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US 8,802,926 B2Granted
Heat stable mutants of starch biosynthesis enzymes
AssigneeUniversity of Florida Research Foundation, Inc.
InventorsL. Curtis Hannah, Thomas W. Greene
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AssigneeUniversity of Florida Research Foundation, Inc.
InventorsL. Curtis Hannah, Thomas W. Greene
Estimating the term…
The subject invention pertains to novel mutant polynucleotide molecules that encode enzymes that have increased heat stability. These polynucleotides, when expressed in plants, result in increased yield in plants grown under conditions of heat stress. The polynucleotide molecules of the subject invention encode maize endosperm ADP glucose pyrophosphorylase (AGP) and soluble starch synthase (SSS) enzyme activities. Plants and plant tissue bred to contain, or transformed with, the mutant polynucleotides, and expressing the polypeptides encoded by the polynucleotides, are also contemplated by the present invention. The subject invention also concerns methods for isolating polynucleotides and polypeptides contemplated within the scope of the invention. Methods for increasing yield in plants grown under conditions of heat stress are also provided.
An isolated polynucleotide encoding a mutant large subunit of a maize, barley, wheat, or rice plant ADP-glucose pyrophosphorylase protein, or a biologically-active fragment or variant of said mutant protein, wherein said mutant protein encoded by said polynucleotide comprises an amino acid mutation at the amino acid corresponding to the histidine at position 333 in the amino acid sequence of a wild type large subunit of ADP-glucose pyrophosphorylase protein of maize, wherein said amino acid corresponding to the histidine at position 333 is substituted with an amino acid that confers heat stability to said protein, and wherein when said mutant large subunit protein is expressed to form a mutant ADP-glucose pyrophosphorylase enzyme, said mutant enzyme, or a biologically-active fragment of said mutant enzyme, exhibits increased heat stability relative to wild type ADP-glucose pyrophosphorylase enzyme.
A method for providing a plant with an ADP-glucose pyrophosphorylase enzyme that exhibits resistance to heat stress conditions, said method comprising incorporating a polynucleotide into the genome of said plant and expressing the protein encoded by said polynucleotide molecule, wherein said polynucleotide encodes a mutant large subunit of a maize, barley, wheat, or rice plant ADP-glucose pyrophosphorylase protein, or a biologically-active fragment or variant of said mutant protein, wherein said mutant protein encoded by said polynucleotide comprises an amino acid mutation at the amino acid corresponding to the histidine at position 333 in the amino acid sequence of a wild type large subunit of ADP-glucose pyrophosphorylase protein of maize, wherein said amino acid corresponding to the histidine at position 333 is substituted with an amino acid that confers heat stability to said protein, and wherein when said mutant large subunit protein is expressed to form a mutant ADP-glucose pyrophosphorylase enzyme, said mutant enzyme, or a biologically-active fragment of said mutant enzyme, exhibits increased heat stability relative to wild type ADP-glucose pyrophosphorylase enzyme.
A plant, plant tissue, or plant seed comprising a polynucleotide encoding a mutant large subunit of a maize, barley, wheat, or rice plant ADP-glucose pyrophosphorylase protein, or a biologically-active fragment or variant of said mutant protein, wherein said mutant protein encoded by said polynucleotide comprises an amino acid mutation at the amino acid corresponding to the histidine at position 333 in the amino acid sequence of a wild type large subunit of ADP-glucose pyrophosphorylase protein of maize, wherein said amino acid corresponding to the histidine at position 333 is substituted with an amino acid that confers heat stability to said protein, and wherein when said mutant large subunit protein is expressed to form a mutant ADP-glucose pyrophosphorylase enzyme, said mutant enzyme, or a biologically-active fragment of said mutant enzyme, exhibits increased heat stability relative to wild type ADP-glucose pyrophosphorylase enzyme.
Dependencies are inferred from the claim text.