ArticleProceedings of the National Academy of Sciences of the United States of America2004
A eukaryotic BLUF domain mediates light-dependent gene expression in the purple bacterium Rhodobacter sphaeroides 2.4.1.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed, 61 citations in OpenAlex.
- Optophysiology: Illuminating cell physiology with optogenetics.Physiological reviews · 2022Review
- Seeing the light with BLUF proteins.Biophysical reviews · 2017Review
- Role of active site conformational changes in photocycle activation of the AppA BLUF photoreceptor.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Insights of Phage-Host Interaction in Hypersaline Ecosystem through Metagenomics Analyses.Frontiers in microbiology · 2017Article
- Members of the PpaA/AerR Antirepressor Family Bind Cobalamin.Journal of bacteriology · 2015Article
- Molecular eyes: proteins that transform light into biological information.Interface focus · 2013Review
- A ternary AppA-PpsR-DNA complex mediates light regulation of photosynthesis-related gene expression.Nature structural & molecular biology · 2013Article
- Interaction of two photoreceptors in the regulation of bacterial photosynthesis genes.Nucleic acids research · 2012Article
- Metagenomic insights into the evolution, function, and complexity of the planktonic microbial community of Lake Lanier, a temperate freshwater ecosystem.Applied and environmental microbiology · 2011Article
- Thiol-based redox switches and gene regulation.Antioxidants & redox signaling · 2011Review
- Tripping the light fantastic: blue-light photoreceptors as examples of environmentally modulated protein-protein interactions.Biochemistry · 2011Review
- In vivo sensitivity of blue-light-dependent signaling mediated by AppA/PpsR or PrrB/PrrA in Rhodobacter sphaeroides.Journal of bacteriology · 2009Article
- Discovering functional novelty in metagenomes: examples from light-mediated processes.Journal of bacteriology · 2009Review
- Light-induced hydrogen bonding pattern and driving force of electron transfer in AppA BLUF domain photoreceptor.The Journal of biological chemistry · 2008Article
- Molecular models predict light-induced glutamine tautomerization in BLUF photoreceptors.Biophysical journal · 2008Article
- The AppA and PpsR proteins from Rhodobacter sphaeroides can establish a redox-dependent signal chain but fail to transmit blue-light signals in other bacteria.Journal of bacteriology · 2007Article
- Structure of a bacterial BLUF photoreceptor: insights into blue light-mediated signal transduction.Proceedings of the National Academy of Sciences of the United States of America · 2005Article
- Structure of a novel photoreceptor, the BLUF domain of AppA from Rhodobacter sphaeroides.Biochemistry · 2005Article
- Transcriptome analysis of the Rhodobacter sphaeroides PpsR regulon: PpsR as a master regulator of photosystem development.Journal of bacteriology · 2005Article
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The flavin-binding BLUF domain functions as a blue-light receptor in eukaryotes and bacteria. In the photoreceptor protein photo-activated adenylyl cyclase (PAC) from the flagellate Euglena gracilis, the BLUF domain is linked to an adenylyl cyclase domain. The PAC protein mediates a photophobic response. In the AppA protein of Rhodobacter sphaeroides, the BLUF domain is linked to a downstream domain without similarity to known proteins. AppA functions as a transcriptional antirepressor, controlling photosynthesis gene expression in the purple bacterium R. sphaeroides in response to light and oxygen. We fused the PACalpha1-BLUF domain from Euglena to the C terminus of AppA. Our results show that the hybrid protein is fully functional in light-dependent gene repression in R. sphaeroides, despite only approximately 30% identity between the eukaryotic and the bacterial BLUF domains. Furthermore, the bacterial BLUF domain and the C terminus of AppA can transmit the light signal even when expressed as separated domains. This finding implies that the BLUF domain is fully modular and can relay signals to completely different output domains.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.