CYB5A

更新于：2025-05-07

基本信息

别名

CYB5、CYB5A、Cytochrome b5

+ [3]

简介

Cytochrome b5 is a membrane-bound hemoprotein functioning as an electron carrier for several membrane-bound oxygenases.

关联

100 项与 CYB5A 相关的临床结果

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100 项与 CYB5A 相关的转化医学

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0 项与 CYB5A 相关的专利（医药）

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2,144

项与 CYB5A 相关的文献（医药）

2025-06-01·Gene

ZmCYB5-1, a cytochrome b5 Gene, negatively regulates drought stress tolerance in maize

Article

作者: Tan, Xiaoting ; Che, Ronghui ; Li, Hui ; Meng, Xiaona

Cytochrome b5 proteins (CYB5s), integral components of electron transport systems, are well-documented mediators in plant-specific fatty acid biogenesis and cuticular lipid deposition. However, the mechanisms through which CYB5 genes modulate drought stress responses in maize remain poorly understood. In this study, we identified a novel drought-responsive gene designated as ZmCYB5-1 and characterized its role in drought adaptation. The transcriptional profile of ZmCYB5-1 was found to be significant down-regulated by both drought stress and abscisic acid (ABA). Sequence analysis revealed that ZmCYB5-1 possesses the conserved cytochrome b5 domain characteristic of this protein family. Transient expression assays in tobacco epidermal cells confirmed that ZmCYB5-1 is predominantly localized in the cytoplasm and nucleus. Strikingly, transgenic maize plants overexpressing ZmCYB5-1 displayed markedly reduced drought tolerance compared to wild-type controls. Transcriptomic profiling under drought stress conditions demonstrated that the overexpression line exhibited significant downregulation of genes related to three key biological processes: ABA signal transduction pathways, stress response mechanisms, and photosynthetic apparatus. Collectively, our findings provide compelling evidence that ZmCYB5-1 acts as a negative regulator of drought stress responses in maize, highlighting its potential as a promising genetic engineering target for improving drought resistance through gene-editing approaches.

2025-05-01·Insect Biochemistry and Molecular Biology

Sex pheromone biosynthesis in the Oriental fruit moth Grapholita molesta involves Δ8 desaturation

Article

作者: Ding, Bao-Jian ; Löfstedt, Christer ; Heckel, David G ; Dam, Marie Inger ; Groot, Astrid T ; Brauburger, Kristina ; Wang, Hong-Lei ; Powell, Daniel

The Oriental fruit moth Grapholita molesta is distributed throughout temperate regions and considered to be a pest in peach production and other high-value fruit crops in the rose family. Insecticide treatment has led to resistance development, but the use of sex pheromones in pest management has shown great promise. We investigated the pheromone biosynthesis pathway in G. molesta with the aim of elucidating pheromone evolution in the Olethreutinae subfamily of moths and harnessing pathway genes in biotechnological production of sex pheromone for use in pest management. In vivo labelling experiments suggested that an uncommon Δ8 fatty acyl desaturase is involved in sex pheromone biosynthesis. CRISPR/Cas9 knock-out of the highly expressed candidate desaturase gene Gmol_CPRQ almost completely blocked the production of Δ8 pheromone components in vivo. Heterologous expression of Gmol_CPRQ protein in yeast- or Sf9 insect cells, however, failed to demonstrate the expected Δ8 desaturase activity. Instead, Δ9 desaturase activity was observed. Co-expression in the yeast system of the electron donor, cytochrome b5, from G. molesta still produced only Δ9 desaturase activity. We suggest that Gmol_CPRQ is intimately involved in pheromone production in vivo, via an unknown reaction mechanism that may possibly involve another co-factor that is absent in the yeast and Sf9 expression systems, or depend on its subcellular site of activity. Solving this puzzle will shed further light on pheromone biosynthesis in the family Tortricidae and will be required for successful biotechnological production of fatty acids and pheromones requiring Δ8 desaturation.

2025-04-01·ChemPhysChem

Iron‐Histidine Coordination in Cytochrome b5: A Local Vibrational Mode Study

Article

作者: Kraka, Elfi ; Fleming, Kevin ; Freindorf, Marek

AbstractFor a series of cytochrome b5 proteins isolated from various species, including bacteria, animals, and humans, we analyzed the intrinsic strength of their distal/proximal FeN bonds and the intrinsic stiffness of their axial NFeN bond angles. To assess intrinsic bond strength and bond angle stiffness, we employed local vibrational stretching force constants ka(FeN) and bending force constants ka(NFeN) derived from the local mode theory developed by our group; the ferric and ferrous oxidation states of the heme Fe were considered. All calculations were conducted with the QM/MM methodology. We found that the reduction of the heme Fe from the ferric to the ferrous state makes the FeN axial bonds weaker, longer, less covalent, and less polar. Additionally, the axial NFeN bond angle becomes stiffer and less flexible. Local mode force constants turned out to be far more sensitive to the protein environment than geometries; evaluating force constant trends across diverse protein groups and monitoring changes in the axial heme‐framework revealed redox‐induced changes to the primary coordination sphere of the protein. These results indicate that local mode force constants can serve as useful feature data for training machine learning models that predict cytochrome b5 redox potentials, which currently rely more on geometric data and qualitative descriptors of the protein environment. The insights gained through our investigation also offer valuable guidance for strategically fine‐tuning artificial cytochrome b5 proteins and designing new, versatile variants.

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