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


     

This Article
Right arrow Full Text
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 (46)
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Cao, H.
Right arrow Articles by Myers, A. M.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Cao, H.
Right arrow Articles by Myers, A. M.
Agricola
Right arrow Articles by Cao, H.
Right arrow Articles by Myers, A. M.

Identification of the Soluble Starch Synthase Activities of Maize Endosperm1

Heping Cao, Jennifer Imparl-Radosevich, Hanping Guan, Peter L. Keeling, Martha G. James, and Alan M. Myers*

Department of Biochemistry, Biophysics, and Molecular Biology, Iowa State University, Ames, Iowa 50011 (H.C., M.G.J., A.M.M.); and ExSeed Genetics, L.L.C., and Department of Agronomy, Food Sciences Building, Iowa State University, Ames, Iowa 50011 (J.I.-P., H.G., P.L.K.)

This study identified the complement of soluble starch synthases (SSs) present in developing maize (Zea mays) endosperm. The product of the du1 gene, DU1, was shown to be one of the two major soluble SSs. The C-terminal 450 residues of DU1 comprise eight sequence blocks conserved in 28 known or predicted glucan synthases. This region of DU1 was expressed in Escherichia coli and shown to possess SS activity. DU1-specific antisera detected a soluble endosperm protein of more than 200 kD that was lacking in du1- mutants. These antisera eliminated 20% to 30% of the soluble SS activity from kernel extracts. Antiserum against the isozyme zSSI eliminated approximately 60% of the total soluble SS, and immunodepletion of du1- mutant extracts with this antiserum nearly eliminated SS activity. Two soluble SS activities were identified by electrophoretic fractionation, each of which correlated specifically with zSSI or DU1. Thus, DU1 and zSSI accounted for the great majority of soluble SS activity present in developing endosperm. The relative activity of the two isozymes did not change significantly during the starch biosynthetic period. DU1 and zSSI may be interdependent, because mutant extracts lacking DU1 exhibited a significant stimulation of the remaining SS activity.

1   This work was supported by the U.S. Department of Agriculture (grant no. 96-35300-3779 to A.M.M. and M.G.J.) and the National Science Foundation (grant no. DIR-9113593 to the Iowa State University Signal Transduction Training Group). This is journal paper no. J-18330 of project no. 3197 of the Iowa Agriculture and Home Economics Experiment Station (Ames). This paper is dedicated to the memory of Dr. Bruce Wasserman.
*   Corresponding author; e-mail ammyers{at}iastate.edu; fax 1-515-294-0453.

Plant Physiol. (1999) 120: 205-216
Copyright Clearance Center:   0032-0889/99/120//12
© 1999 American Society of Plant Physiologists




This article has been cited by other articles:


Home page
 Plant Physiol.Home page
T. A. Hennen-Bierwagen, Q. Lin, F. Grimaud, V. Planchot, P. L. Keeling, M. G. James, and A. M. Myers
Proteins from Multiple Metabolic Pathways Associate with Starch Biosynthetic Enzymes in High Molecular Weight Complexes: A Model for Regulation of Carbon Allocation in Maize Amyloplasts
Plant Physiology, March 1, 2009; 149(3): 1541 - 1559.
[Abstract] [Full Text] [PDF]

Home page
 J Exp BotHome page
F. Grimaud, H. Rogniaux, M. G. James, A. M. Myers, and V. Planchot
Proteome and phosphoproteome analysis of starch granule-associated proteins from normal maize and mutants affected in starch biosynthesis
J. Exp. Bot., September 1, 2008; 59(12): 3395 - 3406.
[Abstract] [Full Text] [PDF]

Home page
 Plant Physiol.Home page
T. A. Hennen-Bierwagen, F. Liu, R. S. Marsh, S. Kim, Q. Gan, I. J. Tetlow, M. J. Emes, M. G. James, and A. M. Myers
Starch Biosynthetic Enzymes from Developing Maize Endosperm Associate in Multisubunit Complexes
Plant Physiology, April 1, 2008; 146(4): 1892 - 1908.
[Abstract] [Full Text] [PDF]

Home page
 Plant Physiol.Home page
N. Fujita, M. Yoshida, T. Kondo, K. Saito, Y. Utsumi, T. Tokunaga, A. Nishi, H. Satoh, J.-H. Park, J.-L. Jane, et al.
Characterization of SSIIIa-Deficient Mutants of Rice: The Function of SSIIIa and Pleiotropic Effects by SSIIIa Deficiency in the Rice Endosperm
Plant Physiology, August 1, 2007; 144(4): 2009 - 2023.
[Abstract] [Full Text] [PDF]

Home page
 Plant Physiol.Home page
N. Fujita, M. Yoshida, N. Asakura, T. Ohdan, A. Miyao, H. Hirochika, and Y. Nakamura
Function and Characterization of Starch Synthase I Using Mutants in Rice
Plant Physiology, March 1, 2006; 140(3): 1070 - 1084.
[Abstract] [Full Text] [PDF]

Home page
 J Exp BotHome page
T. Ohdan, P. B. Francisco Jr, T. Sawada, T. Hirose, T. Terao, H. Satoh, and Y. Nakamura
Expression profiling of genes involved in starch synthesis in sink and source organs of rice
J. Exp. Bot., December 1, 2005; 56(422): 3229 - 3244.
[Abstract] [Full Text] [PDF]

Home page
 J Exp BotHome page
W. Dian, H. Jiang, and P. Wu
Evolution and expression analysis of starch synthase III and IV in rice
J. Exp. Bot., February 1, 2005; 56(412): 623 - 632.
[Abstract] [Full Text] [PDF]

Home page
 Plant CellHome page
J. R. Dinges, C. Colleoni, M. G. James, and A. M. Myers
Mutational Analysis of the Pullulanase-Type Debranching Enzyme of Maize Indicates Multiple Functions in Starch Metabolism
PLANT CELL, March 1, 2003; 15(3): 666 - 680.
[Abstract] [Full Text] [PDF]

Home page
 Proc. Natl. Acad. Sci. USAHome page
P. C. Sehnke, H.-J. Chung, K. Wu, and R. J. Ferl
Regulation of starch accumulation by granule-associated plant 14-3-3 proteins
PNAS, January 5, 2001; (2001) 21304198.
[Abstract] [Full Text]

Home page
 Plant Physiol.Home page
Z. Li, G. Mouille, B. Kosar-Hashemi, S. Rahman, B. Clarke, K. R. Gale, R. Appels, and M. K. Morell
The Structure and Expression of the Wheat Starch Synthase III Gene. Motifs in the Expressed Gene Define the Lineage of the Starch Synthase III Gene Family
Plant Physiology, June 1, 2000; 123(2): 613 - 624.
[Abstract] [Full Text]

Home page
 Plant Physiol.Home page
A. M. Myers, M. K. Morell, M. G. James, and S. G. Ball
Recent Progress toward Understanding Biosynthesis of the Amylopectin Crystal
Plant Physiology, April 1, 2000; 122(4): 989 - 998.
[Full Text]

Home page
 Plant Physiol.Home page
P. L. Vrinten and T. Nakamura
Wheat Granule-Bound Starch Synthase I and II Are Encoded by Separate Genes That Are Expressed in Different Tissues
Plant Physiology, January 1, 2000; 122(1): 255 - 264.
[Abstract] [Full Text] [PDF]

Home page
 Proc. Natl. Acad. Sci. USAHome page
P. C. Sehnke, H.-J. Chung, K. Wu, and R. J. Ferl
Regulation of starch accumulation by granule-associated plant 14-3-3 proteins
PNAS, January 16, 2001; 98(2): 765 - 770.
[Abstract] [Full Text] [PDF]

Home page
 Plant Physiol.Home page
B.-s. Seo, S. Kim, M. P. Scott, G. W. Singletary, K.-s. Wong, M. G. James, and A. M. Myers
Functional Interactions between Heterologously Expressed Starch-Branching Enzymes of Maize and the Glycogen Synthases of Brewer's Yeast
Plant Physiology, April 1, 2002; 128(4): 1189 - 1199.
[Abstract] [Full Text] [PDF]


HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
ASPB Publications PLANT PHYSIOLOGY® THE PLANT CELL
Copyright © 1999 by the American Society of Plant Biologists