Toolkit/PPR-DYW synthetic RNA editors
PPR-DYW synthetic RNA editors
Also known as: PPR-based editors, PPR proteins fused to DYW deaminase domains, synthetic PPR-DYW proteins
Taxonomy: Mechanism Branch / Architecture. Workflows sit above the mechanism and technique branches rather than replacing them.
Summary
Recent advances have extended these synthetic scaffolds to active RNA editors by fusing them to catalytically competent DYW deaminase domains, generating customizable enzymes capable of precise base conversion in bacteria, plants, and even human cells.
Usefulness & Problems
Why this is useful
These constructs combine programmable PPR RNA recognition with DYW deaminase catalytic activity to create targeted RNA base editors. The abstract describes precise C-to-U and U-to-C conversion applications.; targeted C-to-U RNA editing; targeted U-to-C RNA editing; precise RNA base conversion
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These constructs combine programmable PPR RNA recognition with DYW deaminase catalytic activity to create targeted RNA base editors. The abstract describes precise C-to-U and U-to-C conversion applications.
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targeted C-to-U RNA editing
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targeted U-to-C RNA editing
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precise RNA base conversion
Problem solved
They solve the problem of making customizable RNA editors that can direct precise base conversion to chosen RNA sequences.; converts programmable RNA-binding scaffolds into active site-directed RNA editors
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They solve the problem of making customizable RNA editors that can direct precise base conversion to chosen RNA sequences.
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converts programmable RNA-binding scaffolds into active site-directed RNA editors
Problem links
converts programmable RNA-binding scaffolds into active site-directed RNA editors
LiteratureThey solve the problem of making customizable RNA editors that can direct precise base conversion to chosen RNA sequences.
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They solve the problem of making customizable RNA editors that can direct precise base conversion to chosen RNA sequences.
Taxonomy & Function
Primary hierarchy
Mechanism Branch
Architecture: A composed arrangement of multiple parts that instantiates one or more mechanisms.
Techniques
No technique tags yet.
Target processes
recombinationtranslationImplementation Constraints
They require a synthetic PPR targeting scaffold and a catalytically competent DYW deaminase domain. Their function also depends on matching the PPR recognition code to the intended RNA target.; requires fusion of synthetic PPR scaffolds to catalytically competent DYW deaminase domains
The abstract does not claim complete optimization, and it explicitly notes remaining needs to improve specificity and catalytic efficiency.; continued refinement of targeting specificity is needed; continued refinement of catalytic efficiency is needed
Validation
Supporting Sources
Ranked Claims
Synthetic PPR-DYW editors are reported to perform precise base conversion in bacteria, plants, and human cells.
generating customizable enzymes capable of precise base conversion in bacteria, plants, and even human cells
Synthetic PPR proteins have been used as programmable RNA stabilizers, translational regulators, and targeted C-to-U or U-to-C editors.
synthetic PPR proteins have been used as programmable RNA stabilizers, translational regulators, and targeted C-to-U or U-to-C editors
Fusing synthetic PPR scaffolds to catalytically competent DYW deaminase domains creates customizable active RNA editors capable of precise base conversion.
Recent advances have extended these synthetic scaffolds to active RNA editors by fusing them to catalytically competent DYW deaminase domains, generating customizable enzymes capable of precise base conversion
Broader use of PPR-based editors depends on continued refinement of targeting specificity, catalytic efficiency, and effector modularity.
Continued refinement of targeting specificity, catalytic efficiency, and effector modularity will propel PPR-based editors toward broader use
Compact, cofactor-independent editors derived from early-diverging plant lineages expand the versatility of the synthetic PPR platform.
The development of compact, cofactor-independent editors derived from early-diverging plant lineages further expands the versatility of this platform.
Approval Evidence
Recent advances have extended these synthetic scaffolds to active RNA editors by fusing them to catalytically competent DYW deaminase domains, generating customizable enzymes capable of precise base conversion in bacteria, plants, and even human cells.
Source:
Synthetic PPR-DYW editors are reported to perform precise base conversion in bacteria, plants, and human cells.
generating customizable enzymes capable of precise base conversion in bacteria, plants, and even human cells
Source:
Synthetic PPR proteins have been used as programmable RNA stabilizers, translational regulators, and targeted C-to-U or U-to-C editors.
synthetic PPR proteins have been used as programmable RNA stabilizers, translational regulators, and targeted C-to-U or U-to-C editors
Source:
Fusing synthetic PPR scaffolds to catalytically competent DYW deaminase domains creates customizable active RNA editors capable of precise base conversion.
Recent advances have extended these synthetic scaffolds to active RNA editors by fusing them to catalytically competent DYW deaminase domains, generating customizable enzymes capable of precise base conversion
Source:
Broader use of PPR-based editors depends on continued refinement of targeting specificity, catalytic efficiency, and effector modularity.
Continued refinement of targeting specificity, catalytic efficiency, and effector modularity will propel PPR-based editors toward broader use
Source:
Compact, cofactor-independent editors derived from early-diverging plant lineages expand the versatility of the synthetic PPR platform.
The development of compact, cofactor-independent editors derived from early-diverging plant lineages further expands the versatility of this platform.
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Comparisons
Source-stated alternatives
The abstract contrasts active PPR-DYW editors with synPPR proteins used only for RNA stabilization or translational regulation.
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The abstract contrasts active PPR-DYW editors with synPPR proteins used only for RNA stabilization or translational regulation.
Source-backed strengths
customizable enzymes; precise base conversion; reported activity across bacteria, plants, and human cells
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customizable enzymes
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precise base conversion
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reported activity across bacteria, plants, and human cells
Compared with cLIPS2
PPR-DYW synthetic RNA editors and cLIPS2 address a similar problem space because they share recombination, translation.
Shared frame: same top-level item type; shared target processes: recombination, translation; shared mechanisms: translation_control
Strengths here: looks easier to implement in practice.
Compared with CRISPR/Cas9
PPR-DYW synthetic RNA editors and CRISPR/Cas9 address a similar problem space because they share recombination, translation.
Shared frame: same top-level item type; shared target processes: recombination, translation; shared mechanisms: translation_control
Strengths here: may avoid an exogenous cofactor requirement.
Relative tradeoffs: appears more independently replicated.
Compared with prime-editing
PPR-DYW synthetic RNA editors and prime-editing address a similar problem space because they share recombination, translation.
Shared frame: same top-level item type; shared target processes: recombination, translation; shared mechanisms: translation_control
Strengths here: looks easier to implement in practice; may avoid an exogenous cofactor requirement.
Relative tradeoffs: appears more independently replicated.
Ranked Citations
- 1.