Source 1primary paper2020Angewandte Chemie International Edition
Toolkit/FtsZ
FtsZ
Taxonomy: Mechanism Branch / Component. Workflows sit above the mechanism and technique branches rather than replacing them.
Summary
FtsZ is a prokaryotic filamentous cell-division protein that was adapted as a light-responsive protein domain by site-specific incorporation of a photocaged tyrosine. In this engineered form, UV-mediated uncaging at tyrosine 222 was used to control FtsZ self-organization, GTPase regulation, and treadmilling-related dynamics.
Usefulness & Problems
Why this is useful
This tool enables optical perturbation of a defined FtsZ residue to dissect how a single tyrosine contributes to higher-order self-organization and enzymatic regulation. It is useful for studying light-triggered control of protein self-organization in systems where FtsZ filament behavior, ring-pattern formation, and treadmilling dynamics are of interest.
Problem solved
It addresses the problem of how to reversibly and site-specifically mask an essential residue in FtsZ and then restore its function with light. The reported implementation specifically probes the role of tyrosine 222 in regulating FtsZ GTPase activity, self-organization, and treadmilling dynamics.
Problem links
Need conditional control of signaling activity
DerivedFtsZ is a prokaryotic filamentous cell-division protein that was adapted as a light-responsive protein domain through site-specific incorporation of a photocaged tyrosine. In this form, UV-mediated uncaging at tyrosine 222 was used to control FtsZ self-organization, GTPase regulation, and treadmilling-related dynamics.
Need precise spatiotemporal control with light input
DerivedFtsZ is a prokaryotic filamentous cell-division protein that was adapted as a light-responsive protein domain through site-specific incorporation of a photocaged tyrosine. In this form, UV-mediated uncaging at tyrosine 222 was used to control FtsZ self-organization, GTPase regulation, and treadmilling-related dynamics.
Taxonomy & Function
Primary hierarchy
Mechanism Branch
Component: A low-level protein part used inside a larger architecture that realizes a mechanism.
Mechanisms
conformational uncagingconformational uncagingConformational Uncagingphotocaging/photodeprotectionphotocaging/photodeprotectionTechniques
No technique tags yet.
Target processes
signalingInput: Light
Implementation Constraints
cofactor dependency: cofactor requirement unknownencoding mode: genetically encodedimplementation constraint: context specific validationimplementation constraint: spectral hardware requirementoperating role: actuatoroperating role: regulatorswitch architecture: uncaging
Implementation involved site-specific incorporation of a photocaged tyrosine analogue into FtsZ, specifically masking tyrosine 222. Functional activation required UV-mediated uncaging, but the supplied evidence does not provide construct architecture, host system, or noncanonical amino acid incorporation machinery details.
Evidence is limited to a single cited study and the supplied claims focus on mechanistic perturbation rather than broad application across organisms or cellular contexts. The available evidence does not specify quantitative performance metrics, uncaging wavelength details beyond UV, reversibility, or delivery and expression constraints.
Validation
Cell-freeBacteriaMammalianMouseHumanTherapeuticIndep. Replication
Supporting Sources
Ranked Claims
Site-specific incorporation of a photocaged tyrosine analogue into FtsZ masks a tyrosine residue and yields a mutant that still self-assembles into filaments but no longer shows dynamic self-organization into ring patterns.
We masked a tyrosine residue of FtsZ by site-specific incorporation of a photocaged tyrosine analogue. While the mutant still shows self-assembly into filaments, dynamic self-organization into ring patterns can no longer be observed.
Site-specific incorporation of a photocaged tyrosine analogue into FtsZ masks a tyrosine residue and yields a mutant that still self-assembles into filaments but no longer shows dynamic self-organization into ring patterns.
We masked a tyrosine residue of FtsZ by site-specific incorporation of a photocaged tyrosine analogue. While the mutant still shows self-assembly into filaments, dynamic self-organization into ring patterns can no longer be observed.
Site-specific incorporation of a photocaged tyrosine analogue into FtsZ masks a tyrosine residue and yields a mutant that still self-assembles into filaments but no longer shows dynamic self-organization into ring patterns.
We masked a tyrosine residue of FtsZ by site-specific incorporation of a photocaged tyrosine analogue. While the mutant still shows self-assembly into filaments, dynamic self-organization into ring patterns can no longer be observed.
Site-specific incorporation of a photocaged tyrosine analogue into FtsZ masks a tyrosine residue and yields a mutant that still self-assembles into filaments but no longer shows dynamic self-organization into ring patterns.
We masked a tyrosine residue of FtsZ by site-specific incorporation of a photocaged tyrosine analogue. While the mutant still shows self-assembly into filaments, dynamic self-organization into ring patterns can no longer be observed.
Site-specific incorporation of a photocaged tyrosine analogue into FtsZ masks a tyrosine residue and yields a mutant that still self-assembles into filaments but no longer shows dynamic self-organization into ring patterns.
We masked a tyrosine residue of FtsZ by site-specific incorporation of a photocaged tyrosine analogue. While the mutant still shows self-assembly into filaments, dynamic self-organization into ring patterns can no longer be observed.
Site-specific incorporation of a photocaged tyrosine analogue into FtsZ masks a tyrosine residue and yields a mutant that still self-assembles into filaments but no longer shows dynamic self-organization into ring patterns.
We masked a tyrosine residue of FtsZ by site-specific incorporation of a photocaged tyrosine analogue. While the mutant still shows self-assembly into filaments, dynamic self-organization into ring patterns can no longer be observed.
Site-specific incorporation of a photocaged tyrosine analogue into FtsZ masks a tyrosine residue and yields a mutant that still self-assembles into filaments but no longer shows dynamic self-organization into ring patterns.
We masked a tyrosine residue of FtsZ by site-specific incorporation of a photocaged tyrosine analogue. While the mutant still shows self-assembly into filaments, dynamic self-organization into ring patterns can no longer be observed.
Site-specific incorporation of a photocaged tyrosine analogue into FtsZ masks a tyrosine residue and yields a mutant that still self-assembles into filaments but no longer shows dynamic self-organization into ring patterns.
We masked a tyrosine residue of FtsZ by site-specific incorporation of a photocaged tyrosine analogue. While the mutant still shows self-assembly into filaments, dynamic self-organization into ring patterns can no longer be observed.
Site-specific incorporation of a photocaged tyrosine analogue into FtsZ masks a tyrosine residue and yields a mutant that still self-assembles into filaments but no longer shows dynamic self-organization into ring patterns.
We masked a tyrosine residue of FtsZ by site-specific incorporation of a photocaged tyrosine analogue. While the mutant still shows self-assembly into filaments, dynamic self-organization into ring patterns can no longer be observed.
Site-specific incorporation of a photocaged tyrosine analogue into FtsZ masks a tyrosine residue and yields a mutant that still self-assembles into filaments but no longer shows dynamic self-organization into ring patterns.
We masked a tyrosine residue of FtsZ by site-specific incorporation of a photocaged tyrosine analogue. While the mutant still shows self-assembly into filaments, dynamic self-organization into ring patterns can no longer be observed.
Site-specific incorporation of a photocaged tyrosine analogue into FtsZ masks a tyrosine residue and yields a mutant that still self-assembles into filaments but no longer shows dynamic self-organization into ring patterns.
We masked a tyrosine residue of FtsZ by site-specific incorporation of a photocaged tyrosine analogue. While the mutant still shows self-assembly into filaments, dynamic self-organization into ring patterns can no longer be observed.
Site-specific incorporation of a photocaged tyrosine analogue into FtsZ masks a tyrosine residue and yields a mutant that still self-assembles into filaments but no longer shows dynamic self-organization into ring patterns.
We masked a tyrosine residue of FtsZ by site-specific incorporation of a photocaged tyrosine analogue. While the mutant still shows self-assembly into filaments, dynamic self-organization into ring patterns can no longer be observed.
Site-specific incorporation of a photocaged tyrosine analogue into FtsZ masks a tyrosine residue and yields a mutant that still self-assembles into filaments but no longer shows dynamic self-organization into ring patterns.
We masked a tyrosine residue of FtsZ by site-specific incorporation of a photocaged tyrosine analogue. While the mutant still shows self-assembly into filaments, dynamic self-organization into ring patterns can no longer be observed.
Site-specific incorporation of a photocaged tyrosine analogue into FtsZ masks a tyrosine residue and yields a mutant that still self-assembles into filaments but no longer shows dynamic self-organization into ring patterns.
We masked a tyrosine residue of FtsZ by site-specific incorporation of a photocaged tyrosine analogue. While the mutant still shows self-assembly into filaments, dynamic self-organization into ring patterns can no longer be observed.
Site-specific incorporation of a photocaged tyrosine analogue into FtsZ masks a tyrosine residue and yields a mutant that still self-assembles into filaments but no longer shows dynamic self-organization into ring patterns.
We masked a tyrosine residue of FtsZ by site-specific incorporation of a photocaged tyrosine analogue. While the mutant still shows self-assembly into filaments, dynamic self-organization into ring patterns can no longer be observed.
Site-specific incorporation of a photocaged tyrosine analogue into FtsZ masks a tyrosine residue and yields a mutant that still self-assembles into filaments but no longer shows dynamic self-organization into ring patterns.
We masked a tyrosine residue of FtsZ by site-specific incorporation of a photocaged tyrosine analogue. While the mutant still shows self-assembly into filaments, dynamic self-organization into ring patterns can no longer be observed.
Site-specific incorporation of a photocaged tyrosine analogue into FtsZ masks a tyrosine residue and yields a mutant that still self-assembles into filaments but no longer shows dynamic self-organization into ring patterns.
We masked a tyrosine residue of FtsZ by site-specific incorporation of a photocaged tyrosine analogue. While the mutant still shows self-assembly into filaments, dynamic self-organization into ring patterns can no longer be observed.
UV-mediated uncaging revealed that tyrosine 222 is essential for regulation of FtsZ GTPase activity, self-organization, and treadmilling dynamics.
UV-mediated uncaging revealed that tyrosine 222 is essential for the regulation of the protein's GTPase activity, self-organization, and treadmilling dynamics.
UV-mediated uncaging revealed that tyrosine 222 is essential for regulation of FtsZ GTPase activity, self-organization, and treadmilling dynamics.
UV-mediated uncaging revealed that tyrosine 222 is essential for the regulation of the protein's GTPase activity, self-organization, and treadmilling dynamics.
UV-mediated uncaging revealed that tyrosine 222 is essential for regulation of FtsZ GTPase activity, self-organization, and treadmilling dynamics.
UV-mediated uncaging revealed that tyrosine 222 is essential for the regulation of the protein's GTPase activity, self-organization, and treadmilling dynamics.
UV-mediated uncaging revealed that tyrosine 222 is essential for regulation of FtsZ GTPase activity, self-organization, and treadmilling dynamics.
UV-mediated uncaging revealed that tyrosine 222 is essential for the regulation of the protein's GTPase activity, self-organization, and treadmilling dynamics.
UV-mediated uncaging revealed that tyrosine 222 is essential for regulation of FtsZ GTPase activity, self-organization, and treadmilling dynamics.
UV-mediated uncaging revealed that tyrosine 222 is essential for the regulation of the protein's GTPase activity, self-organization, and treadmilling dynamics.
UV-mediated uncaging revealed that tyrosine 222 is essential for regulation of FtsZ GTPase activity, self-organization, and treadmilling dynamics.
UV-mediated uncaging revealed that tyrosine 222 is essential for the regulation of the protein's GTPase activity, self-organization, and treadmilling dynamics.
UV-mediated uncaging revealed that tyrosine 222 is essential for regulation of FtsZ GTPase activity, self-organization, and treadmilling dynamics.
UV-mediated uncaging revealed that tyrosine 222 is essential for the regulation of the protein's GTPase activity, self-organization, and treadmilling dynamics.
UV-mediated uncaging revealed that tyrosine 222 is essential for regulation of FtsZ GTPase activity, self-organization, and treadmilling dynamics.
UV-mediated uncaging revealed that tyrosine 222 is essential for the regulation of the protein's GTPase activity, self-organization, and treadmilling dynamics.
UV-mediated uncaging revealed that tyrosine 222 is essential for regulation of FtsZ GTPase activity, self-organization, and treadmilling dynamics.
UV-mediated uncaging revealed that tyrosine 222 is essential for the regulation of the protein's GTPase activity, self-organization, and treadmilling dynamics.
UV-mediated uncaging revealed that tyrosine 222 is essential for regulation of FtsZ GTPase activity, self-organization, and treadmilling dynamics.
UV-mediated uncaging revealed that tyrosine 222 is essential for the regulation of the protein's GTPase activity, self-organization, and treadmilling dynamics.
UV-mediated uncaging revealed that tyrosine 222 is essential for regulation of FtsZ GTPase activity, self-organization, and treadmilling dynamics.
UV-mediated uncaging revealed that tyrosine 222 is essential for the regulation of the protein's GTPase activity, self-organization, and treadmilling dynamics.
UV-mediated uncaging revealed that tyrosine 222 is essential for regulation of FtsZ GTPase activity, self-organization, and treadmilling dynamics.
UV-mediated uncaging revealed that tyrosine 222 is essential for the regulation of the protein's GTPase activity, self-organization, and treadmilling dynamics.
UV-mediated uncaging revealed that tyrosine 222 is essential for regulation of FtsZ GTPase activity, self-organization, and treadmilling dynamics.
UV-mediated uncaging revealed that tyrosine 222 is essential for the regulation of the protein's GTPase activity, self-organization, and treadmilling dynamics.
UV-mediated uncaging revealed that tyrosine 222 is essential for regulation of FtsZ GTPase activity, self-organization, and treadmilling dynamics.
UV-mediated uncaging revealed that tyrosine 222 is essential for the regulation of the protein's GTPase activity, self-organization, and treadmilling dynamics.
UV-mediated uncaging revealed that tyrosine 222 is essential for regulation of FtsZ GTPase activity, self-organization, and treadmilling dynamics.
UV-mediated uncaging revealed that tyrosine 222 is essential for the regulation of the protein's GTPase activity, self-organization, and treadmilling dynamics.
UV-mediated uncaging revealed that tyrosine 222 is essential for regulation of FtsZ GTPase activity, self-organization, and treadmilling dynamics.
UV-mediated uncaging revealed that tyrosine 222 is essential for the regulation of the protein's GTPase activity, self-organization, and treadmilling dynamics.
UV-mediated uncaging revealed that tyrosine 222 is essential for regulation of FtsZ GTPase activity, self-organization, and treadmilling dynamics.
UV-mediated uncaging revealed that tyrosine 222 is essential for the regulation of the protein's GTPase activity, self-organization, and treadmilling dynamics.
Approval Evidence
1 source2 linked approval claimsfirst-pass slug ftsz
the prokaryotic filamentous cell-division protein (FtsZ)
Source:
mechanistic effectsupports
Site-specific incorporation of a photocaged tyrosine analogue into FtsZ masks a tyrosine residue and yields a mutant that still self-assembles into filaments but no longer shows dynamic self-organization into ring patterns.
We masked a tyrosine residue of FtsZ by site-specific incorporation of a photocaged tyrosine analogue. While the mutant still shows self-assembly into filaments, dynamic self-organization into ring patterns can no longer be observed.
Source:
mechanistic rolesupports
UV-mediated uncaging revealed that tyrosine 222 is essential for regulation of FtsZ GTPase activity, self-organization, and treadmilling dynamics.
UV-mediated uncaging revealed that tyrosine 222 is essential for the regulation of the protein's GTPase activity, self-organization, and treadmilling dynamics.
Source:
Comparisons
Source-backed strengths
The cited study reports residue-level optical control, because photocaging was introduced site-specifically at tyrosine 222 and function was modulated by UV-mediated uncaging. The caged mutant still self-assembled into filaments but lost dynamic self-organization into ring patterns, indicating that the approach can separate filament assembly from higher-order dynamic organization.
Compared with Avena sativa phototropin-1 LOV2 domain
FtsZ and Avena sativa phototropin-1 LOV2 domain address a similar problem space because they share signaling.
Shared frame: same top-level item type; shared target processes: signaling; shared mechanisms: conformational uncaging, conformational_uncaging; same primary input modality: light
Relative tradeoffs: appears more independently replicated; looks easier to implement in practice.
Compared with Avena sativa phototropin LOV2 domain
FtsZ and Avena sativa phototropin LOV2 domain address a similar problem space because they share signaling.
Shared frame: same top-level item type; shared target processes: signaling; shared mechanisms: conformational uncaging, conformational_uncaging; same primary input modality: light
Compared with photoswitchable inhibitory peptides
FtsZ and photoswitchable inhibitory peptides address a similar problem space because they share signaling.
Shared frame: same top-level item type; shared target processes: signaling; shared mechanisms: conformational uncaging, conformational_uncaging; same primary input modality: light
Ranked Citations
- 1.