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Prokaryotic expression, purification, and the in vitro and in vivo protection study of dehydrin WDHN2 from Triticum aestivum.
Zhang, Hongmei; Wu, Jiafa; Fu, Dandan; Zhang, Min; Wang, Lunji; Gong, Minggui.
Afiliación
  • Zhang H; College of Food and Bioengineering, Henan University of Science and Technology, Luoyang, 471023, Henan, China.
  • Wu J; Key Laboratory of Microbial Resources Exploitation and Utilization, Henan University of Science and Technology, Luoyang, 471023, Henan, China.
  • Fu D; College of Food and Bioengineering, Henan University of Science and Technology, Luoyang, 471023, Henan, China.
  • Zhang M; Key Laboratory of Microbial Resources Exploitation and Utilization, Henan University of Science and Technology, Luoyang, 471023, Henan, China.
  • Wang L; College of Food and Bioengineering, Henan University of Science and Technology, Luoyang, 471023, Henan, China.
  • Gong M; College of Food and Bioengineering, Henan University of Science and Technology, Luoyang, 471023, Henan, China.
Protoplasma ; 261(4): 771-781, 2024 Jul.
Article en En | MEDLINE | ID: mdl-38342804
ABSTRACT
Dehydrins proteins accumulate and play important protective roles in most plants during abiotic stresses. The objective of this study was to characterize a YSK2-type dehydrin gene, WDHN2, isolated from Triticum aestivum previously. In this work, wheat dehydrin WDHN2 was expressed in Escherichia coli and purified by immobilized metal affinity chromatography, which exhibited as a single band by sodium dodecyl sulfonate polyacrylamide gel electrophoresis and western blotting. We show that WDHN2 is capable of alleviating lactate dehydrogenase inactivation from heat and desiccation in vitro enzyme activity protection assay. In vivo assay of Escherichia coli viability demonstrates the enhancement of cell survival by the overexpression of WDHN2. The protein aggregation prevention assay explores that WDHN2 has a broad protective effect on the cellular proteome. The results show that WDHN2 is mainly accumulated in the nucleus and cytosol, suggesting that this dehydrin may exert its function in both cellular compartments. Our data suggest that WDHN2 acts as a chaperone molecular in vivo.
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Proteínas de Plantas / Triticum Idioma: En Revista: Protoplasma Asunto de la revista: BIOLOGIA Año: 2024 Tipo del documento: Article País de afiliación: China Pais de publicación: Austria
Texto completo
Añadir a Mi BVS
Imprimir
XML
PubMed Links
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Proteínas de Plantas / Triticum Idioma: En Revista: Protoplasma Asunto de la revista: BIOLOGIA Año: 2024 Tipo del documento: Article País de afiliación: China Pais de publicación: Austria