Details

Autor(en) / Beteiligte

• Wang, Haibo
• Zou, Zhurong
• Gong, Ming

Titel

Molecular Cloning, Expression Analysis, and Preliminarily Functional Characterization of the Gene Encoding Protein Disulfide Isomerase from Jatropha curcas

Ist Teil von

• Applied biochemistry and biotechnology, 2015-05, Vol.176 (2), p.428-439

Ort / Verlag

New York: Springer-Verlag

Erscheinungsjahr

2015

Link zum Volltext

Quelle

SpringerLink (Online service)

Beschreibungen/Notizen

• Reactive oxygen species (ROS) in plants, arising from various environmental stresses, impair the thiol-contained proteins that are susceptible to irregular oxidative formation of disulfide bonds, which might be alleviated by a relatively specific modifier called protein disulfide isomerase (PDI). From our previous data of the transcriptome and digital gene expression of cold-hardened Jatropha curcas, a PDI gene was proposed to be cold-relevant. In this study, its full-length cDNA (JcPDI) was cloned, with the size of 1649 bp containing the entire open reading frame (ORF) of 1515 bp. This ORF encodes a polypeptide of 504 amino acids with theoretical molecular weight of 56.6 kDa and pI value of 4.85. One N-terminal signal peptide (−MASKGSIWSCMFLFSLI VAISAGEG-) and the C-terminal anchoring sequence motif (−KDEL-) specific to the endoplasmic reticulum, as well as two thioredoxin domains (−CGHC-), are also found by predictions. Through semi-quantitative RT-PCR, the expression of JcPDI was characterized to be tissue-differential strongly in leaves and roots, but weakly in stems, and of cold-induced alternations. Furthermore, JcPDI overexpression in yeast could notably enhance the cold resistance of host cells. Conclusively, these results explicitly suggested a considerable association of JcPDI to cold response and a putative application potential for its correlated genetic engineering.