Comput Math Methods Med - Uses of phage display in agriculture: sequence analysis and comparative modeling of late embryogenesis abundant client proteins suggest protein-nucleic acid binding functionality.

Tópicos

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Resumo

A group of intrinsically disordered, hydrophilic proteins-Late Embryogenesis Abundant (LEA) proteins-has been linked to survival in plants and animals in periods of stress, putatively through safeguarding enzymatic function and prevention of aggregation in times of dehydration/heat. Yet despite decades of effort, the molecular-level mechanisms defining this protective function remain unknown. A recent effort to understand LEA functionality began with the unique application of phage display, wherein phage display and biopanning over recombinant Seed Maturation Protein homologs from Arabidopsis thaliana and Glycine max were used to retrieve client proteins at two different temperatures, with one intended to represent heat stress. From this previous study, we identified 21 client proteins for which clones were recovered, sometimes repeatedly. Here, we use sequence analysis and homology modeling of the client proteins to ascertain common sequence and structural properties that may contribute to binding affinity with the protective LEA protein. Our methods uncover what appears to be a predilection for protein-nucleic acid interactions among LEA client proteins, which is suggestive of subcellular residence. The results from this initial computational study will guide future efforts to uncover the protein protective mechanisms during heat stress, potentially leading to phage-display-directed evolution of synthetic LEA molecules.

Resumo Limpo

group intrins disord hydrophil proteinsl embryogenesi abund lea proteinsha link surviv plant anim period stress putat safeguard enzymat function prevent aggreg time dehydrationheat yet despit decad effort molecularlevel mechan defin protect function remain unknown recent effort understand lea function began uniqu applic phage display wherein phage display biopan recombin seed matur protein homolog arabidopsi thaliana glycin max use retriev client protein two differ temperatur one intend repres heat stress previous studi identifi client protein clone recov sometim repeat use sequenc analysi homolog model client protein ascertain common sequenc structur properti may contribut bind affin protect lea protein method uncov appear predilect proteinnucl acid interact among lea client protein suggest subcellular resid result initi comput studi will guid futur effort uncov protein protect mechan heat stress potenti lead phagedisplaydirect evolut synthet lea molecul

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