Bicupin domain protein (BCD) family, an important component of Cupin domain superfamily, plays important roles in oxalic acid (OA) degradation and stress responses in high plants. However, no studies have been reported on the Cupin domain family in cotton up till now. In our study, a total 110 proteins including Cupin domain were identified from the upland cotton (Gossypium hirsutum). Among them, 17 proteins contained Bicupin domain. Subsequently, we found that V. dahliae produces OA leading to cotton leaf wilting. RT-qPCR analysis of GhBCDs revealed that OA and V. dahliae Vd080 significantly enhanced the expression of GhBCD11. The Virus-induced gene silencing and overexpression analysis showed that GhBCD11 positively regulates plant resistance to V. dahliae. Subcellular localization showed GhBCD11 located on the plasma membrane. The analysis of expression pattern showed that GhBCD11 can be induced via hormone-mediated signal pathway including salicylic acid (SA), ethephon (ET), methyl jasmonate (JA) and abscisic acid (ABA). In addition, we identified an interaction between 60 S ribosomal protein GhRPL12-3 and GhBCD11 by yeast double hybridization. Overall, this is the first study, where we identified Cupin domain family in cotton, clarified the role of GhBCD11 in cotton for resistance to V. dahliae and found an interaction between GhRPL12-3 and GhBCD11.
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http://dx.doi.org/10.1016/j.plantsci.2023.111875 | DOI Listing |
J Phys Chem B
December 2024
St Petersburg State University, St. Petersburg 199034, Russia.
The adsorption layers of cupin-1.1, one of the two evolutionary conserved β-barrel domains of vicilin─the garden pea storage globulin─at the liquid-gas interface were studied by a few methods of the surface chemistry. The kinetic dependencies of the surface pressure of cupin-1.
View Article and Find Full Text PDFEnzyme Microb Technol
January 2025
Cell Biology Department, Enzymology Laboratory, University of Brasilia, Brasilia, DF 70910-900, Brazil. Electronic address:
Chem Commun (Camb)
October 2024
Institut für Pharmazeutische Biologie und Biotechnologie, Fachbereich Pharmazie, Philipps-Universität Marburg, Marburg 35037, Germany.
Previous studies demonstrated the requirement of four enzymes including a cupin-domain containing protein for the formation of alkyl salicylaldehydes and derivatives. Heterologous expression of three biosynthetic genes from resulted in the formation of such compounds in high-yields without involvement of a cupin analogue.
View Article and Find Full Text PDFUltrason Sonochem
November 2024
Northeast Agricultural University, Harbin, Heilongjiang, 150030, China. Electronic address:
Protein hydrolysates have attracted much attention for their high biological activity and are a crucial product form for the utilization of foxtail millet bran by-products. In this study, changes in the structure, functionality, activity and peptide profile of foxtail millet bran protein hydrolysates (FMBPHs) at different ultrasound powers (0 - 600 W) were investigated. The results showed that ultrasound promoted the transformation of α-helix and β-sheet to random coils and β-turn, and the exposure of hydrophobic groups and sulfhydryl groups in FMBPHs.
View Article and Find Full Text PDFJ Am Chem Soc
July 2024
Department of Chemistry, University of Texas at Austin, Austin, Texas 78712, United States.
Aerocyanidin and amycomicin are two antibiotics derived from long-chain acids with a rare epoxy isonitrile moiety, the complexity of which renders the total synthesis of these two natural products rather challenging. How this functionality is biosynthesized has also remained obscure. While the biosynthetic gene clusters for these compounds have been identified, both appear to be deficient in genes encoding enzymes seemingly necessary for the oxidative modifications observed in these antibiotics.
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