Toolkit/SecYEG complex
SecYEG complex
Taxonomy: Mechanism Branch / Architecture. Workflows sit above the mechanism and technique branches rather than replacing them.
Summary
The SecYEG complex was engineered as a light-responsive protein translocation switch by introducing an organochemical photoswitch into two transmembrane segments that form the lateral gate of the bacterial membrane-embedded protein-conducting pore. Illumination modulates pore gating and thereby controls SecYEG-dependent protein translocation.
Usefulness & Problems
Why this is useful
This tool enables optical control over a core membrane protein localization process, namely translocation through the bacterial SecYEG channel. It is useful for perturbing protein export with light rather than constitutive genetic alteration, based on direct control of pore gating.
Source:
Light‐Induced Control of Protein Translocation by the SecYEG Complex
Problem solved
It addresses the problem of how to externally and reversibly regulate protein translocation through the SecYEG translocon. The reported solution is to couple lateral-gate opening behavior to a light-responsive chemical modification.
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
localizationInput: Light
Implementation Constraints
Implementation requires site-specific introduction of an organochemical photoswitch into two transmembrane segments of the SecYEG lateral gate. The available evidence does not specify the photoswitch chemistry, construct design details, host system, or illumination parameters.
The supplied evidence does not report quantitative performance metrics, wavelength dependence, reversibility, dynamic range, or substrate scope. Independent replication and validation outside the cited study are not provided in the evidence.
Validation
Observations
Inferred from claim c2 during normalization. Visible and UV light reversibly switched azobenzene between trans and cis configurations, enforcing opening and closure of the protein-conducting pore. Derived from claim c2. Quoted text: Reversible switching of the azobenzene between the trans and cis configurations by irradiation with visible and UV light enforced the opening and closure of the protein-conducting pore
Source:
Inferred from claim c2 during normalization. Visible and UV light reversibly switched azobenzene between trans and cis configurations, enforcing opening and closure of the protein-conducting pore. Derived from claim c2. Quoted text: Reversible switching of the azobenzene between the trans and cis configurations by irradiation with visible and UV light enforced the opening and closure of the protein-conducting pore
Source:
Inferred from claim c2 during normalization. Visible and UV light reversibly switched azobenzene between trans and cis configurations, enforcing opening and closure of the protein-conducting pore. Derived from claim c2. Quoted text: Reversible switching of the azobenzene between the trans and cis configurations by irradiation with visible and UV light enforced the opening and closure of the protein-conducting pore
Source:
Inferred from claim c2 during normalization. Visible and UV light reversibly switched azobenzene between trans and cis configurations, enforcing opening and closure of the protein-conducting pore. Derived from claim c2. Quoted text: Reversible switching of the azobenzene between the trans and cis configurations by irradiation with visible and UV light enforced the opening and closure of the protein-conducting pore
Source:
Inferred from claim c2 during normalization. Visible and UV light reversibly switched azobenzene between trans and cis configurations, enforcing opening and closure of the protein-conducting pore. Derived from claim c2. Quoted text: Reversible switching of the azobenzene between the trans and cis configurations by irradiation with visible and UV light enforced the opening and closure of the protein-conducting pore
Source:
Inferred from claim c2 during normalization. Visible and UV light reversibly switched azobenzene between trans and cis configurations, enforcing opening and closure of the protein-conducting pore. Derived from claim c2. Quoted text: Reversible switching of the azobenzene between the trans and cis configurations by irradiation with visible and UV light enforced the opening and closure of the protein-conducting pore
Source:
Inferred from claim c2 during normalization. Visible and UV light reversibly switched azobenzene between trans and cis configurations, enforcing opening and closure of the protein-conducting pore. Derived from claim c2. Quoted text: Reversible switching of the azobenzene between the trans and cis configurations by irradiation with visible and UV light enforced the opening and closure of the protein-conducting pore
Source:
Inferred from claim c2 during normalization. Visible and UV light reversibly switched azobenzene between trans and cis configurations, enforcing opening and closure of the protein-conducting pore. Derived from claim c2. Quoted text: Reversible switching of the azobenzene between the trans and cis configurations by irradiation with visible and UV light enforced the opening and closure of the protein-conducting pore
Source:
Inferred from claim c2 during normalization. Visible and UV light reversibly switched azobenzene between trans and cis configurations, enforcing opening and closure of the protein-conducting pore. Derived from claim c2. Quoted text: Reversible switching of the azobenzene between the trans and cis configurations by irradiation with visible and UV light enforced the opening and closure of the protein-conducting pore
Source:
Inferred from claim c2 during normalization. Visible and UV light reversibly switched azobenzene between trans and cis configurations, enforcing opening and closure of the protein-conducting pore. Derived from claim c2. Quoted text: Reversible switching of the azobenzene between the trans and cis configurations by irradiation with visible and UV light enforced the opening and closure of the protein-conducting pore
Source:
Inferred from claim c2 during normalization. Visible and UV light reversibly switched azobenzene between trans and cis configurations, enforcing opening and closure of the protein-conducting pore. Derived from claim c2. Quoted text: Reversible switching of the azobenzene between the trans and cis configurations by irradiation with visible and UV light enforced the opening and closure of the protein-conducting pore
Source:
Inferred from claim c2 during normalization. Visible and UV light reversibly switched azobenzene between trans and cis configurations, enforcing opening and closure of the protein-conducting pore. Derived from claim c2. Quoted text: Reversible switching of the azobenzene between the trans and cis configurations by irradiation with visible and UV light enforced the opening and closure of the protein-conducting pore
Source:
Inferred from claim c2 during normalization. Visible and UV light reversibly switched azobenzene between trans and cis configurations, enforcing opening and closure of the protein-conducting pore. Derived from claim c2. Quoted text: Reversible switching of the azobenzene between the trans and cis configurations by irradiation with visible and UV light enforced the opening and closure of the protein-conducting pore
Source:
Inferred from claim c2 during normalization. Visible and UV light reversibly switched azobenzene between trans and cis configurations, enforcing opening and closure of the protein-conducting pore. Derived from claim c2. Quoted text: Reversible switching of the azobenzene between the trans and cis configurations by irradiation with visible and UV light enforced the opening and closure of the protein-conducting pore
Source:
Supporting Sources
Ranked Claims
An organochemical photoswitch was introduced into two transmembrane segments that comprise the lateral gate of the bacterial membrane embedded protein-conducting pore.
An organochemical photoswitch was introduced into two transmembrane segments that comprise the lateral gate of the bacterial-membrane-embedded protein-conducting pore.
An organochemical photoswitch was introduced into two transmembrane segments that comprise the lateral gate of the bacterial membrane embedded protein-conducting pore.
An organochemical photoswitch was introduced into two transmembrane segments that comprise the lateral gate of the bacterial-membrane-embedded protein-conducting pore.
An organochemical photoswitch was introduced into two transmembrane segments that comprise the lateral gate of the bacterial membrane embedded protein-conducting pore.
An organochemical photoswitch was introduced into two transmembrane segments that comprise the lateral gate of the bacterial-membrane-embedded protein-conducting pore.
An organochemical photoswitch was introduced into two transmembrane segments that comprise the lateral gate of the bacterial membrane embedded protein-conducting pore.
An organochemical photoswitch was introduced into two transmembrane segments that comprise the lateral gate of the bacterial-membrane-embedded protein-conducting pore.
An organochemical photoswitch was introduced into two transmembrane segments that comprise the lateral gate of the bacterial membrane embedded protein-conducting pore.
An organochemical photoswitch was introduced into two transmembrane segments that comprise the lateral gate of the bacterial-membrane-embedded protein-conducting pore.
An organochemical photoswitch was introduced into two transmembrane segments that comprise the lateral gate of the bacterial membrane embedded protein-conducting pore.
An organochemical photoswitch was introduced into two transmembrane segments that comprise the lateral gate of the bacterial-membrane-embedded protein-conducting pore.
An organochemical photoswitch was introduced into two transmembrane segments that comprise the lateral gate of the bacterial membrane embedded protein-conducting pore.
An organochemical photoswitch was introduced into two transmembrane segments that comprise the lateral gate of the bacterial-membrane-embedded protein-conducting pore.
An organochemical photoswitch was introduced into two transmembrane segments that comprise the lateral gate of the bacterial membrane embedded protein-conducting pore.
An organochemical photoswitch was introduced into two transmembrane segments that comprise the lateral gate of the bacterial-membrane-embedded protein-conducting pore.
An organochemical photoswitch was introduced into two transmembrane segments that comprise the lateral gate of the bacterial membrane embedded protein-conducting pore.
An organochemical photoswitch was introduced into two transmembrane segments that comprise the lateral gate of the bacterial-membrane-embedded protein-conducting pore.
An organochemical photoswitch was introduced into two transmembrane segments that comprise the lateral gate of the bacterial membrane embedded protein-conducting pore.
An organochemical photoswitch was introduced into two transmembrane segments that comprise the lateral gate of the bacterial-membrane-embedded protein-conducting pore.
An organochemical photoswitch was introduced into two transmembrane segments that comprise the lateral gate of the bacterial membrane embedded protein-conducting pore.
An organochemical photoswitch was introduced into two transmembrane segments that comprise the lateral gate of the bacterial-membrane-embedded protein-conducting pore.
An organochemical photoswitch was introduced into two transmembrane segments that comprise the lateral gate of the bacterial membrane embedded protein-conducting pore.
An organochemical photoswitch was introduced into two transmembrane segments that comprise the lateral gate of the bacterial-membrane-embedded protein-conducting pore.
An organochemical photoswitch was introduced into two transmembrane segments that comprise the lateral gate of the bacterial membrane embedded protein-conducting pore.
An organochemical photoswitch was introduced into two transmembrane segments that comprise the lateral gate of the bacterial-membrane-embedded protein-conducting pore.
An organochemical photoswitch was introduced into two transmembrane segments that comprise the lateral gate of the bacterial membrane embedded protein-conducting pore.
An organochemical photoswitch was introduced into two transmembrane segments that comprise the lateral gate of the bacterial-membrane-embedded protein-conducting pore.
Protein translocation by the SecYEG complex can be controlled by light-induced gating of the pore.
Light‐Induced Control of Protein Translocation by the SecYEG Complex
Protein translocation by the SecYEG complex can be controlled by light-induced gating of the pore.
Light‐Induced Control of Protein Translocation by the SecYEG Complex
Protein translocation by the SecYEG complex can be controlled by light-induced gating of the pore.
Light‐Induced Control of Protein Translocation by the SecYEG Complex
Protein translocation by the SecYEG complex can be controlled by light-induced gating of the pore.
Light‐Induced Control of Protein Translocation by the SecYEG Complex
Protein translocation by the SecYEG complex can be controlled by light-induced gating of the pore.
Light‐Induced Control of Protein Translocation by the SecYEG Complex
Protein translocation by the SecYEG complex can be controlled by light-induced gating of the pore.
Light‐Induced Control of Protein Translocation by the SecYEG Complex
Protein translocation by the SecYEG complex can be controlled by light-induced gating of the pore.
Light‐Induced Control of Protein Translocation by the SecYEG Complex
Protein translocation by the SecYEG complex can be controlled by light-induced gating of the pore.
Light‐Induced Control of Protein Translocation by the SecYEG Complex
Protein translocation by the SecYEG complex can be controlled by light-induced gating of the pore.
Light‐Induced Control of Protein Translocation by the SecYEG Complex
Protein translocation by the SecYEG complex can be controlled by light-induced gating of the pore.
Light‐Induced Control of Protein Translocation by the SecYEG Complex
Protein translocation by the SecYEG complex can be controlled by light-induced gating of the pore.
Light‐Induced Control of Protein Translocation by the SecYEG Complex
Protein translocation by the SecYEG complex can be controlled by light-induced gating of the pore.
Light‐Induced Control of Protein Translocation by the SecYEG Complex
Protein translocation by the SecYEG complex can be controlled by light-induced gating of the pore.
Light‐Induced Control of Protein Translocation by the SecYEG Complex
Protein translocation by the SecYEG complex can be controlled by light-induced gating of the pore.
Light‐Induced Control of Protein Translocation by the SecYEG Complex
Visible and UV light reversibly switched azobenzene between trans and cis configurations, enforcing opening and closure of the protein-conducting pore.
Reversible switching of the azobenzene between the trans and cis configurations by irradiation with visible and UV light enforced the opening and closure of the protein-conducting pore
Visible and UV light reversibly switched azobenzene between trans and cis configurations, enforcing opening and closure of the protein-conducting pore.
Reversible switching of the azobenzene between the trans and cis configurations by irradiation with visible and UV light enforced the opening and closure of the protein-conducting pore
Visible and UV light reversibly switched azobenzene between trans and cis configurations, enforcing opening and closure of the protein-conducting pore.
Reversible switching of the azobenzene between the trans and cis configurations by irradiation with visible and UV light enforced the opening and closure of the protein-conducting pore
Visible and UV light reversibly switched azobenzene between trans and cis configurations, enforcing opening and closure of the protein-conducting pore.
Reversible switching of the azobenzene between the trans and cis configurations by irradiation with visible and UV light enforced the opening and closure of the protein-conducting pore
Visible and UV light reversibly switched azobenzene between trans and cis configurations, enforcing opening and closure of the protein-conducting pore.
Reversible switching of the azobenzene between the trans and cis configurations by irradiation with visible and UV light enforced the opening and closure of the protein-conducting pore
Visible and UV light reversibly switched azobenzene between trans and cis configurations, enforcing opening and closure of the protein-conducting pore.
Reversible switching of the azobenzene between the trans and cis configurations by irradiation with visible and UV light enforced the opening and closure of the protein-conducting pore
Visible and UV light reversibly switched azobenzene between trans and cis configurations, enforcing opening and closure of the protein-conducting pore.
Reversible switching of the azobenzene between the trans and cis configurations by irradiation with visible and UV light enforced the opening and closure of the protein-conducting pore
Visible and UV light reversibly switched azobenzene between trans and cis configurations, enforcing opening and closure of the protein-conducting pore.
Reversible switching of the azobenzene between the trans and cis configurations by irradiation with visible and UV light enforced the opening and closure of the protein-conducting pore
Visible and UV light reversibly switched azobenzene between trans and cis configurations, enforcing opening and closure of the protein-conducting pore.
Reversible switching of the azobenzene between the trans and cis configurations by irradiation with visible and UV light enforced the opening and closure of the protein-conducting pore
Visible and UV light reversibly switched azobenzene between trans and cis configurations, enforcing opening and closure of the protein-conducting pore.
Reversible switching of the azobenzene between the trans and cis configurations by irradiation with visible and UV light enforced the opening and closure of the protein-conducting pore
Visible and UV light reversibly switched azobenzene between trans and cis configurations, enforcing opening and closure of the protein-conducting pore.
Reversible switching of the azobenzene between the trans and cis configurations by irradiation with visible and UV light enforced the opening and closure of the protein-conducting pore
Visible and UV light reversibly switched azobenzene between trans and cis configurations, enforcing opening and closure of the protein-conducting pore.
Reversible switching of the azobenzene between the trans and cis configurations by irradiation with visible and UV light enforced the opening and closure of the protein-conducting pore
Visible and UV light reversibly switched azobenzene between trans and cis configurations, enforcing opening and closure of the protein-conducting pore.
Reversible switching of the azobenzene between the trans and cis configurations by irradiation with visible and UV light enforced the opening and closure of the protein-conducting pore
Visible and UV light reversibly switched azobenzene between trans and cis configurations, enforcing opening and closure of the protein-conducting pore.
Reversible switching of the azobenzene between the trans and cis configurations by irradiation with visible and UV light enforced the opening and closure of the protein-conducting pore
Approval Evidence
Light‐Induced Control of Protein Translocation by the SecYEG Complex
Source:
An organochemical photoswitch was introduced into two transmembrane segments that comprise the lateral gate of the bacterial membrane embedded protein-conducting pore.
An organochemical photoswitch was introduced into two transmembrane segments that comprise the lateral gate of the bacterial-membrane-embedded protein-conducting pore.
Source:
Protein translocation by the SecYEG complex can be controlled by light-induced gating of the pore.
Light‐Induced Control of Protein Translocation by the SecYEG Complex
Source:
Visible and UV light reversibly switched azobenzene between trans and cis configurations, enforcing opening and closure of the protein-conducting pore.
Reversible switching of the azobenzene between the trans and cis configurations by irradiation with visible and UV light enforced the opening and closure of the protein-conducting pore
Source:
Comparisons
Source-backed strengths
The engineering strategy acts directly on the SecYEG pore by modifying two transmembrane segments that comprise the lateral gate. Source evidence supports functional light control of protein translocation through light-induced gating of the channel.
Source:
An organochemical photoswitch was introduced into two transmembrane segments that comprise the lateral gate of the bacterial-membrane-embedded protein-conducting pore.
Ranked Citations
- 1.