Source 1primary paper2015PLoS ONE
Toolkit/A'α/Aβ gap of LOV2
A'α/Aβ gap of LOV2
Also known as: A'α/Aβ gap
Taxonomy: Mechanism Branch / Component. Workflows sit above the mechanism and technique branches rather than replacing them.
Summary
The A'α/Aβ gap is a structurally defined region N-terminal to the LOV2 core of Arabidopsis thaliana phototropin1. In LOV2-serine/threonine kinase polypeptides, this region contributes to blue-light signal transmission from LOV2 to kinase activation, and conserved residues Glu474 and Lys475 are required for efficient light-induced kinase activation.
Usefulness & Problems
Why this is useful
This region is useful as a defined intramolecular signaling element for dissecting how blue-light sensing by LOV2 is coupled to downstream serine/threonine kinase output in phototropin1. The available evidence supports its value for mechanistic studies of signal propagation within plant photoreceptors, particularly at the interface between LOV2 conformational change and kinase activation.
Problem solved
The A'α/Aβ gap helps address the specific problem of identifying which N-terminal LOV2-adjacent structural elements are necessary for transmitting the blue-light signal to the phot1 kinase domain. Mutational and truncation data localize an essential contribution to this gap region, especially residues Glu474 and Lys475.
Taxonomy & Function
Primary hierarchy
Mechanism Branch
Component: A low-level protein part used inside a larger architecture that realizes a mechanism.
Mechanisms
intramolecular allosteric couplinglight-induced conformational changesignal transduction from lov2 to kinase activationTechniques
Structural CharacterizationTarget processes
signalingInput: Light
Implementation Constraints
The reported context is the LOV2-serine/threonine kinase region of Arabidopsis thaliana phototropin1, with functional perturbation tested by A'α-helix truncation and Ala substitution of Glu474 and Lys475. The input modality is blue light, but the supplied evidence does not provide construct architecture details, cofactor requirements, expression systems, or delivery considerations.
The evidence is limited to a single cited study in Arabidopsis thaliana phot1-derived LOV2-STK constructs. The claims support an essential role in kinase activation, but they do not establish portability as an engineered module, quantitative performance metrics, or validation across diverse organisms and assay contexts.
Validation
Cell-freeBacteriaMammalianMouseHumanTherapeuticIndep. Replication
Supporting Sources
Ranked Claims
Glu474 and Lys475 in the LOV2 A'α/Aβ gap are conserved among higher-plant phototropins and may act as a joint connecting Jα-helix structural changes to kinase activation.
The amino acid residues, Glu474 and Lys475, in the gap are conserved among the phots of higher plants and may act as a joint to connect the structural changes in the Jα-helix with the activation of STK.
Section: abstract
Glu474 and Lys475 in the LOV2 A'α/Aβ gap are conserved among higher-plant phototropins and may act as a joint connecting Jα-helix structural changes to kinase activation.
The amino acid residues, Glu474 and Lys475, in the gap are conserved among the phots of higher plants and may act as a joint to connect the structural changes in the Jα-helix with the activation of STK.
Section: abstract
Glu474 and Lys475 in the LOV2 A'α/Aβ gap are conserved among higher-plant phototropins and may act as a joint connecting Jα-helix structural changes to kinase activation.
The amino acid residues, Glu474 and Lys475, in the gap are conserved among the phots of higher plants and may act as a joint to connect the structural changes in the Jα-helix with the activation of STK.
Section: abstract
Glu474 and Lys475 in the LOV2 A'α/Aβ gap are conserved among higher-plant phototropins and may act as a joint connecting Jα-helix structural changes to kinase activation.
The amino acid residues, Glu474 and Lys475, in the gap are conserved among the phots of higher plants and may act as a joint to connect the structural changes in the Jα-helix with the activation of STK.
Section: abstract
Glu474 and Lys475 in the LOV2 A'α/Aβ gap are conserved among higher-plant phototropins and may act as a joint connecting Jα-helix structural changes to kinase activation.
The amino acid residues, Glu474 and Lys475, in the gap are conserved among the phots of higher plants and may act as a joint to connect the structural changes in the Jα-helix with the activation of STK.
Section: abstract
Glu474 and Lys475 in the LOV2 A'α/Aβ gap are conserved among higher-plant phototropins and may act as a joint connecting Jα-helix structural changes to kinase activation.
The amino acid residues, Glu474 and Lys475, in the gap are conserved among the phots of higher plants and may act as a joint to connect the structural changes in the Jα-helix with the activation of STK.
Section: abstract
Glu474 and Lys475 in the LOV2 A'α/Aβ gap are conserved among higher-plant phototropins and may act as a joint connecting Jα-helix structural changes to kinase activation.
The amino acid residues, Glu474 and Lys475, in the gap are conserved among the phots of higher plants and may act as a joint to connect the structural changes in the Jα-helix with the activation of STK.
Section: abstract
Truncation of the A'α-helix and Ala substitutions at Glu474 and Lys475 in the LOV2 A'α/Aβ gap impair blue-light-induced activation of the serine/threonine kinase in Arabidopsis thaliana phot1 LOV2-STK polypeptides.
Using LOV2-STK polypeptides from Arabidopsis thaliana phot1, we found that truncation of the A'α-helix and amino acid substitutions at Glu474 and Lys475 in the gap between the A'α and the Aβ strand of LOV2 (A'α/Aβ gap) to Ala impaired the BL-induced activation of the STK, although they did not affect S390 formation.
Section: abstract
Truncation of the A'α-helix and Ala substitutions at Glu474 and Lys475 in the LOV2 A'α/Aβ gap impair blue-light-induced activation of the serine/threonine kinase in Arabidopsis thaliana phot1 LOV2-STK polypeptides.
Using LOV2-STK polypeptides from Arabidopsis thaliana phot1, we found that truncation of the A'α-helix and amino acid substitutions at Glu474 and Lys475 in the gap between the A'α and the Aβ strand of LOV2 (A'α/Aβ gap) to Ala impaired the BL-induced activation of the STK, although they did not affect S390 formation.
Section: abstract
Truncation of the A'α-helix and Ala substitutions at Glu474 and Lys475 in the LOV2 A'α/Aβ gap impair blue-light-induced activation of the serine/threonine kinase in Arabidopsis thaliana phot1 LOV2-STK polypeptides.
Using LOV2-STK polypeptides from Arabidopsis thaliana phot1, we found that truncation of the A'α-helix and amino acid substitutions at Glu474 and Lys475 in the gap between the A'α and the Aβ strand of LOV2 (A'α/Aβ gap) to Ala impaired the BL-induced activation of the STK, although they did not affect S390 formation.
Section: abstract
Truncation of the A'α-helix and Ala substitutions at Glu474 and Lys475 in the LOV2 A'α/Aβ gap impair blue-light-induced activation of the serine/threonine kinase in Arabidopsis thaliana phot1 LOV2-STK polypeptides.
Using LOV2-STK polypeptides from Arabidopsis thaliana phot1, we found that truncation of the A'α-helix and amino acid substitutions at Glu474 and Lys475 in the gap between the A'α and the Aβ strand of LOV2 (A'α/Aβ gap) to Ala impaired the BL-induced activation of the STK, although they did not affect S390 formation.
Section: abstract
Truncation of the A'α-helix and Ala substitutions at Glu474 and Lys475 in the LOV2 A'α/Aβ gap impair blue-light-induced activation of the serine/threonine kinase in Arabidopsis thaliana phot1 LOV2-STK polypeptides.
Using LOV2-STK polypeptides from Arabidopsis thaliana phot1, we found that truncation of the A'α-helix and amino acid substitutions at Glu474 and Lys475 in the gap between the A'α and the Aβ strand of LOV2 (A'α/Aβ gap) to Ala impaired the BL-induced activation of the STK, although they did not affect S390 formation.
Section: abstract
Truncation of the A'α-helix and Ala substitutions at Glu474 and Lys475 in the LOV2 A'α/Aβ gap impair blue-light-induced activation of the serine/threonine kinase in Arabidopsis thaliana phot1 LOV2-STK polypeptides.
Using LOV2-STK polypeptides from Arabidopsis thaliana phot1, we found that truncation of the A'α-helix and amino acid substitutions at Glu474 and Lys475 in the gap between the A'α and the Aβ strand of LOV2 (A'α/Aβ gap) to Ala impaired the BL-induced activation of the STK, although they did not affect S390 formation.
Section: abstract
Truncation of the A'α-helix and Ala substitutions at Glu474 and Lys475 in the LOV2 A'α/Aβ gap impair blue-light-induced activation of the serine/threonine kinase in Arabidopsis thaliana phot1 LOV2-STK polypeptides.
Using LOV2-STK polypeptides from Arabidopsis thaliana phot1, we found that truncation of the A'α-helix and amino acid substitutions at Glu474 and Lys475 in the gap between the A'α and the Aβ strand of LOV2 (A'α/Aβ gap) to Ala impaired the BL-induced activation of the STK, although they did not affect S390 formation.
Section: abstract
Light-dependent trypsin digestion at Lys603 and Lys475 indicates blue-light-induced structural changes in both the Jα-helix and the A'α/Aβ gap.
Trypsin digested the LOV2-STK at Lys603 and Lys475 in a light-dependent manner indicating BL-induced structural changes in both the Jα-helix and the gap. The digestion at Lys603 is faster than at Lys475.
Section: abstract
relative digestion rate Lys603 faster than Lys475
Light-dependent trypsin digestion at Lys603 and Lys475 indicates blue-light-induced structural changes in both the Jα-helix and the A'α/Aβ gap.
Trypsin digested the LOV2-STK at Lys603 and Lys475 in a light-dependent manner indicating BL-induced structural changes in both the Jα-helix and the gap. The digestion at Lys603 is faster than at Lys475.
Section: abstract
relative digestion rate Lys603 faster than Lys475
Light-dependent trypsin digestion at Lys603 and Lys475 indicates blue-light-induced structural changes in both the Jα-helix and the A'α/Aβ gap.
Trypsin digested the LOV2-STK at Lys603 and Lys475 in a light-dependent manner indicating BL-induced structural changes in both the Jα-helix and the gap. The digestion at Lys603 is faster than at Lys475.
Section: abstract
relative digestion rate Lys603 faster than Lys475
Light-dependent trypsin digestion at Lys603 and Lys475 indicates blue-light-induced structural changes in both the Jα-helix and the A'α/Aβ gap.
Trypsin digested the LOV2-STK at Lys603 and Lys475 in a light-dependent manner indicating BL-induced structural changes in both the Jα-helix and the gap. The digestion at Lys603 is faster than at Lys475.
Section: abstract
relative digestion rate Lys603 faster than Lys475
Light-dependent trypsin digestion at Lys603 and Lys475 indicates blue-light-induced structural changes in both the Jα-helix and the A'α/Aβ gap.
Trypsin digested the LOV2-STK at Lys603 and Lys475 in a light-dependent manner indicating BL-induced structural changes in both the Jα-helix and the gap. The digestion at Lys603 is faster than at Lys475.
Section: abstract
relative digestion rate Lys603 faster than Lys475
Light-dependent trypsin digestion at Lys603 and Lys475 indicates blue-light-induced structural changes in both the Jα-helix and the A'α/Aβ gap.
Trypsin digested the LOV2-STK at Lys603 and Lys475 in a light-dependent manner indicating BL-induced structural changes in both the Jα-helix and the gap. The digestion at Lys603 is faster than at Lys475.
Section: abstract
relative digestion rate Lys603 faster than Lys475
Light-dependent trypsin digestion at Lys603 and Lys475 indicates blue-light-induced structural changes in both the Jα-helix and the A'α/Aβ gap.
Trypsin digested the LOV2-STK at Lys603 and Lys475 in a light-dependent manner indicating BL-induced structural changes in both the Jα-helix and the gap. The digestion at Lys603 is faster than at Lys475.
Section: abstract
relative digestion rate Lys603 faster than Lys475
The A'α-helix truncation and Glu474Ala/Lys475Ala substitutions impair blue-light-induced kinase activation without affecting S390 formation.
truncation of the A'α-helix and amino acid substitutions at Glu474 and Lys475 in the gap between the A'α and the Aβ strand of LOV2 (A'α/Aβ gap) to Ala impaired the BL-induced activation of the STK, although they did not affect S390 formation.
Section: abstract
The A'α-helix truncation and Glu474Ala/Lys475Ala substitutions impair blue-light-induced kinase activation without affecting S390 formation.
truncation of the A'α-helix and amino acid substitutions at Glu474 and Lys475 in the gap between the A'α and the Aβ strand of LOV2 (A'α/Aβ gap) to Ala impaired the BL-induced activation of the STK, although they did not affect S390 formation.
Section: abstract
The A'α-helix truncation and Glu474Ala/Lys475Ala substitutions impair blue-light-induced kinase activation without affecting S390 formation.
truncation of the A'α-helix and amino acid substitutions at Glu474 and Lys475 in the gap between the A'α and the Aβ strand of LOV2 (A'α/Aβ gap) to Ala impaired the BL-induced activation of the STK, although they did not affect S390 formation.
Section: abstract
The A'α-helix truncation and Glu474Ala/Lys475Ala substitutions impair blue-light-induced kinase activation without affecting S390 formation.
truncation of the A'α-helix and amino acid substitutions at Glu474 and Lys475 in the gap between the A'α and the Aβ strand of LOV2 (A'α/Aβ gap) to Ala impaired the BL-induced activation of the STK, although they did not affect S390 formation.
Section: abstract
The A'α-helix truncation and Glu474Ala/Lys475Ala substitutions impair blue-light-induced kinase activation without affecting S390 formation.
truncation of the A'α-helix and amino acid substitutions at Glu474 and Lys475 in the gap between the A'α and the Aβ strand of LOV2 (A'α/Aβ gap) to Ala impaired the BL-induced activation of the STK, although they did not affect S390 formation.
Section: abstract
The A'α-helix truncation and Glu474Ala/Lys475Ala substitutions impair blue-light-induced kinase activation without affecting S390 formation.
truncation of the A'α-helix and amino acid substitutions at Glu474 and Lys475 in the gap between the A'α and the Aβ strand of LOV2 (A'α/Aβ gap) to Ala impaired the BL-induced activation of the STK, although they did not affect S390 formation.
Section: abstract
The A'α-helix truncation and Glu474Ala/Lys475Ala substitutions impair blue-light-induced kinase activation without affecting S390 formation.
truncation of the A'α-helix and amino acid substitutions at Glu474 and Lys475 in the gap between the A'α and the Aβ strand of LOV2 (A'α/Aβ gap) to Ala impaired the BL-induced activation of the STK, although they did not affect S390 formation.
Section: abstract
In Glu474Ala and Lys475Ala substitutes, the blue-light signal reaches the Jα-helix and the A'α/Aβ gap but does not activate the kinase.
These BL-induced structural changes were observed with the Glu474Ala and the Lys475Ala substitutes, indicating that the BL signal reached the Jα-helix as well as the A'α/Aβ gap but could not activate STK.
Section: abstract
In Glu474Ala and Lys475Ala substitutes, the blue-light signal reaches the Jα-helix and the A'α/Aβ gap but does not activate the kinase.
These BL-induced structural changes were observed with the Glu474Ala and the Lys475Ala substitutes, indicating that the BL signal reached the Jα-helix as well as the A'α/Aβ gap but could not activate STK.
Section: abstract
In Glu474Ala and Lys475Ala substitutes, the blue-light signal reaches the Jα-helix and the A'α/Aβ gap but does not activate the kinase.
These BL-induced structural changes were observed with the Glu474Ala and the Lys475Ala substitutes, indicating that the BL signal reached the Jα-helix as well as the A'α/Aβ gap but could not activate STK.
Section: abstract
In Glu474Ala and Lys475Ala substitutes, the blue-light signal reaches the Jα-helix and the A'α/Aβ gap but does not activate the kinase.
These BL-induced structural changes were observed with the Glu474Ala and the Lys475Ala substitutes, indicating that the BL signal reached the Jα-helix as well as the A'α/Aβ gap but could not activate STK.
Section: abstract
In Glu474Ala and Lys475Ala substitutes, the blue-light signal reaches the Jα-helix and the A'α/Aβ gap but does not activate the kinase.
These BL-induced structural changes were observed with the Glu474Ala and the Lys475Ala substitutes, indicating that the BL signal reached the Jα-helix as well as the A'α/Aβ gap but could not activate STK.
Section: abstract
In Glu474Ala and Lys475Ala substitutes, the blue-light signal reaches the Jα-helix and the A'α/Aβ gap but does not activate the kinase.
These BL-induced structural changes were observed with the Glu474Ala and the Lys475Ala substitutes, indicating that the BL signal reached the Jα-helix as well as the A'α/Aβ gap but could not activate STK.
Section: abstract
In Glu474Ala and Lys475Ala substitutes, the blue-light signal reaches the Jα-helix and the A'α/Aβ gap but does not activate the kinase.
These BL-induced structural changes were observed with the Glu474Ala and the Lys475Ala substitutes, indicating that the BL signal reached the Jα-helix as well as the A'α/Aβ gap but could not activate STK.
Section: abstract
Approval Evidence
1 source5 linked approval claimsfirst-pass slug a-a-gap-of-lov2
the gap between the A'α and the Aβ strand of LOV2 (A'α/Aβ gap)
Source:
conservation and proposed mechanismsupports
Glu474 and Lys475 in the LOV2 A'α/Aβ gap are conserved among higher-plant phototropins and may act as a joint connecting Jα-helix structural changes to kinase activation.
The amino acid residues, Glu474 and Lys475, in the gap are conserved among the phots of higher plants and may act as a joint to connect the structural changes in the Jα-helix with the activation of STK.
Source:
functional rolesupports
Truncation of the A'α-helix and Ala substitutions at Glu474 and Lys475 in the LOV2 A'α/Aβ gap impair blue-light-induced activation of the serine/threonine kinase in Arabidopsis thaliana phot1 LOV2-STK polypeptides.
Using LOV2-STK polypeptides from Arabidopsis thaliana phot1, we found that truncation of the A'α-helix and amino acid substitutions at Glu474 and Lys475 in the gap between the A'α and the Aβ strand of LOV2 (A'α/Aβ gap) to Ala impaired the BL-induced activation of the STK, although they did not affect S390 formation.
Source:
light dependent structural changesupports
Light-dependent trypsin digestion at Lys603 and Lys475 indicates blue-light-induced structural changes in both the Jα-helix and the A'α/Aβ gap.
Trypsin digested the LOV2-STK at Lys603 and Lys475 in a light-dependent manner indicating BL-induced structural changes in both the Jα-helix and the gap. The digestion at Lys603 is faster than at Lys475.
Source:
mechanistic separationsupports
The A'α-helix truncation and Glu474Ala/Lys475Ala substitutions impair blue-light-induced kinase activation without affecting S390 formation.
truncation of the A'α-helix and amino acid substitutions at Glu474 and Lys475 in the gap between the A'α and the Aβ strand of LOV2 (A'α/Aβ gap) to Ala impaired the BL-induced activation of the STK, although they did not affect S390 formation.
Source:
signal propagation failure pointsupports
In Glu474Ala and Lys475Ala substitutes, the blue-light signal reaches the Jα-helix and the A'α/Aβ gap but does not activate the kinase.
These BL-induced structural changes were observed with the Glu474Ala and the Lys475Ala substitutes, indicating that the BL signal reached the Jα-helix as well as the A'α/Aβ gap but could not activate STK.
Source:
Comparisons
Source-backed strengths
Functional evidence shows that truncation of the A'α-helix and Ala substitutions at Glu474 and Lys475 impair blue-light-induced activation of the serine/threonine kinase in Arabidopsis phot1 LOV2-STK polypeptides. Conservation of Glu474 and Lys475 among higher-plant phototropins further supports a biologically relevant role for this region in signal transmission.
Ranked Citations
- 1.