Characterization of a broad substrates specificity acyl-CoA: diacylglycerol acyltransferase 1 from the green tide alga <i>Ulva prolifera</i>

Xiaowen Zhang; Xiaoyuan Chi; Yitao Wang; Jian Zhang; Yan Zhang; Dong Xu; Xiao Fan; Chengwei Liang; Naihao Ye

doi:10.1007/s13131-020-1659-0

Volume 39 Issue 10

Oct. 2020

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Xiaowen Zhang, Xiaoyuan Chi, Yitao Wang, Jian Zhang, Yan Zhang, Dong Xu, Xiao Fan, Chengwei Liang, Naihao Ye. Characterization of a broad substrates specificity acyl-CoA: diacylglycerol acyltransferase 1 from the green tide alga Ulva prolifera[J]. Acta Oceanologica Sinica, 2020, 39(10): 42-49. doi: 10.1007/s13131-020-1659-0

Citation:

Xiaowen Zhang, Xiaoyuan Chi, Yitao Wang, Jian Zhang, Yan Zhang, Dong Xu, Xiao Fan, Chengwei Liang, Naihao Ye. Characterization of a broad substrates specificity acyl-CoA: diacylglycerol acyltransferase 1 from the green tide alga Ulva prolifera[J]. Acta Oceanologica Sinica, 2020, 39(10): 42-49. doi: 10.1007/s13131-020-1659-0

Citation:

Xiaowen Zhang, Xiaoyuan Chi, Yitao Wang, Jian Zhang, Yan Zhang, Dong Xu, Xiao Fan, Chengwei Liang, Naihao Ye. Characterization of a broad substrates specificity acyl-CoA: diacylglycerol acyltransferase 1 from the green tide alga Ulva prolifera[J]. Acta Oceanologica Sinica, 2020, 39(10): 42-49. doi: 10.1007/s13131-020-1659-0

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Characterization of a broad substrates specificity acyl-CoA: diacylglycerol acyltransferase 1 from the green tide alga Ulva prolifera

doi: 10.1007/s13131-020-1659-0

Xiaowen Zhang^{1, 2, †},
Xiaoyuan Chi^{3, †},
Yitao Wang¹,
Jian Zhang⁴,
Yan Zhang¹,
Dong Xu¹,
Xiao Fan¹,
Chengwei Liang⁴,
Naihao Ye^{1, 2
,
,}

1.
Yellow Sea Fisheries Research Institute, Chinese Academy of Fishery Sciences, Qingdao 266071, China
2.
Function Laboratory for Marine Fisheries Science and Food Production Processes, Pilot National Laboratory for Marine Science and Technology (Qingdao), Qingdao 266237, China
3.
Shandong Peanut Research Institute, Qingdao 266100, China
4.
College of Marine Science and Biological Engineering, Qingdao University of Science and Technology, Qingdao 266042, China

Funds: The National Key Research and Development Program of China under contract No.2016YFC1402102; the Central Public-interest Scientific Institution Basal Research Fund, CAFS under contract Nos 2020TD19 and 2020TD27; the Major Scientific and Technological Innovation Project of Shandong Provincial Key Research and Development Program under contract 2019JZZY020706; the International Exchange and Cooperation in Agriculture, Ministry of Agriculture and Rural Affairs of China-Science, Technology and Innovation Cooperation in Aquaculture with Tropical Countries along the Belt and Road; China Agriculture Research System under contract No. CARS-50; the Taishan Scholars Funding and Talent Projects of Distinguished Scientific Scholars in Agriculture; the National Ten Thousand Youth Talents Plan of 2014 under contract No. W02070268.

More Information

Corresponding author: E-mail: yenh@ysfri.ac.cn
Received Date: 2019-11-01
Accepted Date: 2020-04-20

Available Online: 2020-12-28

Publish Date: 2020-10-25

Abstract

Abstract

Triacylglycerols (triglycerides, TAGs) are the major carbon and energy storage forms in various organisms, and important components of cellular membranes and signaling molecules; they have essential functions in multiple physiological processes and stress regulation. Acyl-CoA: diacylglycerol acyltransferase (DGAT) catalyzes the final and only committed acylation step in the synthesis of TAGs in eukaryotes. The present work identified and isolated a novel gene, UpDGAT1, from the green tide alga Ulva prolifera. The activity of UpDGAT1 was confirmed by heterologous expression in a Saccharomyces cerevisiae TAG-deficient quadruple mutant. Results of thin-layer chromatography and BODIPY staining indicated that UpDGAT1 was able to restore TAG synthesis and lipid body formation in the yeast. Lipid analysis of yeast cells revealed that UpDGAT1 showed broad substrate specificity, accepting saturated as well as mono- and polyunsaturated acyl-CoAs as substrates. High salinity and high temperature stresses increased UpDGAT1 expression and TAG accumulation in U. prolifera. The present study provides clues to the functions of UpDGAT1 in TAG accumulation in, and stress adaptation of, U. prolifera.
- Ulva prolifera,
- diacylglycerol acyltransferase,
- triacylglycerol,
- stress

†These authors contributated equally to this work.

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References(58)

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