Source 1review2018Biological Chemistry
Toolkit/intein
intein
Also known as: internal protein domains
Taxonomy: Mechanism Branch / Component. Workflows sit above the mechanism and technique branches rather than replacing them.
Summary
Inteins are internal protein domains that mediate conditional protein splicing as a post-translational control strategy. The supplied evidence describes switchable inteins as being developed to control splicing in ways compatible with applications in living cells.
Usefulness & Problems
Why this is useful
Inteins are useful because conditional splicing acts at the post-translational level on pre-existing proteins. The cited review states that post-translational control can provide faster responses than regulating expression of the corresponding genes.
Source:
Conditional splicing of internal protein domains, termed inteins, is an attractive methodology for this purpose.
Problem solved
This tool helps address the problem of achieving rapid conditional control of protein function without relying solely on transcriptional or translational regulation. The evidence specifically frames conditional intein splicing as an attractive method for this purpose in living-cell-compatible contexts.
Source:
Conditional splicing of internal protein domains, termed inteins, is an attractive methodology for this purpose.
Problem links
Need inducible protein relocalization or recruitment
DerivedInteins are internal protein domains that mediate conditional protein splicing as a post-translational control strategy. The supplied evidence indicates that switchable inteins are being developed for applications in living cells, including light-compatible control contexts.
Need precise spatiotemporal control with light input
DerivedInteins are internal protein domains that mediate conditional protein splicing as a post-translational control strategy. The supplied evidence indicates that switchable inteins are being developed for applications in living cells, including light-compatible control contexts.
Need tighter control over protein production
DerivedInteins are internal protein domains that mediate conditional protein splicing as a post-translational control strategy. The supplied evidence indicates that switchable inteins are being developed for applications in living cells, including light-compatible control contexts.
Taxonomy & Function
Primary hierarchy
Mechanism Branch
Component: A low-level protein part used inside a larger architecture that realizes a mechanism.
Mechanisms
post-translational controlpost-translational controlprotein splicingprotein splicingTranslation ControlTechniques
No technique tags yet.
Target processes
localizationtranslationInput: Light
Implementation Constraints
cofactor dependency: cofactor requirement unknownencoding mode: genetically encodedimplementation constraint: context specific validationimplementation constraint: spectral hardware requirementoperating role: regulatorswitch architecture: single chain
The evidence supports the general concept of using inteins as internal protein domains for conditional protein splicing in living cells. It does not provide construct architecture, cofactor requirements, delivery methods, or expression-system details.
The supplied evidence is review-level and does not provide specific performance metrics, host systems, or benchmarked examples. Although light-compatible contexts are mentioned in the current summary, the provided source text does not specify wavelengths, photoreceptors, or validated optical constructs.
Validation
Cell-freeBacteriaMammalianMouseHumanTherapeuticIndep. Replication
Supporting Sources
Ranked Claims
Post-translational modification of pre-existing proteins can provide faster responses than controlling proteins by regulating expression of their encoding genes.
Proteins can be controlled in several ways, for instance by regulating the expression of their encoding genes with small molecules or light. However, post-translationally modifying pre-existing proteins to regulate their function or localization leads to faster responses.
Post-translational modification of pre-existing proteins can provide faster responses than controlling proteins by regulating expression of their encoding genes.
Proteins can be controlled in several ways, for instance by regulating the expression of their encoding genes with small molecules or light. However, post-translationally modifying pre-existing proteins to regulate their function or localization leads to faster responses.
Post-translational modification of pre-existing proteins can provide faster responses than controlling proteins by regulating expression of their encoding genes.
Proteins can be controlled in several ways, for instance by regulating the expression of their encoding genes with small molecules or light. However, post-translationally modifying pre-existing proteins to regulate their function or localization leads to faster responses.
Post-translational modification of pre-existing proteins can provide faster responses than controlling proteins by regulating expression of their encoding genes.
Proteins can be controlled in several ways, for instance by regulating the expression of their encoding genes with small molecules or light. However, post-translationally modifying pre-existing proteins to regulate their function or localization leads to faster responses.
Post-translational modification of pre-existing proteins can provide faster responses than controlling proteins by regulating expression of their encoding genes.
Proteins can be controlled in several ways, for instance by regulating the expression of their encoding genes with small molecules or light. However, post-translationally modifying pre-existing proteins to regulate their function or localization leads to faster responses.
Post-translational modification of pre-existing proteins can provide faster responses than controlling proteins by regulating expression of their encoding genes.
Proteins can be controlled in several ways, for instance by regulating the expression of their encoding genes with small molecules or light. However, post-translationally modifying pre-existing proteins to regulate their function or localization leads to faster responses.
Post-translational modification of pre-existing proteins can provide faster responses than controlling proteins by regulating expression of their encoding genes.
Proteins can be controlled in several ways, for instance by regulating the expression of their encoding genes with small molecules or light. However, post-translationally modifying pre-existing proteins to regulate their function or localization leads to faster responses.
Post-translational modification of pre-existing proteins can provide faster responses than controlling proteins by regulating expression of their encoding genes.
Proteins can be controlled in several ways, for instance by regulating the expression of their encoding genes with small molecules or light. However, post-translationally modifying pre-existing proteins to regulate their function or localization leads to faster responses.
Post-translational modification of pre-existing proteins can provide faster responses than controlling proteins by regulating expression of their encoding genes.
Proteins can be controlled in several ways, for instance by regulating the expression of their encoding genes with small molecules or light. However, post-translationally modifying pre-existing proteins to regulate their function or localization leads to faster responses.
Post-translational modification of pre-existing proteins can provide faster responses than controlling proteins by regulating expression of their encoding genes.
Proteins can be controlled in several ways, for instance by regulating the expression of their encoding genes with small molecules or light. However, post-translationally modifying pre-existing proteins to regulate their function or localization leads to faster responses.
Post-translational modification of pre-existing proteins can provide faster responses than controlling proteins by regulating expression of their encoding genes.
Proteins can be controlled in several ways, for instance by regulating the expression of their encoding genes with small molecules or light. However, post-translationally modifying pre-existing proteins to regulate their function or localization leads to faster responses.
Post-translational modification of pre-existing proteins can provide faster responses than controlling proteins by regulating expression of their encoding genes.
Proteins can be controlled in several ways, for instance by regulating the expression of their encoding genes with small molecules or light. However, post-translationally modifying pre-existing proteins to regulate their function or localization leads to faster responses.
Post-translational modification of pre-existing proteins can provide faster responses than controlling proteins by regulating expression of their encoding genes.
Proteins can be controlled in several ways, for instance by regulating the expression of their encoding genes with small molecules or light. However, post-translationally modifying pre-existing proteins to regulate their function or localization leads to faster responses.
Post-translational modification of pre-existing proteins can provide faster responses than controlling proteins by regulating expression of their encoding genes.
Proteins can be controlled in several ways, for instance by regulating the expression of their encoding genes with small molecules or light. However, post-translationally modifying pre-existing proteins to regulate their function or localization leads to faster responses.
Post-translational modification of pre-existing proteins can provide faster responses than controlling proteins by regulating expression of their encoding genes.
Proteins can be controlled in several ways, for instance by regulating the expression of their encoding genes with small molecules or light. However, post-translationally modifying pre-existing proteins to regulate their function or localization leads to faster responses.
Post-translational modification of pre-existing proteins can provide faster responses than controlling proteins by regulating expression of their encoding genes.
Proteins can be controlled in several ways, for instance by regulating the expression of their encoding genes with small molecules or light. However, post-translationally modifying pre-existing proteins to regulate their function or localization leads to faster responses.
Post-translational modification of pre-existing proteins can provide faster responses than controlling proteins by regulating expression of their encoding genes.
Proteins can be controlled in several ways, for instance by regulating the expression of their encoding genes with small molecules or light. However, post-translationally modifying pre-existing proteins to regulate their function or localization leads to faster responses.
Post-translational modification of pre-existing proteins can provide faster responses than controlling proteins by regulating expression of their encoding genes.
Proteins can be controlled in several ways, for instance by regulating the expression of their encoding genes with small molecules or light. However, post-translationally modifying pre-existing proteins to regulate their function or localization leads to faster responses.
Post-translational modification of pre-existing proteins can provide faster responses than controlling proteins by regulating expression of their encoding genes.
Proteins can be controlled in several ways, for instance by regulating the expression of their encoding genes with small molecules or light. However, post-translationally modifying pre-existing proteins to regulate their function or localization leads to faster responses.
Post-translational modification of pre-existing proteins can provide faster responses than controlling proteins by regulating expression of their encoding genes.
Proteins can be controlled in several ways, for instance by regulating the expression of their encoding genes with small molecules or light. However, post-translationally modifying pre-existing proteins to regulate their function or localization leads to faster responses.
Post-translational modification of pre-existing proteins can provide faster responses than controlling proteins by regulating expression of their encoding genes.
Proteins can be controlled in several ways, for instance by regulating the expression of their encoding genes with small molecules or light. However, post-translationally modifying pre-existing proteins to regulate their function or localization leads to faster responses.
Post-translational modification of pre-existing proteins can provide faster responses than controlling proteins by regulating expression of their encoding genes.
Proteins can be controlled in several ways, for instance by regulating the expression of their encoding genes with small molecules or light. However, post-translationally modifying pre-existing proteins to regulate their function or localization leads to faster responses.
Post-translational modification of pre-existing proteins can provide faster responses than controlling proteins by regulating expression of their encoding genes.
Proteins can be controlled in several ways, for instance by regulating the expression of their encoding genes with small molecules or light. However, post-translationally modifying pre-existing proteins to regulate their function or localization leads to faster responses.
Post-translational modification of pre-existing proteins can provide faster responses than controlling proteins by regulating expression of their encoding genes.
Proteins can be controlled in several ways, for instance by regulating the expression of their encoding genes with small molecules or light. However, post-translationally modifying pre-existing proteins to regulate their function or localization leads to faster responses.
Post-translational modification of pre-existing proteins can provide faster responses than controlling proteins by regulating expression of their encoding genes.
Proteins can be controlled in several ways, for instance by regulating the expression of their encoding genes with small molecules or light. However, post-translationally modifying pre-existing proteins to regulate their function or localization leads to faster responses.
Post-translational modification of pre-existing proteins can provide faster responses than controlling proteins by regulating expression of their encoding genes.
Proteins can be controlled in several ways, for instance by regulating the expression of their encoding genes with small molecules or light. However, post-translationally modifying pre-existing proteins to regulate their function or localization leads to faster responses.
Post-translational modification of pre-existing proteins can provide faster responses than controlling proteins by regulating expression of their encoding genes.
Proteins can be controlled in several ways, for instance by regulating the expression of their encoding genes with small molecules or light. However, post-translationally modifying pre-existing proteins to regulate their function or localization leads to faster responses.
The review discusses methods to control intein activity with a focus on approaches compatible with applications in living cells.
Here we discuss methods to control intein activity with a focus on those compatible with applications in living cells.
The review discusses methods to control intein activity with a focus on approaches compatible with applications in living cells.
Here we discuss methods to control intein activity with a focus on those compatible with applications in living cells.
The review discusses methods to control intein activity with a focus on approaches compatible with applications in living cells.
Here we discuss methods to control intein activity with a focus on those compatible with applications in living cells.
The review discusses methods to control intein activity with a focus on approaches compatible with applications in living cells.
Here we discuss methods to control intein activity with a focus on those compatible with applications in living cells.
The review discusses methods to control intein activity with a focus on approaches compatible with applications in living cells.
Here we discuss methods to control intein activity with a focus on those compatible with applications in living cells.
The review discusses methods to control intein activity with a focus on approaches compatible with applications in living cells.
Here we discuss methods to control intein activity with a focus on those compatible with applications in living cells.
The review discusses methods to control intein activity with a focus on approaches compatible with applications in living cells.
Here we discuss methods to control intein activity with a focus on those compatible with applications in living cells.
The review discusses methods to control intein activity with a focus on approaches compatible with applications in living cells.
Here we discuss methods to control intein activity with a focus on those compatible with applications in living cells.
The review discusses methods to control intein activity with a focus on approaches compatible with applications in living cells.
Here we discuss methods to control intein activity with a focus on those compatible with applications in living cells.
The review discusses methods to control intein activity with a focus on approaches compatible with applications in living cells.
Here we discuss methods to control intein activity with a focus on those compatible with applications in living cells.
The review discusses methods to control intein activity with a focus on approaches compatible with applications in living cells.
Here we discuss methods to control intein activity with a focus on those compatible with applications in living cells.
The review discusses methods to control intein activity with a focus on approaches compatible with applications in living cells.
Here we discuss methods to control intein activity with a focus on those compatible with applications in living cells.
The review discusses methods to control intein activity with a focus on approaches compatible with applications in living cells.
Here we discuss methods to control intein activity with a focus on those compatible with applications in living cells.
The review discusses methods to control intein activity with a focus on approaches compatible with applications in living cells.
Here we discuss methods to control intein activity with a focus on those compatible with applications in living cells.
The review discusses methods to control intein activity with a focus on approaches compatible with applications in living cells.
Here we discuss methods to control intein activity with a focus on those compatible with applications in living cells.
The review discusses methods to control intein activity with a focus on approaches compatible with applications in living cells.
Here we discuss methods to control intein activity with a focus on those compatible with applications in living cells.
The review discusses methods to control intein activity with a focus on approaches compatible with applications in living cells.
Here we discuss methods to control intein activity with a focus on those compatible with applications in living cells.
The review discusses methods to control intein activity with a focus on approaches compatible with applications in living cells.
Here we discuss methods to control intein activity with a focus on those compatible with applications in living cells.
The review discusses methods to control intein activity with a focus on approaches compatible with applications in living cells.
Here we discuss methods to control intein activity with a focus on those compatible with applications in living cells.
The review discusses methods to control intein activity with a focus on approaches compatible with applications in living cells.
Here we discuss methods to control intein activity with a focus on those compatible with applications in living cells.
The review discusses methods to control intein activity with a focus on approaches compatible with applications in living cells.
Here we discuss methods to control intein activity with a focus on those compatible with applications in living cells.
The review discusses methods to control intein activity with a focus on approaches compatible with applications in living cells.
Here we discuss methods to control intein activity with a focus on those compatible with applications in living cells.
The review discusses methods to control intein activity with a focus on approaches compatible with applications in living cells.
Here we discuss methods to control intein activity with a focus on those compatible with applications in living cells.
The review discusses methods to control intein activity with a focus on approaches compatible with applications in living cells.
Here we discuss methods to control intein activity with a focus on those compatible with applications in living cells.
The review discusses methods to control intein activity with a focus on approaches compatible with applications in living cells.
Here we discuss methods to control intein activity with a focus on those compatible with applications in living cells.
The review discusses methods to control intein activity with a focus on approaches compatible with applications in living cells.
Here we discuss methods to control intein activity with a focus on those compatible with applications in living cells.
The review discusses methods to control intein activity with a focus on approaches compatible with applications in living cells.
Here we discuss methods to control intein activity with a focus on those compatible with applications in living cells.
Conditional splicing mediated by inteins is presented as an attractive method for controlling protein function or localization.
Conditional splicing of internal protein domains, termed inteins, is an attractive methodology for this purpose.
Conditional splicing mediated by inteins is presented as an attractive method for controlling protein function or localization.
Conditional splicing of internal protein domains, termed inteins, is an attractive methodology for this purpose.
Conditional splicing mediated by inteins is presented as an attractive method for controlling protein function or localization.
Conditional splicing of internal protein domains, termed inteins, is an attractive methodology for this purpose.
Conditional splicing mediated by inteins is presented as an attractive method for controlling protein function or localization.
Conditional splicing of internal protein domains, termed inteins, is an attractive methodology for this purpose.
Conditional splicing mediated by inteins is presented as an attractive method for controlling protein function or localization.
Conditional splicing of internal protein domains, termed inteins, is an attractive methodology for this purpose.
Conditional splicing mediated by inteins is presented as an attractive method for controlling protein function or localization.
Conditional splicing of internal protein domains, termed inteins, is an attractive methodology for this purpose.
Conditional splicing mediated by inteins is presented as an attractive method for controlling protein function or localization.
Conditional splicing of internal protein domains, termed inteins, is an attractive methodology for this purpose.
Conditional splicing mediated by inteins is presented as an attractive method for controlling protein function or localization.
Conditional splicing of internal protein domains, termed inteins, is an attractive methodology for this purpose.
Conditional splicing mediated by inteins is presented as an attractive method for controlling protein function or localization.
Conditional splicing of internal protein domains, termed inteins, is an attractive methodology for this purpose.
Conditional splicing mediated by inteins is presented as an attractive method for controlling protein function or localization.
Conditional splicing of internal protein domains, termed inteins, is an attractive methodology for this purpose.
Conditional splicing mediated by inteins is presented as an attractive method for controlling protein function or localization.
Conditional splicing of internal protein domains, termed inteins, is an attractive methodology for this purpose.
Conditional splicing mediated by inteins is presented as an attractive method for controlling protein function or localization.
Conditional splicing of internal protein domains, termed inteins, is an attractive methodology for this purpose.
Conditional splicing mediated by inteins is presented as an attractive method for controlling protein function or localization.
Conditional splicing of internal protein domains, termed inteins, is an attractive methodology for this purpose.
Conditional splicing mediated by inteins is presented as an attractive method for controlling protein function or localization.
Conditional splicing of internal protein domains, termed inteins, is an attractive methodology for this purpose.
Conditional splicing mediated by inteins is presented as an attractive method for controlling protein function or localization.
Conditional splicing of internal protein domains, termed inteins, is an attractive methodology for this purpose.
Conditional splicing mediated by inteins is presented as an attractive method for controlling protein function or localization.
Conditional splicing of internal protein domains, termed inteins, is an attractive methodology for this purpose.
Conditional splicing mediated by inteins is presented as an attractive method for controlling protein function or localization.
Conditional splicing of internal protein domains, termed inteins, is an attractive methodology for this purpose.
Conditional splicing mediated by inteins is presented as an attractive method for controlling protein function or localization.
Conditional splicing of internal protein domains, termed inteins, is an attractive methodology for this purpose.
Conditional splicing mediated by inteins is presented as an attractive method for controlling protein function or localization.
Conditional splicing of internal protein domains, termed inteins, is an attractive methodology for this purpose.
Conditional splicing mediated by inteins is presented as an attractive method for controlling protein function or localization.
Conditional splicing of internal protein domains, termed inteins, is an attractive methodology for this purpose.
Conditional splicing mediated by inteins is presented as an attractive method for controlling protein function or localization.
Conditional splicing of internal protein domains, termed inteins, is an attractive methodology for this purpose.
Conditional splicing mediated by inteins is presented as an attractive method for controlling protein function or localization.
Conditional splicing of internal protein domains, termed inteins, is an attractive methodology for this purpose.
Conditional splicing mediated by inteins is presented as an attractive method for controlling protein function or localization.
Conditional splicing of internal protein domains, termed inteins, is an attractive methodology for this purpose.
Conditional splicing mediated by inteins is presented as an attractive method for controlling protein function or localization.
Conditional splicing of internal protein domains, termed inteins, is an attractive methodology for this purpose.
Conditional splicing mediated by inteins is presented as an attractive method for controlling protein function or localization.
Conditional splicing of internal protein domains, termed inteins, is an attractive methodology for this purpose.
Conditional splicing mediated by inteins is presented as an attractive method for controlling protein function or localization.
Conditional splicing of internal protein domains, termed inteins, is an attractive methodology for this purpose.
Conditional splicing mediated by inteins is presented as an attractive method for controlling protein function or localization.
Conditional splicing of internal protein domains, termed inteins, is an attractive methodology for this purpose.
Approval Evidence
1 source3 linked approval claimsfirst-pass slug intein
Conditional splicing of internal protein domains, termed inteins, is an attractive methodology for this purpose.
Source:
comparative advantagesupports
Post-translational modification of pre-existing proteins can provide faster responses than controlling proteins by regulating expression of their encoding genes.
Proteins can be controlled in several ways, for instance by regulating the expression of their encoding genes with small molecules or light. However, post-translationally modifying pre-existing proteins to regulate their function or localization leads to faster responses.
Source:
review scope statementneutral
The review discusses methods to control intein activity with a focus on approaches compatible with applications in living cells.
Here we discuss methods to control intein activity with a focus on those compatible with applications in living cells.
Source:
use casesupports
Conditional splicing mediated by inteins is presented as an attractive method for controlling protein function or localization.
Conditional splicing of internal protein domains, termed inteins, is an attractive methodology for this purpose.
Source:
Comparisons
Source-backed strengths
A key strength supported by the evidence is the potential for faster response kinetics relative to gene-expression-based control, because inteins act through post-translational modification of existing proteins. The review also indicates active development of switchable inteins for use in living cells.
Source:
Proteins can be controlled in several ways, for instance by regulating the expression of their encoding genes with small molecules or light. However, post-translationally modifying pre-existing proteins to regulate their function or localization leads to faster responses.
Compared with LOVdeg tag
intein and LOVdeg tag address a similar problem space because they share translation.
Shared frame: same top-level item type; shared target processes: translation; shared mechanisms: post-translational control, translation_control; same primary input modality: light
Relative tradeoffs: appears more independently replicated; looks easier to implement in practice.
Compared with optogenetic circuits
intein and optogenetic circuits address a similar problem space because they share translation.
Shared frame: same top-level item type; shared target processes: translation; shared mechanisms: translation_control; same primary input modality: light
Compared with optogenetic systems adapted to regulate gene expression
intein and optogenetic systems adapted to regulate gene expression address a similar problem space because they share localization, translation.
Shared frame: shared target processes: localization, translation; shared mechanisms: translation_control; same primary input modality: light
Strengths here: looks easier to implement in practice.
Ranked Citations
- 1.