Formation of wheat protein bodies: Involvement of the Golgi apparatus in gliadin transport |
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Authors: | Woo Taek Kim Vincent R Franceschi Hari B Krishnan Thomas W Okita |
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Institution: | (1) Graduate Program in Plant Physiology, Washington State University, 99164-6340 Pullman, WA, USA;(2) Department of Botany, Washington State University, 99164-6340 Pullman, WA, USA;(3) Institute of Biological Chemistry, Washington State University, 99164-6340 Pullman, WA, USA;(4) Present address: Department of Plant Pathology, University of Missouri, 108 Waters Hall, 65211 Columbia, MO, USA |
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Abstract: | Developing wheat (Triticum aestivum L.) endosperm was examined using ultrathin sections prepared from tissues harvested at 5, 9, 16 and 25 d after flowering. Protein bodies were evident by 9 d and displayed a variety of membranous structures and inclusions. The Golgi apparatus was a prominent organelle at all stages, and by 9 d was associated with small electron-dense inclusions. By immunocytochemical techniques, gliadin (wheat prolamine) was localized within these vesicles and in homogeneous regions of protein bodies, but not in the lumen of the rough endoplasmic reticulum. The protein bodies appear to enlarge by fusion of smaller protein bodies resulting in larger, irregular-shaped organelles. The affinity of the Golgi-derived vesicles for gliadin-specific probes during the period of maximal storage-protein synthesis and deposition indicates that this organelle includes the bulk, if not all, of the gliadin produced. The involvement of the Golgi apparatus in the packaging of gliadins into protein bodies indicates a pathway which differs from the mode of prolamine deposition in other cereals such as maize, rice and sorghum, and resembles the mechanism employed for the storage of rice glutelin and legume globulins.Abbreviations ER
endoplasmic reticulum
- IgG
immunoglobulin G
- DAF
days after flowering |
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Keywords: | Gliadin Golgi apparatus Protein deposition Storage protein Triticum (protein bodies) |
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