Dehydrin Client Proteins Identified Using Phage Display Affinity Selected Libraries Processed With Paired-End Phage Sequencing

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Autor(es): dc.contributorUniversity of Kentucky-
Autor(es): dc.contributorUniversidade Estadual Paulista (UNESP)-
Autor(es): dc.contributorPastotech Pasture Seeds-
Autor(es): dc.contributorUniversity of Texas Rio Grande Valley-
Autor(es): dc.contributorCatalent Pharma Solution-
Autor(es): dc.contributorUniversity of Kentucky Agricultural and Medical Biotechnology Program-
Autor(es): dc.contributorKentucky Tobacco Research and Development Center-
Autor(es): dc.contributorFayette County Public Schools (FCPS)-
Autor(es): dc.contributorSchool of Medicine-
Autor(es): dc.contributorSKUAST- Kashmir-
Autor(es): dc.creatorUnêda-Trevisoli, Sandra Helena-
Autor(es): dc.creatorDirk, Lynnette M.A.-
Autor(es): dc.creatorPereira, Francisco Elder Carlos Bezerra-
Autor(es): dc.creatorChakrabarti, Manohar-
Autor(es): dc.creatorHao, Guijie-
Autor(es): dc.creatorCampbell, James M.-
Autor(es): dc.creatorNayakwadi, Sai Deepshikha Bassetti-
Autor(es): dc.creatorMorrison, Ashley-
Autor(es): dc.creatorJoshi, Sanjay-
Autor(es): dc.creatorPerry, Sharyn E.-
Autor(es): dc.creatorSharma, Vijyesh-
Autor(es): dc.creatorMensah, Caleb-
Autor(es): dc.creatorWillard, Barbara-
Autor(es): dc.creatorde Lorenzo, Laura-
Autor(es): dc.creatorAfroza, Baseerat-
Autor(es): dc.creatorHunt, Arthur G.-
Autor(es): dc.creatorKawashima, Tomokazu-
Autor(es): dc.creatorVaillancourt, Lisa-
Autor(es): dc.creatorPinheiro, Daniel Guariz-
Autor(es): dc.creatorDownie, A. Bruce-
Data de aceite: dc.date.accessioned2025-08-21T19:39:22Z-
Data de disponibilização: dc.date.available2025-08-21T19:39:22Z-
Data de envio: dc.date.issued2025-04-29-
Data de envio: dc.date.issued2024-11-30-
Fonte completa do material: dc.identifierhttp://dx.doi.org/10.1016/j.mcpro.2024.100867-
Fonte completa do material: dc.identifierhttps://hdl.handle.net/11449/300893-
Fonte: dc.identifier.urihttp://educapes.capes.gov.br/handle/11449/300893-
Descrição: dc.descriptionThe late embryogenesis abundant proteins (LEAPs) are a class of noncatalytic, intrinsically disordered proteins with a malleable structure. Some LEAPs exhibit a protein and/ or membrane binding capacity and LEAP binding to various targets has been positively correlated with abiotic stress tolerance. Regarding the LEAPs’ presumptive role in protein protection, identifying client proteins (CtPs) to which LEAPs bind is one practicable means of revealing the mechanism by which they exert their function. To this end, we used phage display affinity selection to screen libraries derived from Arabidopsis thaliana seed mRNA with recombinant orthologous LEAPs from Arabidopsis and soybean (Glycine max). Subsequent high-throughput sequencing of DNA from affinity-purified phage was performed to characterize the entire subpopulation of phage retained by each LEAP ortholog. This entailed cataloging in-frame fusions, elimination of false positives, and aligning the hits on the CtP scaffold to reveal domains of respective CtPs that bound to orthologous LEAPs. This approach (paired-end phage sequencing) revealed a subpopulation of the proteome constituting the CtP repertoire in common between the two dehydrin orthologs (LEA14 and GmPm12) compared to bovine serum albumin (unrelated binding control). The veracity of LEAP:CtP binding for one of the CtPs (LEA14 and GmPM12 self-association) was independently assessed using temperature-related intensity change analysis. Moreover, LEAP:CtP interactions for four other CtPs were confirmed in planta using bimolecular fluorescence complementation assays. The results provide insights into the involvement of the dehydrin Y-segments and K-domains in protein binding.-
Descrição: dc.descriptionDepartment of Horticulture Martin-Gatton College of Agriculture Food and Environment University of Kentucky-
Descrição: dc.descriptionSeed Biology Program University of Kentucky-
Descrição: dc.descriptionDepartment of Crop Production São Paulo State University (Unesp) School of Agricultural and Veterinarian Sciences-
Descrição: dc.descriptionPastotech Pasture Seeds, Mato Grosso do Sul-
Descrição: dc.descriptionSchool of Integrative Biological and Chemical Sciences University of Texas Rio Grande Valley-
Descrição: dc.descriptionDepartment of Plant and Soil Science Martin-Gatton College of Agriculture Food and Environment University of Kentucky-
Descrição: dc.descriptionCatalent Pharma Solution-
Descrição: dc.descriptionUniversity of Kentucky Agricultural and Medical Biotechnology Program-
Descrição: dc.descriptionDepartment of Toxicology and Cancer Biology College of Medicine University of Kentucky-
Descrição: dc.descriptionKentucky Tobacco Research and Development Center-
Descrição: dc.descriptionCarter G. Woodson Academy Fayette County Public Schools (FCPS)-
Descrição: dc.descriptionDepartment of Biochemistry and Molecular Biology University of New Mexico School of Medicine-
Descrição: dc.descriptionDivision of Vegetable Science SKUAST- Kashmir, Kashmir-
Descrição: dc.descriptionDepartment of Plant Pathology Martin-Gatton College of Agriculture Food and Environment University of Kentucky-
Descrição: dc.descriptionDepartment of Agricultural Livestock and Environmental Biotechnology São Paulo State University (UNESP) School of Agricultural and Veterinary Sciences, São Paulo-
Descrição: dc.descriptionDepartment of Crop Production São Paulo State University (Unesp) School of Agricultural and Veterinarian Sciences-
Descrição: dc.descriptionDepartment of Agricultural Livestock and Environmental Biotechnology São Paulo State University (UNESP) School of Agricultural and Veterinary Sciences, São Paulo-
Idioma: dc.languageen-
Relação: dc.relationMolecular and Cellular Proteomics-
???dc.source???: dc.sourceScopus-
Título: dc.titleDehydrin Client Proteins Identified Using Phage Display Affinity Selected Libraries Processed With Paired-End Phage Sequencing-
Tipo de arquivo: dc.typelivro digital-
Aparece nas coleções:Repositório Institucional - Unesp

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