IAA2 Protein Degron Deletion for Synthetic Auxin Herbicide Tolerance

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Solution Overview

Problem

The intensive use of synthetic auxin herbicides has led to the evolution of herbicide resistance in weeds, with 39 weed species developing resistance to one or more synthetic auxin herbicides, limiting their efficacy in agricultural settings.

Innovation Solution

Deleting or disrupting the degron tail region of the IAA2 protein in plants confers increased tolerance to synthetic auxin herbicides, including 2,4-D, by altering the protein's interaction with herbicides and reducing its degradation.

Engineering Contradictions & Design Principles

VSEngineering Contradiction Analysis

1Reliability

If synthetic auxin herbicides are intensively used to control weeds, then weed control effectiveness is improved, but herbicide resistance evolves in weed populations

Engineering Contradiction:
Improveherbicide control effectivenessVSAvoidherbicide resistance evolution
Core Design Contradiction:
ReliabilityVSAdaptability or versatility

Solution Approach 1:

Instead of trying to prevent resistance evolution through reduced herbicide use, the invention inverts the approach by genetically modifying the target protein (IAA2) in crops to alter its herbicide binding properties. This molecular inversion allows crops to survive herbicide applications that would normally kill them, effectively reversing the vulnerability-culnerability relationship between crop and weed to crop-resistance and weed-sensitivity.

Inventive Principle:
Principle #13The other way round (Inversion)

Solution Approach 2:

The invention changes the molecular parameters of the IAA2 protein by deleting or disrupting the degron tail region. This parameter change modifies the protein's interaction with synthetic auxin herbicides, altering its degradation rate and conferring herbicide tolerance. The specific amino acid sequence modification (deletion of degron tail) directly changes the biochemical parameters that determine herbicide sensitivity.

Inventive Principle:
Principle #35Parameter changes

2Reliability

If the degron tail region of IAA2 protein is deleted or disrupted to confer herbicide tolerance, then plant survival under herbicide application is improved, but protein stability and normal auxin response may be affected

Engineering Contradiction:
Improveplant survival under herbicide stressVSAvoidIAA2 protein stability
Core Design Contradiction:
ReliabilityVSStability of the object's composition

Solution Approach 1:

The invention extracts or removes the specific degron tail region from the IAA2 protein sequence. This extraction of the harmful element (the region responsible for rapid degradation upon herbicide binding) allows the rest of the protein to maintain its function while conferring herbicide tolerance. The degron tail is taken out selectively without removing the entire protein or its essential domains.

Inventive Principle:
Principle #2Taking out (Extraction)

Solution Approach 2:

The invention applies local quality modification by specifically altering only the degron tail region of the IAA2 protein while leaving the rest of the protein structure intact. This localized change affects only the herbicide binding and degradation aspects of the protein, while preserving other critical functions such as auxin response regulation in the remaining protein domains.

Inventive Principle:
Principle #3Local quality

3Reliability

If herbicide tolerant plants are produced through genetic modification, then crop survival under herbicide application is improved, but complexity of genetic engineering and regulation is increased

Engineering Contradiction:
Improvecrop herbicide toleranceVSAvoidgenetic modification complexity
Core Design Contradiction:
ReliabilityVSDevice complexity

Solution Approach 1:

The invention uses a simple, straightforward genetic modification approach that deletes or disrupts a specific region (degron tail) of the IAA2 gene. This simplified molecular design makes the genetic engineering more tractable and potentially cheaper compared to more complex transgenic approaches. The modification is essentially a targeted deletion rather than requiring complex transgene insertion or multiple gene edits.

Inventive Principle:
Principle #27Cheap short-living objects (Disposable)

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 modification results in plants that are significantly more resistant to synthetic auxin herbicides, allowing them to survive applications that would otherwise be lethal, thereby maintaining herbicide effectiveness in controlling weeds.

Implementation Method 1

Auxin interacts with both TIR1/AFB and the transcriptional repressor protein Aux/IAA. This leads to ubiquitination of the Aux/IAA protein, signaling the 26s proteasome to degrade the Aux/IAA protein

Methodology Applied
Scientific EffectProtein-protein interaction:

Implementation Method 2

This leads to ubiquitination of the Aux/IAA protein, signaling the 26s proteasome to degrade the Aux/IAA protein

Methodology Applied
Scientific EffectUbiquitination:

Implementation Method 3

This leads to ubiquitination of the Aux/IAA protein, signaling the 26s proteasome to degrade the Aux/IAA protein

Methodology Applied
Scientific EffectProteasome degradation:

Data Source

PatentUS20250179515A1Herbicide tolerant plants and production and detection of same
Publication Date: 2025.06.05 COLORADO STATE UNIV RES FOUND
  • US20250179515A1 patent drawing
  • US20250179515A1 patent drawing
  • US20250179515A1 patent drawing

AI summary

The present invention refers to a plant or plant part comprising a polynucleotide encoding an herbicide tolerant IAA2 polypeptide having a deleted or disrupted degron tail region, the expression of said polynucleotide confers to the plant or plant part tolerance to synthetic auxin herbicides, such as 2,4-D. The present invention relates to methods and plants and that have a deleted or disrupted degron tail region of the IAA2 protein obtained by gene editing, transformation, mutagenesis, breeding, and the like.