Mutated TriA Enzyme Herbicide Tolerance in Plants
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Solution Overview
Problem
Current methods for making plants tolerant to herbicides are limited in effectively conferring resistance to herbicides that inhibit cellulose biosynthesis, such as azines, as existing strategies do not provide sufficient tolerance or are not efficient in detoxifying these specific herbicides.
Innovation Solution
Introduction of bacterial genes encoding mutated TriA polypeptides that biodegrade herbicides, specifically engineered to maintain or enhance amidohydrolase activity and expand substrate acceptance, allowing for over-expression in plants to confer tolerance to herbicides like azines.
Engineering Contradictions & Design Principles
Engineering Contradiction Analysis
1Reliability
If existing herbicide tolerance methods are used, then general herbicide resistance is achieved, but tolerance to cellulose biosynthesis inhibitors (azines) is insufficient
Solution Approach 1:
The patent applies parameter changes by mutating specific amino acid residues in the TriA enzyme (e.g., expanding the enzyme pocket through mutagenesis) to alter its substrate binding properties. This enables the enzyme to accept bulkier azine herbicides while maintaining catalytic activity, thereby resolving the contradiction between herbicide tolerance and substrate acceptance versatility
Solution Approach 2:
The engineered TriA enzyme achieves universality by being able to degrade multiple types of herbicides including both traditional substrates and bulkier azine compounds. The mutated enzyme maintains its original amidohydrolase activity while gaining expanded substrate acceptance, making it a multi-functional detoxification system
2Reliability
If bacterial genes encoding TriA are introduced, then herbicide detoxification capability is enhanced, but enzyme pocket size limits substrate acceptance of bulkier herbicides
Solution Approach 1:
The patent uses site-directed mutagenesis to change specific amino acid parameters in the TriA enzyme structure, particularly expanding the enzyme pocket volume and altering residue compositions. This enables the enzyme to accommodate bulkier azine herbicides while preserving catalytic efficiency, thereby reducing herbicide toxicity through enhanced detoxification
Solution Approach 2:
The patent converts the harmful effect of azine herbicides into a benefit by engineering the TriA enzyme to specifically target and degrade these compounds. The mutated enzyme transforms toxic azines into non-toxic degradation products, turning the previously problematic bulkier substrates into manageable targets for detoxification
Applied Scientific Principles
This section explains which scientific principles are used to turn an abstract innovation direction into a practical engineering solution.
Function Achieved in This Case
The expression of mutated TriA polypeptides in plants significantly increases tolerance to herbicides, enabling plants to withstand herbicide applications that would typically inhibit growth or be toxic, thereby improving weed control without harming crop plants.
Implementation Method 1
bacterial genes encoding mutated TriA polypeptides that biodegrade herbicides, specifically engineered to maintain or enhance amidohydrolase activity
Implementation Method 2
The amidohydrolase superfamily comprises a remarkable set of enzymes that catalyze the hydrolysis of a wide range of substrates bearing amide or ester functional groups
Data Source
AI summary
The present invention refers to a plant or plant part comprising a polynucleotide encoding a mutated TriA polypeptide, the expression of said polynucleotide confers to the plant or plant part tolerance to herbicides.