Source 1review2024Annual Review of Microbiology
Toolkit/cyanobacteriochrome
cyanobacteriochrome
Also known as: CBCR, CBCRs, cyanobacteriochrome proteins
Taxonomy: Mechanism Branch / Component. Workflows sit above the mechanism and technique branches rather than replacing them.
Summary
Cyanobacteriochromes are cyanobacterial photoreceptor proteins built around a bilin-binding GAF domain related to phytochromes. They sense colors of light distinct from canonical phytochromes and have been applied in synthetic biology, including as the basis for an engineered near-infrared fluorescent protein tag.
Usefulness & Problems
Why this is useful
CBCRs are useful as genetically encoded light-responsive protein domains because they expand the spectral range of photoreception beyond canonical phytochromes. The cited review also places them in synthetic biology applications, and one cited study shows that a CBCR scaffold can be engineered into a small near-infrared fluorescent tag for spectral multiplexing.
Source:
This review examines spectral tuning, photoconversion, and photobiology of CBCRs and recent developments in understanding their evolution and in applying them in synthetic biology.
Source:
Cyanobacteria also contain distantly related cyanobacteriochrome (CBCR) proteins that share the bilin-binding GAF domain of phytochromes but sense other colors of light.
Problem solved
CBCRs help address the need for photoreceptor modules that detect light colors other than those sensed by canonical phytochromes. The cited engineering example further addresses the need for compact near-infrared fluorescent tags for multiplexed imaging.
Source:
This review examines spectral tuning, photoconversion, and photobiology of CBCRs and recent developments in understanding their evolution and in applying them in synthetic biology.
Taxonomy & Function
Primary hierarchy
Mechanism Branch
Component: A low-level protein part used inside a larger architecture that realizes a mechanism.
Techniques
Directed EvolutionTarget processes
signalingInput: Light
Implementation Constraints
CBCRs contain a bilin-binding GAF domain, so implementation depends at minimum on a construct that preserves this chromophore-binding photosensory module. The evidence supports use in cyanobacterial signaling contexts and as a starting scaffold for engineered near-infrared fluorescent tags, but it does not specify expression systems, chromophore supplementation strategies, or construct architectures for particular applications.
The supplied evidence is broad at the family level and does not define a single CBCR variant, spectral state pair, or quantitative performance metrics for a specific tool implementation. Practical constraints such as required bilin availability, switching kinetics, dynamic range, and host-dependent behavior are not described in the provided evidence.
Validation
Cell-freeBacteriaMammalianMouseHumanTherapeuticIndep. Replication
Supporting Sources
Source 2primary paper2019Nature Communications
Ranked Claims
The review describes recent developments in applying CBCRs in synthetic biology.
This review examines spectral tuning, photoconversion, and photobiology of CBCRs and recent developments in understanding their evolution and in applying them in synthetic biology.
The review describes recent developments in applying CBCRs in synthetic biology.
This review examines spectral tuning, photoconversion, and photobiology of CBCRs and recent developments in understanding their evolution and in applying them in synthetic biology.
The review describes recent developments in applying CBCRs in synthetic biology.
This review examines spectral tuning, photoconversion, and photobiology of CBCRs and recent developments in understanding their evolution and in applying them in synthetic biology.
The review describes recent developments in applying CBCRs in synthetic biology.
This review examines spectral tuning, photoconversion, and photobiology of CBCRs and recent developments in understanding their evolution and in applying them in synthetic biology.
The review describes recent developments in applying CBCRs in synthetic biology.
This review examines spectral tuning, photoconversion, and photobiology of CBCRs and recent developments in understanding their evolution and in applying them in synthetic biology.
The review describes recent developments in applying CBCRs in synthetic biology.
This review examines spectral tuning, photoconversion, and photobiology of CBCRs and recent developments in understanding their evolution and in applying them in synthetic biology.
The review describes recent developments in applying CBCRs in synthetic biology.
This review examines spectral tuning, photoconversion, and photobiology of CBCRs and recent developments in understanding their evolution and in applying them in synthetic biology.
CBCRs regulate multiple aspects of cyanobacterial photobiology, including phototaxis, cyclic nucleotide second-messenger metabolism, and optimization of the light-harvesting apparatus.
CBCRs thus can regulate several aspects of cyanobacterial photobiology, including phototaxis, metabolism of cyclic nucleotide second messengers, and optimization of the cyanobacterial light-harvesting apparatus.
CBCRs regulate multiple aspects of cyanobacterial photobiology, including phototaxis, cyclic nucleotide second-messenger metabolism, and optimization of the light-harvesting apparatus.
CBCRs thus can regulate several aspects of cyanobacterial photobiology, including phototaxis, metabolism of cyclic nucleotide second messengers, and optimization of the cyanobacterial light-harvesting apparatus.
CBCRs regulate multiple aspects of cyanobacterial photobiology, including phototaxis, cyclic nucleotide second-messenger metabolism, and optimization of the light-harvesting apparatus.
CBCRs thus can regulate several aspects of cyanobacterial photobiology, including phototaxis, metabolism of cyclic nucleotide second messengers, and optimization of the cyanobacterial light-harvesting apparatus.
CBCRs regulate multiple aspects of cyanobacterial photobiology, including phototaxis, cyclic nucleotide second-messenger metabolism, and optimization of the light-harvesting apparatus.
CBCRs thus can regulate several aspects of cyanobacterial photobiology, including phototaxis, metabolism of cyclic nucleotide second messengers, and optimization of the cyanobacterial light-harvesting apparatus.
CBCRs regulate multiple aspects of cyanobacterial photobiology, including phototaxis, cyclic nucleotide second-messenger metabolism, and optimization of the light-harvesting apparatus.
CBCRs thus can regulate several aspects of cyanobacterial photobiology, including phototaxis, metabolism of cyclic nucleotide second messengers, and optimization of the cyanobacterial light-harvesting apparatus.
CBCRs regulate multiple aspects of cyanobacterial photobiology, including phototaxis, cyclic nucleotide second-messenger metabolism, and optimization of the light-harvesting apparatus.
CBCRs thus can regulate several aspects of cyanobacterial photobiology, including phototaxis, metabolism of cyclic nucleotide second messengers, and optimization of the cyanobacterial light-harvesting apparatus.
CBCRs regulate multiple aspects of cyanobacterial photobiology, including phototaxis, cyclic nucleotide second-messenger metabolism, and optimization of the light-harvesting apparatus.
CBCRs thus can regulate several aspects of cyanobacterial photobiology, including phototaxis, metabolism of cyclic nucleotide second messengers, and optimization of the cyanobacterial light-harvesting apparatus.
Cyanobacteriochromes are distantly related to phytochromes, share the bilin-binding GAF domain, and sense colors of light beyond red/far-red.
Cyanobacteria also contain distantly related cyanobacteriochrome (CBCR) proteins that share the bilin-binding GAF domain of phytochromes but sense other colors of light.
Cyanobacteriochromes are distantly related to phytochromes, share the bilin-binding GAF domain, and sense colors of light beyond red/far-red.
Cyanobacteria also contain distantly related cyanobacteriochrome (CBCR) proteins that share the bilin-binding GAF domain of phytochromes but sense other colors of light.
Cyanobacteriochromes are distantly related to phytochromes, share the bilin-binding GAF domain, and sense colors of light beyond red/far-red.
Cyanobacteria also contain distantly related cyanobacteriochrome (CBCR) proteins that share the bilin-binding GAF domain of phytochromes but sense other colors of light.
Cyanobacteriochromes are distantly related to phytochromes, share the bilin-binding GAF domain, and sense colors of light beyond red/far-red.
Cyanobacteria also contain distantly related cyanobacteriochrome (CBCR) proteins that share the bilin-binding GAF domain of phytochromes but sense other colors of light.
Cyanobacteriochromes are distantly related to phytochromes, share the bilin-binding GAF domain, and sense colors of light beyond red/far-red.
Cyanobacteria also contain distantly related cyanobacteriochrome (CBCR) proteins that share the bilin-binding GAF domain of phytochromes but sense other colors of light.
Cyanobacteriochromes are distantly related to phytochromes, share the bilin-binding GAF domain, and sense colors of light beyond red/far-red.
Cyanobacteria also contain distantly related cyanobacteriochrome (CBCR) proteins that share the bilin-binding GAF domain of phytochromes but sense other colors of light.
Cyanobacteriochromes are distantly related to phytochromes, share the bilin-binding GAF domain, and sense colors of light beyond red/far-red.
Cyanobacteria also contain distantly related cyanobacteriochrome (CBCR) proteins that share the bilin-binding GAF domain of phytochromes but sense other colors of light.
Photoisomerization of the bilin chromophore triggers CBCR photoconversion and modulates the biochemical signaling state of output domains.
Photoisomerization of the bilin triggers photoconversion of the CBCR input, thereby modulating the biochemical signaling state of output domains such as histidine kinase bidomains
Photoisomerization of the bilin chromophore triggers CBCR photoconversion and modulates the biochemical signaling state of output domains.
Photoisomerization of the bilin triggers photoconversion of the CBCR input, thereby modulating the biochemical signaling state of output domains such as histidine kinase bidomains
Photoisomerization of the bilin chromophore triggers CBCR photoconversion and modulates the biochemical signaling state of output domains.
Photoisomerization of the bilin triggers photoconversion of the CBCR input, thereby modulating the biochemical signaling state of output domains such as histidine kinase bidomains
Photoisomerization of the bilin chromophore triggers CBCR photoconversion and modulates the biochemical signaling state of output domains.
Photoisomerization of the bilin triggers photoconversion of the CBCR input, thereby modulating the biochemical signaling state of output domains such as histidine kinase bidomains
Photoisomerization of the bilin chromophore triggers CBCR photoconversion and modulates the biochemical signaling state of output domains.
Photoisomerization of the bilin triggers photoconversion of the CBCR input, thereby modulating the biochemical signaling state of output domains such as histidine kinase bidomains
Photoisomerization of the bilin chromophore triggers CBCR photoconversion and modulates the biochemical signaling state of output domains.
Photoisomerization of the bilin triggers photoconversion of the CBCR input, thereby modulating the biochemical signaling state of output domains such as histidine kinase bidomains
Photoisomerization of the bilin chromophore triggers CBCR photoconversion and modulates the biochemical signaling state of output domains.
Photoisomerization of the bilin triggers photoconversion of the CBCR input, thereby modulating the biochemical signaling state of output domains such as histidine kinase bidomains
CBCR photocycles span an extremely broad spectral range from near-UV to near-IR.
CBCR photocycles are extremely diverse, ranging from the near-UV to the near-IR.
CBCR photocycles span an extremely broad spectral range from near-UV to near-IR.
CBCR photocycles are extremely diverse, ranging from the near-UV to the near-IR.
CBCR photocycles span an extremely broad spectral range from near-UV to near-IR.
CBCR photocycles are extremely diverse, ranging from the near-UV to the near-IR.
CBCR photocycles span an extremely broad spectral range from near-UV to near-IR.
CBCR photocycles are extremely diverse, ranging from the near-UV to the near-IR.
CBCR photocycles span an extremely broad spectral range from near-UV to near-IR.
CBCR photocycles are extremely diverse, ranging from the near-UV to the near-IR.
CBCR photocycles span an extremely broad spectral range from near-UV to near-IR.
CBCR photocycles are extremely diverse, ranging from the near-UV to the near-IR.
CBCR photocycles span an extremely broad spectral range from near-UV to near-IR.
CBCR photocycles are extremely diverse, ranging from the near-UV to the near-IR.
A smallest near-infrared fluorescent protein was evolved from cyanobacteriochrome.
A smallest near-infrared fluorescent protein was evolved from cyanobacteriochrome.
A smallest near-infrared fluorescent protein was evolved from cyanobacteriochrome.
A smallest near-infrared fluorescent protein was evolved from cyanobacteriochrome.
A smallest near-infrared fluorescent protein was evolved from cyanobacteriochrome.
A smallest near-infrared fluorescent protein was evolved from cyanobacteriochrome.
A smallest near-infrared fluorescent protein was evolved from cyanobacteriochrome.
Approval Evidence
2 sources6 linked approval claimsfirst-pass slug cyanobacteriochrome
Cyanobacteria also contain distantly related cyanobacteriochrome (CBCR) proteins that share the bilin-binding GAF domain of phytochromes but sense other colors of light.
Source:
Smallest near-infrared fluorescent protein evolved from cyanobacteriochrome as versatile tag for spectral multiplexing
Source:
application scopesupports
The review describes recent developments in applying CBCRs in synthetic biology.
This review examines spectral tuning, photoconversion, and photobiology of CBCRs and recent developments in understanding their evolution and in applying them in synthetic biology.
Source:
biological rolesupports
CBCRs regulate multiple aspects of cyanobacterial photobiology, including phototaxis, cyclic nucleotide second-messenger metabolism, and optimization of the light-harvesting apparatus.
CBCRs thus can regulate several aspects of cyanobacterial photobiology, including phototaxis, metabolism of cyclic nucleotide second messengers, and optimization of the cyanobacterial light-harvesting apparatus.
Source:
functional scopesupports
Cyanobacteriochromes are distantly related to phytochromes, share the bilin-binding GAF domain, and sense colors of light beyond red/far-red.
Cyanobacteria also contain distantly related cyanobacteriochrome (CBCR) proteins that share the bilin-binding GAF domain of phytochromes but sense other colors of light.
Source:
mechanistic summarysupports
Photoisomerization of the bilin chromophore triggers CBCR photoconversion and modulates the biochemical signaling state of output domains.
Photoisomerization of the bilin triggers photoconversion of the CBCR input, thereby modulating the biochemical signaling state of output domains such as histidine kinase bidomains
Source:
spectral rangesupports
CBCR photocycles span an extremely broad spectral range from near-UV to near-IR.
CBCR photocycles are extremely diverse, ranging from the near-UV to the near-IR.
Source:
engineering originsupports
A smallest near-infrared fluorescent protein was evolved from cyanobacteriochrome.
Source:
Comparisons
Source-backed strengths
A key strength is their bilin-binding GAF domain architecture, which supports light sensing across colors distinct from canonical phytochromes. Biological evidence indicates that CBCRs regulate diverse cyanobacterial processes, including phototaxis, cyclic nucleotide second-messenger metabolism, and optimization of the light-harvesting apparatus, supporting their functional versatility. An additional strength is demonstrated engineerability, as a CBCR-derived scaffold yielded the smallest near-infrared fluorescent protein reported in the cited study.
Source:
A smallest near-infrared fluorescent protein was evolved from cyanobacteriochrome.
Ranked Citations
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