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1.
Plant J ; 118(6): 2154-2168, 2024 Jun.
Artigo em Inglês | MEDLINE | ID: mdl-38558071

RESUMO

Verticillium wilt (VW) is a devasting disease affecting various plants, including upland cotton, a crucial fiber crop. Despite its impact, the genetic basis underlying cotton's susceptibility or defense against VW remains unclear. Here, we conducted a genome-wide association study on VW phenotyping in upland cotton and identified a locus on A13 that is significantly associated with VW resistance. We then identified a cystathionine ß-synthase domain gene at A13 locus, GhCBSX3A, which was induced by Verticillium dahliae. Functional analysis, including expression silencing in cotton and overexpression in Arabidopsis thaliana, confirmed that GhCBSX3A is a causal gene at the A13 locus, enhancing SAR-RBOHs-mediated apoplastic oxidative burst. We found allelic variation on the TATA-box of GhCBSX3A promoter attenuated its expression in upland cotton, thereby weakening VW resistance. Interestingly, we discovered that altered artificial selection of GhCBSX3A_R (an elite allele for VW) under different VW pressures during domestication and other improved processes allows specific human needs to be met. Our findings underscore the importance of GhCBSX3A in response to VW, and we propose a model for defense-associated genes being selected depending on the pathogen's pressure. The identified locus and gene serve as promising targets for VW resistance enhancement in cotton through genetic engineering.


Assuntos
Ascomicetos , Resistência à Doença , Gossypium , Doenças das Plantas , Proteínas de Plantas , Gossypium/genética , Gossypium/microbiologia , Gossypium/imunologia , Gossypium/metabolismo , Resistência à Doença/genética , Doenças das Plantas/microbiologia , Doenças das Plantas/imunologia , Doenças das Plantas/genética , Ascomicetos/fisiologia , Proteínas de Plantas/genética , Proteínas de Plantas/metabolismo , Estudo de Associação Genômica Ampla , Explosão Respiratória , Regulação da Expressão Gênica de Plantas , Arabidopsis/genética , Arabidopsis/microbiologia , Arabidopsis/imunologia , Arabidopsis/metabolismo , Cistationina beta-Sintase/genética , Cistationina beta-Sintase/metabolismo , Plantas Geneticamente Modificadas , Verticillium
2.
J Am Chem Soc ; 146(17): 11657-11668, 2024 May 01.
Artigo em Inglês | MEDLINE | ID: mdl-38641862

RESUMO

All protein-directed syntheses of metal nanoclusters (NCs) and nanoparticles (NPs) have attracted considerable attention because protein scaffolds provide a unique metal coordination environment and can adjust the shape and morphology of NCs and NPs. However, the detailed formation mechanisms of NCs or NPs directed by protein templates remain unclear. In this study, by taking advantage of the ferritin nanocage as a biotemplate to monitor the growth of Fe-O NCs as a function of time, we synthesized a series of iron NCs with different sizes and shapes and subsequently solved their corresponding three-dimensional atomic-scale structures by X-ray protein crystallography and cryo-electron microscopy. The time-dependent structure analyses revealed the growth process of these Fe-O NCs with the 4-fold channel of ferritin as nucleation sites. To our knowledge, the newly biosynthesized Fe35O23Glu12 represents the largest Fe-O NCs with a definite atomic structure. This study contributes to our understanding of the formation mechanism of iron NCs and provides an effective method for metal NC synthesis.


Assuntos
Ferritinas , Tamanho da Partícula , Ferritinas/química , Nanopartículas Metálicas/química , Ferro/química , Modelos Moleculares , Cristalografia por Raios X , Compostos Férricos/química
3.
J Agric Food Chem ; 71(1): 934-943, 2023 Jan 11.
Artigo em Inglês | MEDLINE | ID: mdl-36576327

RESUMO

The extension peptide (EP) is the most distinctive feature of mature plant ferritin. Some EPs have exhibited serine-like protease activity, which is associated with iron uptake and release. EP forms a helix and a long loop, followed by a conserved core helical bundle. However, whether the EP adopts a stable or uniform folding pattern in all plants remains unclear. To clarify this, we investigated the crystal structure of ferritin-1 from Setaria italica (SiFer1), a type of monocotyledon. In our structure of SiFer1, the EP is different from other EPs in other solved structures of plant ferritins and consisted of a pair of ß-sheets, a shorter helix, and two loops, which masks two hydrophobic pockets on the outer surface of every subunit. Furthermore, sequence analysis and structure comparison suggest that the EPs in ferritins from monocotyledons may adopt a novel fold pattern, and the conformations of EPs in ferritins are alterable among different plant species. Furthermore, additional eight iron atoms were first founded binding in the fourfold channels, demonstrating the vital function of fourfold channels in iron diffusion. In all, our structure provides new clues for understanding plant ferritins and the functions of the EP.


Assuntos
Ferritinas , Setaria (Planta) , Ferritinas/química , Setaria (Planta)/metabolismo , Ferro/metabolismo , Plantas/metabolismo , Peptídeos/metabolismo
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