Functional identification of two Glycerol-3-phosphate Acyltransferase5 homologs from Chenopodium quinoa.

Autor: Wang Z; College of Life Sciences, Shandong Normal University, Jinan 250014, China., Liu Y; College of Life Sciences, Shandong Normal University, Jinan 250014, China., Huang H; State Key Laboratory of Biocatalysis and Enzyme Engineering, School of Life Sciences, Hubei University, Wuhan 430062, China., Zheng Z; The Key Laboratory for Quality Improvement of Agricultural Products of Zhejiang Province, College of Advanced Agricultural Sciences, Zhejiang A&F University, Hangzhou 311300, China., Lü S; State Key Laboratory of Biocatalysis and Enzyme Engineering, School of Life Sciences, Hubei University, Wuhan 430062, China., Yang X; College of Life Sciences, Shandong Normal University, Jinan 250014, China; National Center of Technology Innovation for Comprehensive Utilization of Saline-Alkali Land, Dongying 257000, China. Electronic address: yangxp2006@sdnu.edu.cn., Ma C; College of Life Sciences, Shandong Normal University, Jinan 250014, China; National Center of Technology Innovation for Comprehensive Utilization of Saline-Alkali Land, Dongying 257000, China. Electronic address: machangle@sdnu.edu.cn.
Jazyk: angličtina
Zdroj: Plant science : an international journal of experimental plant biology [Plant Sci] 2025 Jan; Vol. 350, pp. 112313. Date of Electronic Publication: 2024 Nov 07.
DOI: 10.1016/j.plantsci.2024.112313
Abstrakt: Glycerol-3-phosphate acyltransferase5 (GPAT5) is the key enzyme in suberin biosynthesis in Arabidopsis, tomato and Sarracenia purpurea. However, little is known about whether GPAT5 function is conserved in halophytes. In this study, we identified two GPAT5 homologs, CqGPAT5a and CqGPAT5b, in Chenopodium quinoa, the typical halophyte. Using RT-qPCR, we found that CqGPAT5a and CqGPAT5b were highly expressed in quinoa roots and rapidly induced by high salt stress. CqGPAT5a and CqGPAT5b were localized to the endoplasmic reticulum and found to have glycerol-3-phosphate acyltransferase activity using yeast complementation assays. Compared with CqGPAT5b, CqGPAT5a showed relatively weaker function and less protein abundance when expressed in yeast, Arabidopsis or Nicotiana benthamiana. Subsequently, we identified a serine (S) to leucine (L) variation in the CqGPAT5a protein sequence (S251L) compared with CqGPAT5b, located in the connecting region between the second and third transmembrane domains. Site-directed mutagenesis together with yeast mutant complementation and transient expression in tobacco demonstrated that this variation significantly affected CqGPAT5a activity and protein abundance. These findings expand our understanding of GPAT5 and provide new evidence that GPAT5 may be functionally conserved in halophytes.
Competing Interests: Declaration of Competing Interest All co-authors have read the manuscript and agree with the content, and there are no competing financial interests. We certify that the manuscript is original, has not been previously published, and is not currently submitted for review by any other journal.
(Copyright © 2024 Elsevier B.V. All rights reserved.)
Databáze: MEDLINE
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