Source 1primary paper2019eScholarship (California Digital Library)
Toolkit/PACE
PACE
Also known as: PACE, Phage Assisted Continuous Evolution
Taxonomy: Technique Branch / Method. Workflows sit above the mechanism and technique branches rather than replacing them.
Summary
PACE (Phage Assisted Continuous Evolution) is an engineering method used in this study to evolve cryptochrome properties. In the cited work, it was applied to increase the dynamic range of the blue-light-dependent interaction between Arabidopsis thaliana CRY2 and BIC1.
Usefulness & Problems
Why this is useful
This method is useful for engineering light-responsive protein behavior, as evidenced by its use to improve the dynamic range of the CRY2-BIC1 interaction. The supplied evidence does not provide broader performance comparisons or operational details beyond this application.
Source:
Chapter 3 focused on the development of a novel pair of blue-light-dependent interacting proteins: CRY2-BIC1
Problem solved
PACE was used here to address the problem of insufficient dynamic range in the blue-light-dependent interaction between Arabidopsis thaliana CRY2 and BIC1. This supports its role as a protein engineering approach for optimizing cryptochrome-based optogenetic interactions.
Source:
Chapter 3 focused on the development of a novel pair of blue-light-dependent interacting proteins: CRY2-BIC1
Taxonomy & Function
Primary hierarchy
Technique Branch
Method: A concrete method used to build, optimize, or evolve an engineered system.
Mechanisms
directed evolutionTarget processes
editingrecombinationImplementation Constraints
The available evidence identifies PACE as Phage Assisted Continuous Evolution and places its use in cryptochrome engineering. No practical details are provided here on phage system design, selection linkage, expression host, construct architecture, or culture conditions.
The supplied evidence is limited to a single study context and one reported outcome. It does not include experimental setup, selection architecture, mutation rates, host system, or evidence for generalizability beyond CRY2-BIC1 engineering.
Validation
Cell-freeBacteriaMammalianMouseHumanTherapeuticIndep. Replication
Supporting Sources
Source 2primary paper2026MED
Ranked Claims
Next-generation countermeasures for Bt resistance include synergistic Cry/Vip pyramiding, CRISPR/Cas9-validated receptor knockouts revealing functional redundancy, Domain III chimerization, PACE, and AlphaFold3-guided rational redesign.
Countermeasures now integrate synergistic Cry/Vip pyramiding, CRISPR/Cas9-validated receptor knockouts revealing functional redundancy, Domain III chimerization (e.g., Cry1A.105), phage-assisted continuous evolution (PACE), and the emerging application of AlphaFold3 for structure-guided rational redesign of resistance-breaking variants.
Universally conserved residues required for stable protein expression of Arabidopsis CRY2 in plants were not similarly required for stable protein expression of human hCRY1 in human cells.
I found that UCRs required for stable protein expression of CRY2 in plants are not similarly required for stable protein expression of human hCRY1 in human cells.
Universally conserved residues required for stable protein expression of Arabidopsis CRY2 in plants were not similarly required for stable protein expression of human hCRY1 in human cells.
I found that UCRs required for stable protein expression of CRY2 in plants are not similarly required for stable protein expression of human hCRY1 in human cells.
Universally conserved residues required for stable protein expression of Arabidopsis CRY2 in plants were not similarly required for stable protein expression of human hCRY1 in human cells.
I found that UCRs required for stable protein expression of CRY2 in plants are not similarly required for stable protein expression of human hCRY1 in human cells.
Universally conserved residues required for stable protein expression of Arabidopsis CRY2 in plants were not similarly required for stable protein expression of human hCRY1 in human cells.
I found that UCRs required for stable protein expression of CRY2 in plants are not similarly required for stable protein expression of human hCRY1 in human cells.
Universally conserved residues required for stable protein expression of Arabidopsis CRY2 in plants were not similarly required for stable protein expression of human hCRY1 in human cells.
I found that UCRs required for stable protein expression of CRY2 in plants are not similarly required for stable protein expression of human hCRY1 in human cells.
Universally conserved residues required for stable protein expression of Arabidopsis CRY2 in plants were not similarly required for stable protein expression of human hCRY1 in human cells.
I found that UCRs required for stable protein expression of CRY2 in plants are not similarly required for stable protein expression of human hCRY1 in human cells.
Universally conserved residues required for stable protein expression of Arabidopsis CRY2 in plants were not similarly required for stable protein expression of human hCRY1 in human cells.
I found that UCRs required for stable protein expression of CRY2 in plants are not similarly required for stable protein expression of human hCRY1 in human cells.
PACE was applied to increase the dynamic range of the CRY2-BIC1 blue-light-dependent interaction.
applied PACE (Phage Assisted Continuous Evolution) to increase the dynamic range of CRY2-BIC1 blue-light dependent interaction
PACE was applied to increase the dynamic range of the CRY2-BIC1 blue-light-dependent interaction.
applied PACE (Phage Assisted Continuous Evolution) to increase the dynamic range of CRY2-BIC1 blue-light dependent interaction
PACE was applied to increase the dynamic range of the CRY2-BIC1 blue-light-dependent interaction.
applied PACE (Phage Assisted Continuous Evolution) to increase the dynamic range of CRY2-BIC1 blue-light dependent interaction
PACE was applied to increase the dynamic range of the CRY2-BIC1 blue-light-dependent interaction.
applied PACE (Phage Assisted Continuous Evolution) to increase the dynamic range of CRY2-BIC1 blue-light dependent interaction
PACE was applied to increase the dynamic range of the CRY2-BIC1 blue-light-dependent interaction.
applied PACE (Phage Assisted Continuous Evolution) to increase the dynamic range of CRY2-BIC1 blue-light dependent interaction
PACE was applied to increase the dynamic range of the CRY2-BIC1 blue-light-dependent interaction.
applied PACE (Phage Assisted Continuous Evolution) to increase the dynamic range of CRY2-BIC1 blue-light dependent interaction
PACE was applied to increase the dynamic range of the CRY2-BIC1 blue-light-dependent interaction.
applied PACE (Phage Assisted Continuous Evolution) to increase the dynamic range of CRY2-BIC1 blue-light dependent interaction
The study experimentally analyzed 51 universally conserved residues of Arabidopsis thaliana CRY2 that are conserved in eukaryotic cryptochromes from Arabidopsis to human.
In Chapter 2, I experimentally analyzed 51 UCRs of Arabidopsis CRY2 that are universally conserved in eukaryotic cryptochromes from Arabidopsis to human.
UCRs analyzed 51
The study experimentally analyzed 51 universally conserved residues of Arabidopsis thaliana CRY2 that are conserved in eukaryotic cryptochromes from Arabidopsis to human.
In Chapter 2, I experimentally analyzed 51 UCRs of Arabidopsis CRY2 that are universally conserved in eukaryotic cryptochromes from Arabidopsis to human.
UCRs analyzed 51
The study experimentally analyzed 51 universally conserved residues of Arabidopsis thaliana CRY2 that are conserved in eukaryotic cryptochromes from Arabidopsis to human.
In Chapter 2, I experimentally analyzed 51 UCRs of Arabidopsis CRY2 that are universally conserved in eukaryotic cryptochromes from Arabidopsis to human.
UCRs analyzed 51
The study experimentally analyzed 51 universally conserved residues of Arabidopsis thaliana CRY2 that are conserved in eukaryotic cryptochromes from Arabidopsis to human.
In Chapter 2, I experimentally analyzed 51 UCRs of Arabidopsis CRY2 that are universally conserved in eukaryotic cryptochromes from Arabidopsis to human.
UCRs analyzed 51
The study experimentally analyzed 51 universally conserved residues of Arabidopsis thaliana CRY2 that are conserved in eukaryotic cryptochromes from Arabidopsis to human.
In Chapter 2, I experimentally analyzed 51 UCRs of Arabidopsis CRY2 that are universally conserved in eukaryotic cryptochromes from Arabidopsis to human.
UCRs analyzed 51
The study experimentally analyzed 51 universally conserved residues of Arabidopsis thaliana CRY2 that are conserved in eukaryotic cryptochromes from Arabidopsis to human.
In Chapter 2, I experimentally analyzed 51 UCRs of Arabidopsis CRY2 that are universally conserved in eukaryotic cryptochromes from Arabidopsis to human.
UCRs analyzed 51
The study experimentally analyzed 51 universally conserved residues of Arabidopsis thaliana CRY2 that are conserved in eukaryotic cryptochromes from Arabidopsis to human.
In Chapter 2, I experimentally analyzed 51 UCRs of Arabidopsis CRY2 that are universally conserved in eukaryotic cryptochromes from Arabidopsis to human.
UCRs analyzed 51
The study developed soluble expression PACE and protein-dissociating PACE to facilitate further engineering of CRY2.
developed soluble expression and protein-dissociating PACE to facilitate further engineering of CRY2
The study developed soluble expression PACE and protein-dissociating PACE to facilitate further engineering of CRY2.
developed soluble expression and protein-dissociating PACE to facilitate further engineering of CRY2
The study developed soluble expression PACE and protein-dissociating PACE to facilitate further engineering of CRY2.
developed soluble expression and protein-dissociating PACE to facilitate further engineering of CRY2
The study developed soluble expression PACE and protein-dissociating PACE to facilitate further engineering of CRY2.
developed soluble expression and protein-dissociating PACE to facilitate further engineering of CRY2
The study developed soluble expression PACE and protein-dissociating PACE to facilitate further engineering of CRY2.
developed soluble expression and protein-dissociating PACE to facilitate further engineering of CRY2
The study developed soluble expression PACE and protein-dissociating PACE to facilitate further engineering of CRY2.
developed soluble expression and protein-dissociating PACE to facilitate further engineering of CRY2
The study developed soluble expression PACE and protein-dissociating PACE to facilitate further engineering of CRY2.
developed soluble expression and protein-dissociating PACE to facilitate further engineering of CRY2
Among stably expressed CRY2 proteins mutated in universally conserved residues, 74% retained wild-type-like activity for at least one analyzed photoresponse.
74% of the stably expressed CRY2 proteins mutated in UCRs retained wild-type-like activities for at least one of the photoresponses I analyzed.
fraction retaining wild-type-like activity 74%
Among stably expressed CRY2 proteins mutated in universally conserved residues, 74% retained wild-type-like activity for at least one analyzed photoresponse.
74% of the stably expressed CRY2 proteins mutated in UCRs retained wild-type-like activities for at least one of the photoresponses I analyzed.
fraction retaining wild-type-like activity 74%
Among stably expressed CRY2 proteins mutated in universally conserved residues, 74% retained wild-type-like activity for at least one analyzed photoresponse.
74% of the stably expressed CRY2 proteins mutated in UCRs retained wild-type-like activities for at least one of the photoresponses I analyzed.
fraction retaining wild-type-like activity 74%
Among stably expressed CRY2 proteins mutated in universally conserved residues, 74% retained wild-type-like activity for at least one analyzed photoresponse.
74% of the stably expressed CRY2 proteins mutated in UCRs retained wild-type-like activities for at least one of the photoresponses I analyzed.
fraction retaining wild-type-like activity 74%
Among stably expressed CRY2 proteins mutated in universally conserved residues, 74% retained wild-type-like activity for at least one analyzed photoresponse.
74% of the stably expressed CRY2 proteins mutated in UCRs retained wild-type-like activities for at least one of the photoresponses I analyzed.
fraction retaining wild-type-like activity 74%
Among stably expressed CRY2 proteins mutated in universally conserved residues, 74% retained wild-type-like activity for at least one analyzed photoresponse.
74% of the stably expressed CRY2 proteins mutated in UCRs retained wild-type-like activities for at least one of the photoresponses I analyzed.
fraction retaining wild-type-like activity 74%
Among stably expressed CRY2 proteins mutated in universally conserved residues, 74% retained wild-type-like activity for at least one analyzed photoresponse.
74% of the stably expressed CRY2 proteins mutated in UCRs retained wild-type-like activities for at least one of the photoresponses I analyzed.
fraction retaining wild-type-like activity 74%
The study developed a novel pair of blue-light-dependent interacting proteins, CRY2-BIC1.
Chapter 3 focused on the development of a novel pair of blue-light-dependent interacting proteins: CRY2-BIC1
The study developed a novel pair of blue-light-dependent interacting proteins, CRY2-BIC1.
Chapter 3 focused on the development of a novel pair of blue-light-dependent interacting proteins: CRY2-BIC1
The study developed a novel pair of blue-light-dependent interacting proteins, CRY2-BIC1.
Chapter 3 focused on the development of a novel pair of blue-light-dependent interacting proteins: CRY2-BIC1
The study developed a novel pair of blue-light-dependent interacting proteins, CRY2-BIC1.
Chapter 3 focused on the development of a novel pair of blue-light-dependent interacting proteins: CRY2-BIC1
The study developed a novel pair of blue-light-dependent interacting proteins, CRY2-BIC1.
Chapter 3 focused on the development of a novel pair of blue-light-dependent interacting proteins: CRY2-BIC1
The study developed a novel pair of blue-light-dependent interacting proteins, CRY2-BIC1.
Chapter 3 focused on the development of a novel pair of blue-light-dependent interacting proteins: CRY2-BIC1
The study developed a novel pair of blue-light-dependent interacting proteins, CRY2-BIC1.
Chapter 3 focused on the development of a novel pair of blue-light-dependent interacting proteins: CRY2-BIC1
The study isolated CRY2 variants with stronger interactions with BIC1.
I isolated variants of CRY2 with stronger interactions with BIC1
The study isolated CRY2 variants with stronger interactions with BIC1.
I isolated variants of CRY2 with stronger interactions with BIC1
The study isolated CRY2 variants with stronger interactions with BIC1.
I isolated variants of CRY2 with stronger interactions with BIC1
The study isolated CRY2 variants with stronger interactions with BIC1.
I isolated variants of CRY2 with stronger interactions with BIC1
The study isolated CRY2 variants with stronger interactions with BIC1.
I isolated variants of CRY2 with stronger interactions with BIC1
The study isolated CRY2 variants with stronger interactions with BIC1.
I isolated variants of CRY2 with stronger interactions with BIC1
The study isolated CRY2 variants with stronger interactions with BIC1.
I isolated variants of CRY2 with stronger interactions with BIC1
Approval Evidence
2 sources4 linked approval claimsfirst-pass slugs pace, phage-assisted-continuous-evolution
Countermeasures now integrate ... phage-assisted continuous evolution (PACE)
Source:
applied PACE (Phage Assisted Continuous Evolution) to increase the dynamic range of CRY2-BIC1 blue-light dependent interaction
Source:
engineering strategysupports
Next-generation countermeasures for Bt resistance include synergistic Cry/Vip pyramiding, CRISPR/Cas9-validated receptor knockouts revealing functional redundancy, Domain III chimerization, PACE, and AlphaFold3-guided rational redesign.
Countermeasures now integrate synergistic Cry/Vip pyramiding, CRISPR/Cas9-validated receptor knockouts revealing functional redundancy, Domain III chimerization (e.g., Cry1A.105), phage-assisted continuous evolution (PACE), and the emerging application of AlphaFold3 for structure-guided rational redesign of resistance-breaking variants.
Source:
engineering outcomesupports
PACE was applied to increase the dynamic range of the CRY2-BIC1 blue-light-dependent interaction.
applied PACE (Phage Assisted Continuous Evolution) to increase the dynamic range of CRY2-BIC1 blue-light dependent interaction
Source:
method developmentsupports
The study developed soluble expression PACE and protein-dissociating PACE to facilitate further engineering of CRY2.
developed soluble expression and protein-dissociating PACE to facilitate further engineering of CRY2
Source:
variant isolationsupports
The study isolated CRY2 variants with stronger interactions with BIC1.
I isolated variants of CRY2 with stronger interactions with BIC1
Source:
Comparisons
Source-backed strengths
The cited study reports a successful engineering outcome: increased dynamic range of the CRY2-BIC1 blue-light-dependent interaction. The evidence supports utility in cryptochrome optimization, but does not quantify the magnitude of improvement in the provided text.
Source:
I found that UCRs required for stable protein expression of CRY2 in plants are not similarly required for stable protein expression of human hCRY1 in human cells.
Source:
applied PACE (Phage Assisted Continuous Evolution) to increase the dynamic range of CRY2-BIC1 blue-light dependent interaction
Ranked Citations
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