ArticleProtein science : a publication of the Protein Society2021
Structural basis of bilin binding by the chlorophyll biosynthesis regulator GUN4.
Article in Protein science : a publication of the Protein Society, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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11 citing papers in PubMed, 11 citations in OpenAlex.
- Metabolism and regulation of chlorophyll and carotenoids in tomato fruits.Horticulture research · 2026Article
- Carbon allocation strategy of Thalassiosira weissflogii in response to elevated pCOBMC plant biology · 2026Article
- CRISPR-enhanced microalgae biosynthesis: a promising approach for future functional feed ingredients.Journal of animal science and biotechnology · 2026Review
- Regulatory and retrograde signaling networks in the chlorophyll biosynthetic pathway.Journal of integrative plant biology · 2025Review
- Modification of aggregation-prone regions of Arabidopsis glutamyl-tRNA reductase leads to increased stability while maintaining enzyme activity.Frontiers in plant science · 2025Article
- Cyanobacteriochromes: A Rainbow of Photoreceptors.Annual review of microbiology · 2024Review
- Chlorophyll biosynthesis under the control of arginine metabolism.Cell reports · 2023Article
- GUN4 appeared early in cyanobacterial evolution.PNAS nexus · 2023Article
- Elucidating the origins of phycocyanobilin biosynthesis and phycobiliproteins.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Impact of Porphyrin Binding to GENOMES UNCOUPLED 4 on Tetrapyrrole BiosynthesisFrontiers in plant science · 2022Article
- Structural basis of bilin binding by the chlorophyll biosynthesis regulator GUN4.Protein science : a publication of the Protein Society · 2021Article
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8 authors at 3 institutions in 2 countries.
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No grant is acknowledged in the PubMed record.
Abstract
The chlorophyll biosynthesis regulator GENOMES UNCOUPLED 4 (GUN4) is conserved in nearly all oxygenic photosynthetic organisms. Recently, GUN4 has been found to be able to bind the linear tetrapyrroles (bilins) and stimulate the magnesium chelatase activity in the unicellular green alga Chlamydomonas reinhardtii. Here, we characterize GUN4 proteins from Arabidopsis thaliana and the cyanobacterium Synechocystis sp. PCC 6803 for their ability to bind bilins, and present the crystal structures of Synechocystis GUN4 in biliverdin-bound, phycocyanobilin-bound, and phytochromobilin-bound forms at the resolutions of 1.05, 1.10, and 1.70 Å, respectively. These linear molecules adopt a cyclic-helical conformation, and bind more tightly than planar porphyrins to the tetrapyrrole-binding pocket of GUN4. Based on structural comparison, we propose a working model of GUN4 in regulation of tetrapyrrole biosynthetic pathway, and address the role of the bilin-bound GUN4 in retrograde signaling.
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