Plant Physiol.
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 (29)
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Burton, R. A.
Right arrow Articles by Fincher, G. B.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Burton, R. A.
Right arrow Articles by Fincher, G. B.
Agricola
Right arrow Articles by Burton, R. A.
Right arrow Articles by Fincher, G. B.

A Single Limit Dextrinase Gene Is Expressed Both in the Developing Endosperm and in Germinated Grains of Barley1

Rachel A. Burton2, Xiao-Qi Zhang2, Maria Hrmova, and Geoffrey B. Fincher*

Department of Plant Science, University of Adelaide, Waite Campus, Glen Osmond, South Australia 5064, Australia

The single gene encoding limit dextrinase (pullulan 6-glucanohydrolase; EC 3.2.1.41) in barley (Hordeum vulgare) has 26 introns that range in size from 93 to 822 base pairs. The mature polypeptide encoded by the gene has 884 amino acid residues and a calculated molecular mass of 97,417 D. Limit dextrinase mRNA is abundant in gibberellic acid-treated aleurone layers and in germinated grain. Gibberellic acid response elements were found in the promoter region of the gene. These observations suggest that the enzyme participates in starch hydrolysis during endosperm mobilization in germinated grain. The mRNA encoding the enzyme is present at lower levels in the developing endosperm of immature grain, a location consistent with a role for limit dextrinase in starch synthesis. Enzyme activity was also detected in developing grain. The limit dextrinase has a presequence typical of transit peptides that target nascent polypeptides to amyloplasts, but this would not be expected to direct secretion of the mature enzyme from aleurone cells in germinated grain. It remains to be discovered how the enzyme is released from the aleurone and whether another enzyme, possibly of the isoamylase group, might be equally important for starch hydrolysis in germinated grain.


1   This work was supported by a grant from the South East Australian Malting Barley Quality Improvement Program, which includes contributions from Joe White Maltings, the Grains Research and Development Corporation, the Strategic Research Foundation, Barrett-Burston International, the Australian Associated Brewers, and the Adelaide Malting Company.
2   These two authors contributed equally to this work.
*   Corresponding author; e-mail gfincher{at}waite.adelaide.edu.au; fax 61-8-8303-7109.

Plant Physiol. (1999) 119: 859-872
Copyright Clearance Center:   0032-0889/99/119//14
© 1999 American Society of Plant Physiologists




This article has been cited by other articles:


Home page
Plant Physiol.Home page
V. V. Radchuk, L. Borisjuk, N. Sreenivasulu, K. Merx, H.-P. Mock, H. Rolletschek, U. Wobus, and W. Weschke
Spatiotemporal Profiling of Starch Biosynthesis and Degradation in the Developing Barley Grain
Plant Physiology, May 1, 2009; 150(1): 190 - 204.
[Abstract] [Full Text] [PDF]


Home page
J Exp BotHome page
L. Li, H. Ilarslan, M. G. James, A. M. Myers, and E. S. Wurtele
Genome wide co-expression among the starch debranching enzyme genes AtISA1, AtISA2, and AtISA3 in Arabidopsis thaliana
J. Exp. Bot., September 20, 2007; (2007) erm180v1.
[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
Plant Physiol.Home page
R. A. Burton, P. E. Johnson, D. M. Beckles, G. B. Fincher, H. L. Jenner, M. J. Naldrett, and K. Denyer
Characterization of the Genes Encoding the Cytosolic and Plastidial Forms of ADP-Glucose Pyrophosphorylase in Wheat Endosperm
Plant Physiology, November 1, 2002; 130(3): 1464 - 1475.
[Abstract] [Full Text] [PDF]


Home page
Plant CellHome page
R. A. Burton, D. M. Gibeaut, A. Bacic, K. Findlay, K. Roberts, A. Hamilton, D. C. Baulcombe, and G. B. Fincher
Virus-Induced Silencing of a Plant Cellulose Synthase Gene
PLANT CELL, May 1, 2000; 12(5): 691 - 706.
[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 HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
ASPB Publications PLANT PHYSIOLOGY® THE PLANT CELL
Copyright © 1999 by the American Society of Plant Biologists