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Integrative bioinformatics approaches reveal key hub genes in cyanobacteria: insights from Synechocystis sp. PCC 6803 and Geminocystis sp. NIES-3708 under abiotic stress conditions.
Genes Genomics
January 2025
Department of Molecular Biosciences, Wenner-Gren Institute, Stockholm University, 106 91, Stockholm, Sweden.
Background: Cyanobacteria, particularly Synechocystis sp. PCC 6803, serve as model organisms for studying acclimation strategies that enable adaptation to various environmental stresses. Understanding the molecular mechanisms underlying these adaptations provides insight into how cells adjust gene expression in response to challenging conditions.
View Article and Find Full Text PDFMolecular glue for phycobilisome attachment to photosystem II in sp. PCC 7002.
Proc Natl Acad Sci U S A
January 2025
State Key Laboratory of Protein and Plant Genetic Engineering, School of Life Science, Peking University, Beijing 100871, People's Republic of China.
Phycobilisomes (PBS) are the major photosynthetic light-harvesting complexes in cyanobacteria and red algae. While the structures of PBS have been determined in atomic resolutions, how PBS are attached to the reaction centers of photosystems remains less clear. Here, we report that a linker protein (LcpA) is required for the attachment of PBS to photosystem II (PSII) in the cyanobacterium sp.
View Article and Find Full Text PDFAssociations between water exposure and the development of amyotrophic lateral sclerosis: a matched case-control study.
Amyotroph Lateral Scler Frontotemporal Degener
January 2025
Stan Cassidy Centre for Rehabilitation, Fredericton, New Brunswick, Canada.
Objective: Previous studies have hinted at an association between water exposure and the development of ALS. However, proximity measures to these water sources have been limited to questionnaires or large buffers due to a lack of fine geospatial measures. They also do not distinguish the various classes of hydrographic features.
View Article and Find Full Text PDFTwo-Photon-Driven Photoprotection Mechanism in Echinenone-Functionalized Orange Carotenoid Protein.
J Am Chem Soc
January 2025
Max Planck Institute for Medical Research, Jahnstr. 29, Heidelberg 69120, Germany.
Orange carotenoid protein (OCP) is a photoactive protein that mediates photoprotection in cyanobacteria. OCP binds different ketocarotenoid chromophores such as echinenone (ECN), 3'- hydroxyechinenone (hECN), and canthaxanthin (CAN). In the dark, OCP is in an inactive orange form known as OCP; upon illumination, a red active state is formed, referred to as OCP, that can interact with the phycobilisome.
View Article and Find Full Text PDFEngineering hydrogen bonding at tyrosine-201 in the orange carotenoid protein using halogenated analogues.
Photosynth Res
January 2025
Faculty of Biology, Lomonosov Moscow State University, Moscow, Russia.
The Orange Carotenoid Protein (OCP) is a unique water-soluble photoactive protein that plays a critical role in regulating the balance between light harvesting and photoprotective responses in cyanobacteria. The challenge in understanding OCP´s photoactivation mechanism stems from the heterogeneity of the initial configurations of its embedded ketocarotenoid, which in the dark-adapted state can form up to two hydrogen bonds to critical amino acids in the protein's C-terminal domain, and the extremely low quantum yield of primary photoproduct formation. While a series of experiments involving point mutations within these contacts helped us to identify these challenges, they did not resolve them.
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