Source 1primary paper2012The Plant Journal
Toolkit/intermolecular disulfide-based light switch
intermolecular disulfide-based light switch
Taxonomy: Mechanism Branch / Architecture. Workflows sit above the mechanism and technique branches rather than replacing them.
Summary
The intermolecular disulfide-based light switch is a regulatory construct pattern proposed for chloroplast psbD gene expression in Chlamydomonas reinhardtii. It is based on a putative intermolecular disulfide bridge between Nac2 and Cys11 of RBP40 in light-grown cells, with reduction of this covalent link in the dark.
Usefulness & Problems
Why this is useful
This construct pattern is useful as a mechanistic model for coupling light conditions to chloroplast gene expression through a reversible redox-sensitive protein interaction. The available evidence specifically supports its relevance to light-regulated psbD expression in Chlamydomonas reinhardtii, but does not establish broader utility across other genes or organisms.
Problem solved
It addresses the problem of how light-dependent signals can be transduced into regulation of chloroplast psbD gene expression. The cited work links this regulation to a reversible covalent association between Nac2 and RBP40 that differs between light-grown and dark conditions.
Problem links
Need precise spatiotemporal control with light input
DerivedThe intermolecular disulfide-based light switch is a regulatory construct pattern proposed for chloroplast psbD gene expression in Chlamydomonas reinhardtii. It is based on a putative intermolecular disulfide bridge between Nac2 and Cys11 of RBP40 in light-grown cells, with reduction of this covalent link in the dark.
Taxonomy & Function
Primary hierarchy
Mechanism Branch
Architecture: A reusable architecture pattern for arranging parts into an engineered system.
Mechanisms
intermolecular disulfide bond formationlight-regulated gene expressionredox-dependent reversible covalent protein associationTechniques
Functional AssayTarget processes
No target processes tagged yet.
Input: Light
Implementation Constraints
cofactor dependency: cofactor requirement unknownencoding mode: genetically encodedimplementation constraint: context specific validationimplementation constraint: spectral hardware requirementoperating role: actuator
Implementation appears to depend on the presence of Nac2, RBP40, and the Cys11 residue of RBP40 in the chloroplast regulatory context of Chlamydomonas reinhardtii. The dark-state reversal is proposed to involve NADPH-dependent thioredoxin reductase C, but the supplied evidence does not provide construct design rules, delivery methods, or expression protocols.
The evidence describes the disulfide linkage as putative, so the molecular model is not presented as definitively proven. Validation is limited to chloroplast psbD gene expression in Chlamydomonas reinhardtii, and the supplied evidence does not report quantitative performance, transferability, or independent replication.
Validation
Cell-freeBacteriaMammalianMouseHumanTherapeuticIndep. Replication
Supporting Sources
Ranked Claims
An intermolecular disulfide bridge between Nac2 and Cys11 of RBP40 is the putative molecular basis for attachment of RBP40 to the complex in light-grown cells.
2D redox SDS-PAGE assays suggest an intermolecular disulfide bridge between Nac2 and Cys11 of RBP40 as the putative molecular basis for attachment of RBP40 to the complex in light-grown cells.
An intermolecular disulfide bridge between Nac2 and Cys11 of RBP40 is the putative molecular basis for attachment of RBP40 to the complex in light-grown cells.
2D redox SDS-PAGE assays suggest an intermolecular disulfide bridge between Nac2 and Cys11 of RBP40 as the putative molecular basis for attachment of RBP40 to the complex in light-grown cells.
An intermolecular disulfide bridge between Nac2 and Cys11 of RBP40 is the putative molecular basis for attachment of RBP40 to the complex in light-grown cells.
2D redox SDS-PAGE assays suggest an intermolecular disulfide bridge between Nac2 and Cys11 of RBP40 as the putative molecular basis for attachment of RBP40 to the complex in light-grown cells.
An intermolecular disulfide bridge between Nac2 and Cys11 of RBP40 is the putative molecular basis for attachment of RBP40 to the complex in light-grown cells.
2D redox SDS-PAGE assays suggest an intermolecular disulfide bridge between Nac2 and Cys11 of RBP40 as the putative molecular basis for attachment of RBP40 to the complex in light-grown cells.
An intermolecular disulfide bridge between Nac2 and Cys11 of RBP40 is the putative molecular basis for attachment of RBP40 to the complex in light-grown cells.
2D redox SDS-PAGE assays suggest an intermolecular disulfide bridge between Nac2 and Cys11 of RBP40 as the putative molecular basis for attachment of RBP40 to the complex in light-grown cells.
An intermolecular disulfide bridge between Nac2 and Cys11 of RBP40 is the putative molecular basis for attachment of RBP40 to the complex in light-grown cells.
2D redox SDS-PAGE assays suggest an intermolecular disulfide bridge between Nac2 and Cys11 of RBP40 as the putative molecular basis for attachment of RBP40 to the complex in light-grown cells.
An intermolecular disulfide bridge between Nac2 and Cys11 of RBP40 is the putative molecular basis for attachment of RBP40 to the complex in light-grown cells.
2D redox SDS-PAGE assays suggest an intermolecular disulfide bridge between Nac2 and Cys11 of RBP40 as the putative molecular basis for attachment of RBP40 to the complex in light-grown cells.
The covalent link between Nac2 and RBP40 is reduced in the dark, most likely via NADPH-dependent thioredoxin reductase C.
This covalent link is reduced in the dark, most likely via NADPH-dependent thioredoxin reductase C
The covalent link between Nac2 and RBP40 is reduced in the dark, most likely via NADPH-dependent thioredoxin reductase C.
This covalent link is reduced in the dark, most likely via NADPH-dependent thioredoxin reductase C
The covalent link between Nac2 and RBP40 is reduced in the dark, most likely via NADPH-dependent thioredoxin reductase C.
This covalent link is reduced in the dark, most likely via NADPH-dependent thioredoxin reductase C
The covalent link between Nac2 and RBP40 is reduced in the dark, most likely via NADPH-dependent thioredoxin reductase C.
This covalent link is reduced in the dark, most likely via NADPH-dependent thioredoxin reductase C
The covalent link between Nac2 and RBP40 is reduced in the dark, most likely via NADPH-dependent thioredoxin reductase C.
This covalent link is reduced in the dark, most likely via NADPH-dependent thioredoxin reductase C
The covalent link between Nac2 and RBP40 is reduced in the dark, most likely via NADPH-dependent thioredoxin reductase C.
This covalent link is reduced in the dark, most likely via NADPH-dependent thioredoxin reductase C
The covalent link between Nac2 and RBP40 is reduced in the dark, most likely via NADPH-dependent thioredoxin reductase C.
This covalent link is reduced in the dark, most likely via NADPH-dependent thioredoxin reductase C
Chloroplast psbD gene expression is regulated by light in Chlamydomonas reinhardtii.
Expression of the chloroplast psbD gene encoding the D2 protein of the photosystem II reaction center is regulated by light.
Chloroplast psbD gene expression is regulated by light in Chlamydomonas reinhardtii.
Expression of the chloroplast psbD gene encoding the D2 protein of the photosystem II reaction center is regulated by light.
Chloroplast psbD gene expression is regulated by light in Chlamydomonas reinhardtii.
Expression of the chloroplast psbD gene encoding the D2 protein of the photosystem II reaction center is regulated by light.
Chloroplast psbD gene expression is regulated by light in Chlamydomonas reinhardtii.
Expression of the chloroplast psbD gene encoding the D2 protein of the photosystem II reaction center is regulated by light.
Chloroplast psbD gene expression is regulated by light in Chlamydomonas reinhardtii.
Expression of the chloroplast psbD gene encoding the D2 protein of the photosystem II reaction center is regulated by light.
Chloroplast psbD gene expression is regulated by light in Chlamydomonas reinhardtii.
Expression of the chloroplast psbD gene encoding the D2 protein of the photosystem II reaction center is regulated by light.
Chloroplast psbD gene expression is regulated by light in Chlamydomonas reinhardtii.
Expression of the chloroplast psbD gene encoding the D2 protein of the photosystem II reaction center is regulated by light.
Approval Evidence
1 source3 linked approval claimsfirst-pass slug intermolecular-disulfide-based-light-switch
An intermolecular disulfide‐based light switch for chloroplast psbD gene expression in Chlamydomonas reinhardtii
Source:
mechanismsupports
An intermolecular disulfide bridge between Nac2 and Cys11 of RBP40 is the putative molecular basis for attachment of RBP40 to the complex in light-grown cells.
2D redox SDS-PAGE assays suggest an intermolecular disulfide bridge between Nac2 and Cys11 of RBP40 as the putative molecular basis for attachment of RBP40 to the complex in light-grown cells.
Source:
mechanismsupports
The covalent link between Nac2 and RBP40 is reduced in the dark, most likely via NADPH-dependent thioredoxin reductase C.
This covalent link is reduced in the dark, most likely via NADPH-dependent thioredoxin reductase C
Source:
regulationsupports
Chloroplast psbD gene expression is regulated by light in Chlamydomonas reinhardtii.
Expression of the chloroplast psbD gene encoding the D2 protein of the photosystem II reaction center is regulated by light.
Source:
Comparisons
Source-backed strengths
The reported mechanism is molecularly specific, naming Nac2, RBP40, and Cys11 of RBP40 as components of the light-associated complex. The evidence also proposes a dark-state reduction pathway involving NADPH-dependent thioredoxin reductase C, providing a plausible reversible redox control mechanism.
intermolecular disulfide-based light switch and blue light-regulated synthetic genetic circuit for CheZ-controlled motility address a similar problem space.
Shared frame: same top-level item type; shared mechanisms: light-regulated gene expression; same primary input modality: light
Relative tradeoffs: looks easier to implement in practice.
Compared with Cu-TCPP membrane
intermolecular disulfide-based light switch and Cu-TCPP membrane address a similar problem space.
Shared frame: same top-level item type; same primary input modality: light
Compared with mMORp
intermolecular disulfide-based light switch and mMORp address a similar problem space.
Shared frame: same top-level item type; same primary input modality: light
Ranked Citations
- 1.