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Microalgal plastidial lysophosphatidic acid acyltransferase interacts with upstream glycerol-3-phosphate acyltransferase and defines its substrate selectivity via the two transmembrane domains
Huang, Linfei1,6; Yu, Lihua1; Li, Zhongze1,6; Li, Yanhua1; Yoon, Kang-sup1; Hu, Qiang1,2,3,4,5,7,8; Yuan, Li1; Han, Danxiang1,4,5
Corresponding AuthorYuan, Li(liyuan@ihb.ac.cn) ; Han, Danxiang(danxianghan@ihb.ac.cn)
2020
Source PublicationALGAL RESEARCH-BIOMASS BIOFUELS AND BIOPRODUCTS
ISSN2211-9264
Volume45Pages:11
AbstractThe plastidial lysophosphatidic acid acyltransferase of the unicellular green alga Chlamydomonas reinhardtii (CrLPAAT1) is a key enzyme involved in triacylglycerol biosynthesis. However, research on the biochemical characteristics of CrLPAAT1 has been impeded by its membrane-bound nature. In this study, the recombinant CrLPAAT1 was purified in a soluble form and was utilized for comprehensive biochemical characterization. The recombinant CrLPAAT1 favors the conditions of pH 6.5-7.5, 30 degrees C and the presence of magnesium ion in vitro. Similar with the CrLPAAT1 associated with the membranes, the purified CrLPAAT1 prefers to utilize C16:0-CoA over other acyl donors, whereas it showed broader substrate selectivity than the membrane-bound enzyme. By comparing the wild-type CrLPAAT1 and a transmembrane domain-truncated enzyme, it was uncovered in this study that the two transmembrane domains of CrLPAAT1 are involved in shaping its substrate preference for C16:0-CoA. Additionally, CrLPAAT1 was found to be interacting with the water-soluble plastidial glycerol-3-phosphate acyltransferase (CrGAPTcl) via its two transmembrane domains in vitro. The interaction between CrLPAAT1 and CrGPATcl can be negatively regulated by both the acyl-CoAs and lysophosphatidic acid in a dosage-dependent manner. Such a regulation pattern may represent a novel mechanism adopted by algal cells to control lipid metabolism homeostasis under various environmental conditions.
KeywordMicroalgae Lysophosphatidic acid acyltransferase Transmembrane domain Substrate selectivity Protein-protein interaction
DOI10.1016/j.algal.2019.101758
Funding OrganizationNational Key R&D Program of China ; National Key R&D Program of China ; National Key R&D Program of China ; National Key R&D Program of China ; Chinese Academy of Sciences ; Chinese Academy of Sciences ; Chinese Academy of Sciences ; Chinese Academy of Sciences ; State Development & Investment Corporation, China ; State Development & Investment Corporation, China ; State Development & Investment Corporation, China ; State Development & Investment Corporation, China ; National Key R&D Program of China ; National Key R&D Program of China ; National Key R&D Program of China ; National Key R&D Program of China ; Chinese Academy of Sciences ; Chinese Academy of Sciences ; Chinese Academy of Sciences ; Chinese Academy of Sciences ; State Development & Investment Corporation, China ; State Development & Investment Corporation, China ; State Development & Investment Corporation, China ; State Development & Investment Corporation, China ; National Key R&D Program of China ; National Key R&D Program of China ; National Key R&D Program of China ; National Key R&D Program of China ; Chinese Academy of Sciences ; Chinese Academy of Sciences ; Chinese Academy of Sciences ; Chinese Academy of Sciences ; State Development & Investment Corporation, China ; State Development & Investment Corporation, China ; State Development & Investment Corporation, China ; State Development & Investment Corporation, China ; National Key R&D Program of China ; National Key R&D Program of China ; National Key R&D Program of China ; National Key R&D Program of China ; Chinese Academy of Sciences ; Chinese Academy of Sciences ; Chinese Academy of Sciences ; Chinese Academy of Sciences ; State Development & Investment Corporation, China ; State Development & Investment Corporation, China ; State Development & Investment Corporation, China ; State Development & Investment Corporation, China
Indexed BySCI ; SCI
Language英语
Funding ProjectNational Key R&D Program of China[2018YFA0902500] ; Chinese Academy of Sciences[Y72B031Z03] ; State Development & Investment Corporation, China[Y841171Z01]
WOS Research AreaBiotechnology & Applied Microbiology
WOS SubjectBiotechnology & Applied Microbiology
WOS IDWOS:000507580300025
WOS KeywordPHOSPHATIDIC-ACID ; MICROSOMAL PREPARATIONS ; ESCHERICHIA-COLI ; SN-2 POSITION ; MEMBRANE ; TRIACYLGLYCEROL ; INSERTION ; PROTEINS ; IDENTIFICATION ; SPECIFICITIES
PublisherELSEVIER
Funding OrganizationNational Key R&D Program of China ; National Key R&D Program of China ; National Key R&D Program of China ; National Key R&D Program of China ; Chinese Academy of Sciences ; Chinese Academy of Sciences ; Chinese Academy of Sciences ; Chinese Academy of Sciences ; State Development & Investment Corporation, China ; State Development & Investment Corporation, China ; State Development & Investment Corporation, China ; State Development & Investment Corporation, China ; National Key R&D Program of China ; National Key R&D Program of China ; National Key R&D Program of China ; National Key R&D Program of China ; Chinese Academy of Sciences ; Chinese Academy of Sciences ; Chinese Academy of Sciences ; Chinese Academy of Sciences ; State Development & Investment Corporation, China ; State Development & Investment Corporation, China ; State Development & Investment Corporation, China ; State Development & Investment Corporation, China ; National Key R&D Program of China ; National Key R&D Program of China ; National Key R&D Program of China ; National Key R&D Program of China ; Chinese Academy of Sciences ; Chinese Academy of Sciences ; Chinese Academy of Sciences ; Chinese Academy of Sciences ; State Development & Investment Corporation, China ; State Development & Investment Corporation, China ; State Development & Investment Corporation, China ; State Development & Investment Corporation, China ; National Key R&D Program of China ; National Key R&D Program of China ; National Key R&D Program of China ; National Key R&D Program of China ; Chinese Academy of Sciences ; Chinese Academy of Sciences ; Chinese Academy of Sciences ; Chinese Academy of Sciences ; State Development & Investment Corporation, China ; State Development & Investment Corporation, China ; State Development & Investment Corporation, China ; State Development & Investment Corporation, China
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Document Type期刊论文
Identifierhttp://ir.ihb.ac.cn/handle/342005/35463
Collection藻类生物技术和生物能源研发中心_期刊论文
Corresponding AuthorYuan, Li; Han, Danxiang
Affiliation1.Chinese Acad Sci, Ctr Microalgal Biotechnol & Biofuels, Inst Hydrobiol, Wuhan 430072, Peoples R China
2.Qingdao Natl Lab Marine Sci & Technol, Lab Marine Biol & Biotechnol, Qingdao 266237, Peoples R China
3.Chinese Acad Sci, Inst Hydrobiol, State Key Lab Freshwater Ecol & Biotechnol, Wuhan 430072, Peoples R China
4.Chinese Acad Sci, Inst Hydrobiol, Key Lab Algal Biol, Wuhan 430072, Peoples R China
5.Chinese Acad Sci, Innovat Acad Seed Design, Beijing 100864, Peoples R China
6.Univ Chinese Acad Sci, Coll Life Sci, Beijing 100049, Peoples R China
7.State Dev & Investment Corp, SDIC Biotech Investment Co LTD, Microalgae Biotechnol Ctr, Beijing 100142, Peoples R China
8.SDIC Biotech Investment Corp, Beijing Key Lab Algae Biomass, Beijing 100142, Peoples R China
Recommended Citation
GB/T 7714
Huang, Linfei,Yu, Lihua,Li, Zhongze,et al. Microalgal plastidial lysophosphatidic acid acyltransferase interacts with upstream glycerol-3-phosphate acyltransferase and defines its substrate selectivity via the two transmembrane domains[J]. ALGAL RESEARCH-BIOMASS BIOFUELS AND BIOPRODUCTS,2020,45:11.
APA Huang, Linfei.,Yu, Lihua.,Li, Zhongze.,Li, Yanhua.,Yoon, Kang-sup.,...&Han, Danxiang.(2020).Microalgal plastidial lysophosphatidic acid acyltransferase interacts with upstream glycerol-3-phosphate acyltransferase and defines its substrate selectivity via the two transmembrane domains.ALGAL RESEARCH-BIOMASS BIOFUELS AND BIOPRODUCTS,45,11.
MLA Huang, Linfei,et al."Microalgal plastidial lysophosphatidic acid acyltransferase interacts with upstream glycerol-3-phosphate acyltransferase and defines its substrate selectivity via the two transmembrane domains".ALGAL RESEARCH-BIOMASS BIOFUELS AND BIOPRODUCTS 45(2020):11.
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