ArticleBMC biology2018
Two-component cyclase opsins of green algae are ATP-dependent and light-inhibited guanylyl cyclases.
Article in BMC biology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
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Who cites it
27 citing papers in PubMed, 55 citations in OpenAlex.
- Light-dependent processes in algae across scales: from cellular physiology to ecological organization.Plant physiology · 2026Review
- Septin-mediated coupling of protein import and division during chloroplast evolution.bioRxiv : the preprint server for biology · 2026Article
- Apusomonad rhodopsins: A new family of ultraviolet to blue light-absorbing rhodopsin channels.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Transcriptomic and metabolomic insights into light-mediated unicellular-to-multicellular transition inOpen biology · 2025Article
- Two Decades of Optogenetic Tools: A Retrospective and a Look Ahead.Advanced genetics (Hoboken, N.J.) · 2025Review
- Spatiotemporal distribution of the glycoprotein pherophorin II reveals stochastic geometry of the growing ECM ofProceedings of the National Academy of Sciences of the United States of America · 2025Article
- Light Affects Host-Symbiont Dynamics in the Non-Photosynthetic Social Amoeba Symbiosis.Ecology and evolution · 2025Article
- Sensing a rainbow of colors: algal photoreceptors.Frontiers in plant science · 2025Review
- COP5/HKR1 changes ciliary beat pattern and biases cell steering during chemotaxis in Chlamydomonas reinhardtii.Scientific reports · 2024Article
- Plastid-localized xanthorhodopsin increases diatom biomass and ecosystem productivity in iron-limited surface oceans.Nature microbiology · 2023Article
- Cell Type-Specific Promoters ofGenes · 2023Article
- Cell Type-Specific Pherophorins ofCells · 2022Article
- Rhodopsin-bestrophin fusion proteins from unicellular algae form gigantic pentameric ion channels.Nature structural & molecular biology · 2022Article
- Molecular and cellular dynamics of early embryonic cell divisions in Volvox carteri.The Plant cell · 2022Article
- Characterization and Modification of Light-Sensitive Phosphodiesterases from Choanoflagellates.Biomolecules · 2022Article
- Microbial Rhodopsins.Methods in molecular biology (Clifton, N.J.) · 2022Article
- Article
- PACmn for improved optogenetic control of intracellular cAMP.BMC biology · 2021Article
- Advances and prospects of rhodopsin-based optogenetics in plant research.Plant physiology · 2021Review
- Article
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
backgroundThe green algae Chlamydomonas reinhardtii and Volvox carteri are important models for studying light perception and response, expressing many different photoreceptors. More than 10 opsins were reported in C. reinhardtii, yet only two-the channelrhodopsins-were functionally characterized. Characterization of new opsins would help to understand the green algae photobiology and to develop new tools for optogenetics.
resultsHere we report the characterization of a novel opsin family from these green algae: light-inhibited guanylyl cyclases regulated through a two-component-like phosphoryl transfer, called "two-component cyclase opsins" (2c-Cyclops). We prove the existence of such opsins in C. reinhardtii and V. carteri and show that they have cytosolic N- and C-termini, implying an eight-transmembrane helix structure. We also demonstrate that cGMP production is both light-inhibited and ATP-dependent. The cyclase activity of Cr2c-Cyclop1 is kept functional by the ongoing phosphorylation and phosphoryl transfer from the histidine kinase to the response regulator in the dark, proven by mutagenesis. Absorption of a photon inhibits the cyclase activity, most likely by inhibiting the phosphoryl transfer. Overexpression of Vc2c-Cyclop1 protein in V. carteri leads to significantly increased cGMP levels, demonstrating guanylyl cyclase activity of Vc2c-Cyclop1 in vivo. Live cell imaging of YFP-tagged Vc2c-Cyclop1 in V. carteri revealed a development-dependent, layer-like structure at the immediate periphery of the nucleus and intense spots in the cell periphery.
conclusionsCr2c-Cyclop1 and Vc2c-Cyclop1 are light-inhibited and ATP-dependent guanylyl cyclases with an unusual eight-transmembrane helix structure of the type I opsin domain which we propose to classify as type Ib, in contrast to the 7 TM type Ia opsins. Overexpression of Vc2c-Cyclop1 protein in V. carteri led to a significant increase of cGMP, demonstrating enzyme functionality in the organism of origin. Fluorescent live cell imaging revealed that Vc2c-Cyclop1 is located in the periphery of the nucleus and in confined areas at the cell periphery.
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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.