MULTIPLE FORMS OF MAIZE ENDOSPERM ADP-GLUCOSE PYROPHOSPHORYLASE AND THEIR CONTROL BY SHRUNKEN-2 AND BRITTLE-2

1 Vegetable Crops Department, Department of Microbiology and Cell Science, University of Florida, Gainesville, Florida 32611
2 Vegetable Crops Department, University of Florida, Gainesville, Florida 32611
3 Department of Biochemistry and Molecular Biology, University of Florida, Gainesville, Florida 32611

Heat-labile and heat stable forms of ADP-glucose pyrophosphorylase were identified in the maize endosperm. The heat-labile form is destroyed by normal electrophoretic conditions. The heat-stable form corresponds to pyrophosphorylase B. In wild type, 96% of the total activity is heat labile. Both forms are reduced in 11 brittle-2 (bt2) and 12 shrunken-2 (sh2) mutants. The heat-labile form is reduced to a greater extent than is the heat-stable form in each of the 23 mutants. Deletion of sh2 abolishes both forms. The original ratio of the two forms is restored after sh2 function is expressed via transposition of Dissociation from sh2. The possible roles of these genes in the control of ADP-glucose pyrophosphorylase are discussed.

Submitted on December 15, 1979
Revised on April 25, 1980




This article has been cited by other articles:


Home page
Plant Physiol.Home page
S. K. Boehlein, J. R. Shaw, J. D. Stewart, and L. C. Hannah
Heat Stability and Allosteric Properties of the Maize Endosperm ADP-Glucose Pyrophosphorylase Are Intimately Intertwined
Plant Physiology, January 1, 2008; 146(1): 289 - 299.
[Abstract] [Full Text] [PDF]


Home page
Plant Physiol.Home page
C. R. L. Linebarger, S. K. Boehlein, A. K. Sewell, J. Shaw, and L. C. Hannah
Heat Stability of Maize Endosperm ADP-Glucose Pyrophosphorylase Is Enhanced by Insertion of a Cysteine in the N Terminus of the Small Subunit
Plant Physiology, December 1, 2005; 139(4): 1625 - 1634.
[Abstract] [Full Text] [PDF]


Home page
Plant CellHome page
N. A. Eckardt
A New Twist on Transposons: The Maize Genome Harbors Helitron Insertion
PLANT CELL, February 1, 2003; 15(2): 293 - 295.
[Full Text] [PDF]


Home page
Proc. Natl. Acad. Sci. USAHome page
E. D. Smidansky, M. Clancy, F. D. Meyer, S. P. Lanning, N. K. Blake, L. E. Talbert, and M. J. Giroux
Enhanced ADP-glucose pyrophosphorylase activity in wheat endosperm increases seed yield
PNAS, February 5, 2002; 99(3): 1724 - 1729.
[Abstract] [Full Text] [PDF]


Home page
Plant Physiol.Home page
S. Lal, J.-H. Choi, J. R. Shaw, and L. C. Hannah
A Splice Site Mutant of Maize Activates Cryptic Splice Sites, Elicits Intron Inclusion and Exon Exclusion, and Permits Branch Point Elucidation
Plant Physiology, October 1, 1999; 121(2): 411 - 418.
[Abstract] [Full Text]


Home page
Plant Physiol.Home page
S. Lal, J.-H. Choi, and L. C. Hannah
The AG Dinucleotide Terminating Introns Is Important but Not Always Required for Pre-mRNA Splicing in the Maize Endosperm
Plant Physiology, May 1, 1999; 120(1): 65 - 72.
[Abstract] [Full Text]


Home page
Proc. Natl. Acad. Sci. USAHome page
T. W. Greene and L. C. Hannah
Enhanced stability of maize endosperm ADP-glucose pyrophosphorylase is gained through mutants that alter subunit interactions
PNAS, October 27, 1998; 95(22): 13342 - 13347.
[Abstract] [Full Text] [PDF]


Home page
Plant CellHome page
T. W. Greene and L. C. Hannah
Maize Endosperm ADP–Glucose Pyrophosphorylase SHRUNKEN2 and BRITTLE2 Subunit Interactions
PLANT CELL, August 1, 1998; 10(8): 1295 - 1306.
[Abstract] [Full Text]