Full Text] [PDF]

				A. J. Kinney, R. Jung, and E. M. Herman Cosuppression of the {{alpha}} Subunits of {beta}-Conglycinin in Transgenic Soybean Seeds Induces the Formation of Endoplasmic Reticulum-Derived Protein Bodies PLANT CELL, May 1, 2001; 13(5): 1165 - 1178. [Abstract] [Full Text]

				K. J. Shank, P. Su, I. Brglez, W. F. Boss, R. E. Dewey, and R. S. Boston Induction of Lipid Metabolic Enzymes during the Endoplasmic Reticulum Stress Response in Plants Plant Physiology, May 1, 2001; 126(1): 267 - 277. [Abstract] [Full Text]

				M. J. Chrispeels and E. M. Herman Endoplasmic Reticulum-Derived Compartments Function in Storage and as Mediators of Vacuolar Remodeling via a New Type of Organelle, Precursor Protease Vesicles Plant Physiology, August 1, 2000; 123(4): 1227 - 1234. [Full Text]

				E. L. Kemper, G. C. Neto, F. Papes, K. C. M. Moraes, A. Leite, and P. Arruda The Role of Opaque2 in the Control of Lysine-Degrading Activities in Developing Maize Endosperm PLANT CELL, October 1, 1999; 11(10): 1981 - 1994. [Abstract] [Full Text]

				E. M. Herman and B. A. Larkins Protein Storage Bodies and Vacuoles PLANT CELL, April 1, 1999; 11(4): 601 - 614. [Full Text]

				J de Dios Alche, A. Castro, A Olmedilla, M. Fernandez, R Rodriguez, M Villalba, and M. Rodriguez-Garcia The major olive pollen allergen (Ole e I) shows both gametophytic and sporophytic expression during anther development, and its synthesis and storage takes place in the RER J. Cell Sci., January 8, 1999; 112(15): 2501 - 2509. [Abstract] [PDF]

				K. A. Hadfield, J. K.C. Rose, D. S. Yaver, R. M. Berka, and A. B. Bennett Polygalacturonase Gene Expression in Ripe Melon Fruit Supports a Role for Polygalacturonase in Ripening-Associated Pectin Disassembly Plant Physiology, June 1, 1998; 117(2): 363 - 373. [Abstract] [Full Text]

				I. Hara-Nishimura, T. Shimada, K. Hatano, Y. Takeuchi, and M. Nishimura Transport of Storage Proteins to Protein Storage Vacuoles Is Mediated by Large Precursor-Accumulating Vesicles PLANT CELL, May 1, 1998; 10(5): 825 - 836. [Abstract] [Full Text] [PDF]

				B Hoh, G Hinz, B. Jeong, and D. Robinson Protein storage vacuoles form de novo during pea cotyledon development J. Cell Sci., January 1, 1995; 108(1): 299 - 310. [Abstract] [PDF]