Ectopic expression of BrIQD35 promotes drought stress tolerance in Nicotiana benthamiana. (4th May 2022)

• Record Type: Journal Article
• Authors: Yuan, J.; Yu, Z.; Li, Y.; Shah, S. H. A.; Xiao, D.; Hou, X.; Li, Y.
• Editors: Luo, Z.‐B.
• Is Part Of: Plant biology. Volume 24:Number 5(2022)
• Page Start: 887
• Page End: 896
• Publication Date: 2022-05-04
• Subjects: BrIQD35 -- Chinese cabbage -- Drought stress -- Protein interaction -- Tobacco; Botany -- Periodicals; Plants -- genetics -- Periodicals; Plants -- growth & development -- Periodicals; Plant Proteins -- Periodicals; Gene Expression Regulation, Plant -- Periodicals; Botanique -- Périodiques; 580
• DOI: 10.1111/plb.13425
• Languages: English
• ISSNs: 1435-8603

Abstract

ABSTRACT: The plant IQD gene family is responsive to a variety of stresses. In this study, we studied the structural features and functions of the gene BrIQD35 in Chinese cabbage, a member of the IQD gene family. BrIQD35 was cloned and shown to contain an IQ motif. Transient expression of BrIQD35 indicated that it was localized on the plasma membrane and was significantly upregulated under drought and salt stress in Chinese cabbage. To further identify the function of BrIQD35, it was heterologously overexpressed in Nicotiana benthamiana . Although there was no significant difference between BrIQD35 ‐overexpressed and wild‐type (WT) plants under salt stress, WT N . benthamiana showed more wilting than the BrIQD35 ‐overexpressed plants under drought stress. Since the IQ motif has been annotated as a CaM binding site, yeast two‐hybrid assays were used to explore the interaction between BrIQD35 and CaM. The results indicated that BrIQD35 interacts weakly with CaMb, but not with CaMa, suggesting that BrIQD35 may function through the Ca 2+ ‐CaMb pathway. The findings reveal a novel gene involved in drought tolerance, which is important for plant breeding and quality improvement for Chinese cabbage. Abstract : Overexpression of BrIQD35 enhances drought tolerance; the BrIQD35 protein interacts differentially with Calmodulin‐a and Calmodulin‐b proteins, suggesting that it is functioning through interaction with the CaMb signalling pathway.