Protein complex formation in methionine chain-elongation and leucine biosynthesis

Abstract During the past two decades, glucosinolate (GLS) metabolic pathways have been under extensive studies because of the importance of the specialized metabolites in plant defense against herbivores and pathogens. The studies have led to a nearly complete characterization of biosynthetic genes...

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Autores principales:	Li-Qun Chen, Shweta Chhajed, Tong Zhang, Joseph M. Collins, Qiuying Pang, Wenyuan Song, Yan He, Sixue Chen
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2021
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/58ab62216ba94c8e9ead76082433e2ef
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spelling	oai:doaj.org-article:58ab62216ba94c8e9ead76082433e2ef2021-12-02T14:26:54ZProtein complex formation in methionine chain-elongation and leucine biosynthesis10.1038/s41598-021-82790-42045-2322https://doaj.org/article/58ab62216ba94c8e9ead76082433e2ef2021-02-01T00:00:00Zhttps://doi.org/10.1038/s41598-021-82790-4https://doaj.org/toc/2045-2322Abstract During the past two decades, glucosinolate (GLS) metabolic pathways have been under extensive studies because of the importance of the specialized metabolites in plant defense against herbivores and pathogens. The studies have led to a nearly complete characterization of biosynthetic genes in the reference plant Arabidopsis thaliana. Before methionine incorporation into the core structure of aliphatic GLS, it undergoes chain-elongation through an iterative three-step process recruited from leucine biosynthesis. Although enzymes catalyzing each step of the reaction have been characterized, the regulatory mode is largely unknown. In this study, using three independent approaches, yeast two-hybrid (Y2H), coimmunoprecipitation (Co-IP) and bimolecular fluorescence complementation (BiFC), we uncovered the presence of protein complexes consisting of isopropylmalate isomerase (IPMI) and isopropylmalate dehydrogenase (IPMDH). In addition, simultaneous decreases in both IPMI and IPMDH activities in a leuc:ipmdh1 double mutants resulted in aggregated changes of GLS profiles compared to either leuc or ipmdh1 single mutants. Although the biological importance of the formation of IPMI and IPMDH protein complexes has not been documented in any organisms, these complexes may represent a new regulatory mechanism of substrate channeling in GLS and/or leucine biosynthesis. Since genes encoding the two enzymes are widely distributed in eukaryotic and prokaryotic genomes, such complexes may have universal significance in the regulation of leucine biosynthesis.Li-Qun ChenShweta ChhajedTong ZhangJoseph M. CollinsQiuying PangWenyuan SongYan HeSixue ChenNature PortfolioarticleMedicineRScienceQENScientific Reports, Vol 11, Iss 1, Pp 1-8 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Li-Qun Chen Shweta Chhajed Tong Zhang Joseph M. Collins Qiuying Pang Wenyuan Song Yan He Sixue Chen Protein complex formation in methionine chain-elongation and leucine biosynthesis
description	Abstract During the past two decades, glucosinolate (GLS) metabolic pathways have been under extensive studies because of the importance of the specialized metabolites in plant defense against herbivores and pathogens. The studies have led to a nearly complete characterization of biosynthetic genes in the reference plant Arabidopsis thaliana. Before methionine incorporation into the core structure of aliphatic GLS, it undergoes chain-elongation through an iterative three-step process recruited from leucine biosynthesis. Although enzymes catalyzing each step of the reaction have been characterized, the regulatory mode is largely unknown. In this study, using three independent approaches, yeast two-hybrid (Y2H), coimmunoprecipitation (Co-IP) and bimolecular fluorescence complementation (BiFC), we uncovered the presence of protein complexes consisting of isopropylmalate isomerase (IPMI) and isopropylmalate dehydrogenase (IPMDH). In addition, simultaneous decreases in both IPMI and IPMDH activities in a leuc:ipmdh1 double mutants resulted in aggregated changes of GLS profiles compared to either leuc or ipmdh1 single mutants. Although the biological importance of the formation of IPMI and IPMDH protein complexes has not been documented in any organisms, these complexes may represent a new regulatory mechanism of substrate channeling in GLS and/or leucine biosynthesis. Since genes encoding the two enzymes are widely distributed in eukaryotic and prokaryotic genomes, such complexes may have universal significance in the regulation of leucine biosynthesis.
format	article
author	Li-Qun Chen Shweta Chhajed Tong Zhang Joseph M. Collins Qiuying Pang Wenyuan Song Yan He Sixue Chen
author_facet	Li-Qun Chen Shweta Chhajed Tong Zhang Joseph M. Collins Qiuying Pang Wenyuan Song Yan He Sixue Chen
author_sort	Li-Qun Chen
title	Protein complex formation in methionine chain-elongation and leucine biosynthesis
title_short	Protein complex formation in methionine chain-elongation and leucine biosynthesis
title_full	Protein complex formation in methionine chain-elongation and leucine biosynthesis
title_fullStr	Protein complex formation in methionine chain-elongation and leucine biosynthesis
title_full_unstemmed	Protein complex formation in methionine chain-elongation and leucine biosynthesis
title_sort	protein complex formation in methionine chain-elongation and leucine biosynthesis
publisher	Nature Portfolio
publishDate	2021
url	https://doaj.org/article/58ab62216ba94c8e9ead76082433e2ef
work_keys_str_mv	AT liqunchen proteincomplexformationinmethioninechainelongationandleucinebiosynthesis AT shwetachhajed proteincomplexformationinmethioninechainelongationandleucinebiosynthesis AT tongzhang proteincomplexformationinmethioninechainelongationandleucinebiosynthesis AT josephmcollins proteincomplexformationinmethioninechainelongationandleucinebiosynthesis AT qiuyingpang proteincomplexformationinmethioninechainelongationandleucinebiosynthesis AT wenyuansong proteincomplexformationinmethioninechainelongationandleucinebiosynthesis AT yanhe proteincomplexformationinmethioninechainelongationandleucinebiosynthesis AT sixuechen proteincomplexformationinmethioninechainelongationandleucinebiosynthesis
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Protein complex formation in methionine chain-elongation and leucine biosynthesis

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