Plant Physiol. Illumina
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
QUICK SEARCH:   [advanced]


     

This Article
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in Web of Science
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via CrossRef
Right arrow Citing Articles via Web of Science (64)
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Bagga, S.
Right arrow Articles by Sengupta-Gopalan, C.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Bagga, S.
Right arrow Articles by Sengupta-Gopalan, C.
Agricola
Right arrow Articles by Bagga, S.
Right arrow Articles by Sengupta-Gopalan, C.

PLANT PHYSIOLOGY , Vol 107, Issue 1 13-23, Copyright © 1995 by American Society of Plant Biologists

CELL BIOLOGY AND SIGNAL TRANSDUCTION

Accumulation of 15-Kilodalton Zein in Novel Protein Bodies in Transgenic Tobacco

S. Bagga, H. Adams, J. D. Kemp and C. Sengupta-Gopalan
Plant Genetic Engineering Laboratory (S.B., J.D.K.), Electron Microscopy Laboratory (H.A.), and Agronomy and Horticulture Department (S.B., C.S.-G.), New Mexico State University, Las Cruces, New Mexico 88003

Zeins, the seed storage proteins of maize, are a group of alcohol-soluble polypeptides of different molecular masses that share a similar amino acid composition but vary in their sulfur amino acid composition. They are synthesized on the rough endoplasmic reticulum (ER) in the endosperm and are stored in ER-derived protein bodies. Our goal is to balance the amino acid composition of the methionine-deficient forage legumes by expressing the sulfur amino acid-rich 15-kD zeins in their leaves. However, it is crucial to know whether this protein would be stable in nonseed tissues of transgenic plants. The major focus of this paper is to compare the accumulation pattern of the 15-kD zein protein with a vacuolar targeted seed protein, [beta]-phaseolin, in nonseed tissues and to determine the basis for its stability/instability. We have introduced the 15-kD zein and bean [beta]-phaseolin-coding sequences behind the 35S cauliflower mosaic virus promoter into tobacco (Nicotiana tabacum) and analyzed the protein's accumulation pattern in different tissues. Our results demonstrate that the 15-kD seed protein is stable not only in seeds but in all nonseed tissues tested, whereas the [beta]-phaseolin protein accumulated only in mid- and postmaturation seeds. Interestingly, zein accumulates in novel protein bodies both in the seeds and in nonseed tissues. We attribute the instability of the [beta]-phaseolin protein in nonseed tissues to the fact that it is targeted to protease-rich vacuoles. The stability of the 15-kD zein could be attributed to its retention in the ER or to the protease-resistant nature of the protein.


This article has been cited by other articles:


Home page
 J Exp BotHome page
Y. Saito, K. Kishida, K. Takata, H. Takahashi, T. Shimada, K. Tanaka, S. Morita, S. Satoh, and T. Masumura
A green fluorescent protein fused to rice prolamin forms protein body-like structures in transgenic rice
J. Exp. Bot., February 1, 2009; 60(2): 615 - 627.
[Abstract] [Full Text] [PDF]

Home page
 Plant CellHome page
K. Yamada, A. J. Nagano, M. Nishina, I. Hara-Nishimura, and M. Nishimura
NAI2 Is an Endoplasmic Reticulum Body Component That Enables ER Body Formation in Arabidopsis thaliana
PLANT CELL, September 1, 2008; 20(9): 2529 - 2540.
[Abstract] [Full Text] [PDF]

Home page
 Plant CellHome page
D. R. Holding, M. S. Otegui, B. Li, R. B. Meeley, T. Dam, B. G. Hunter, R. Jung, and B. A. Larkins
The Maize Floury1 Gene Encodes a Novel Endoplasmic Reticulum Protein Involved in Zein Protein Body Formation
PLANT CELL, August 1, 2007; 19(8): 2569 - 2582.
[Abstract] [Full Text] [PDF]

Home page
 Plant CellHome page
A. Pompa and A. Vitale
Retention of a Bean Phaseolin/Maize {gamma}-Zein Fusion in the Endoplasmic Reticulum Depends on Disulfide Bond Formation
PLANT CELL, October 1, 2006; 18(10): 2608 - 2621.
[Abstract] [Full Text] [PDF]

Home page
 Mol. Interv.Home page
A. Vitale and E. Pedrazzini
Recombinant Pharmaceuticals from Plants: The Plant Endomembrane System as Bioreactor
Mol. Interv., August 1, 2005; 5(4): 216 - 225.
[Abstract] [Full Text] [PDF]

Home page
 J Exp BotHome page
M. Bellucci, F. De Marchis, R. Mannucci, R. Bock, and S. Arcioni
Cytoplasm and chloroplasts are not suitable subcellular locations for {beta}-zein accumulation in transgenic plants
J. Exp. Bot., April 1, 2005; 56(414): 1205 - 1212.
[Abstract] [Full Text] [PDF]

Home page
 Plant Physiol.Home page
D. Mainieri, M. Rossi, M. Archinti, M. Bellucci, F. De Marchis, S. Vavassori, A. Pompa, S. Arcioni, and A. Vitale
Zeolin. A New Recombinant Storage Protein Constructed Using Maize {gamma}-Zein and Bean Phaseolin
Plant Physiology, November 1, 2004; 136(3): 3447 - 3456.
[Abstract] [Full Text] [PDF]

Home page
 Plant Cell PhysiolHome page
C. E. Coleman, P. R. Yoho, S. Escobar, and M. Ogawa
The Accumulation of {alpha}-Zein in Transgenic Tobacco Endosperm is Stabilized by Co-expression of {beta}-Zein
Plant Cell Physiol., July 15, 2004; 45(7): 864 - 871.
[Abstract] [Full Text] [PDF]

Home page
 Plant Physiol.Home page
M. Park, S. J. Kim, A. Vitale, and I. Hwang
Identification of the Protein Storage Vacuole and Protein Targeting to the Vacuole in Leaf Cells of Three Plant Species
Plant Physiology, February 1, 2004; 134(2): 625 - 639.
[Abstract] [Full Text] [PDF]

Home page
 J Exp BotHome page
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]

Home page
 Plant Physiol.Home page
E. Torres, P. Gonzalez-Melendi, E. Stoger, P. Shaw, R. M. Twyman, L. Nicholson, C. Vaquero, R. Fischer, P. Christou, and Y. Perrin
Native and Artificial Reticuloplasmins Co-Accumulate in Distinct Domains of the Endoplasmic Reticulum and in Post-Endoplasmic Reticulum Compartments
Plant Physiology, November 1, 2001; 127(3): 1212 - 1223.
[Abstract] [Full Text] [PDF]

Home page
 Plant CellHome page
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]

Home page
 Plant Physiol.Home page
E. Stöger, M. Parker, P. Christou, and R. Casey
Pea Legumin Overexpressed in Wheat Endosperm Assembles into an Ordered Paracrystalline Matrix
Plant Physiology, April 1, 2001; 125(4): 1732 - 1742.
[Abstract] [Full Text]

Home page
 Plant Physiol.Home page
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]

Home page
 Plant Physiol.Home page
A. Goossens, W. Dillen, J. De Clercq, M. Van Montagu, and G. Angenon
The arcelin-5 Gene of Phaseolus vulgaris Directs High Seed-Specific Expression in Transgenic Phaseolus acutifolius and Arabidopsis Plants
Plant Physiology, August 1, 1999; 120(4): 1095 - 1104.
[Abstract] [Full Text]

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


HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
ASPB Publications PLANT PHYSIOLOGY® THE PLANT CELL
Copyright © 1995 by the American Society of Plant Biologists