Functional Evidence for the Critical Amino-Terminal Conserved Domain and Key Amino Acids of Arabidopsis 4-Hydroxy-3-Methylbut-2-Enyl Diphosphate Reductase1[w][open]

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Title:	Functional Evidence for the Critical Amino-Terminal Conserved Domain and Key Amino Acids of Arabidopsis 4-Hydroxy-3-Methylbut-2-Enyl Diphosphate Reductase1[w][open]
Authors:	謝明勳;Hsieh, Wei-Yu;Sung, Tzu-Ying;Wang, Hsin-Tzu;Hsieh, Ming-Hsiun
Contributors:	生醫理工學院生命科學系
Keywords:	active sites;Albinism;Amino Acid Sequence;Amino acids;Arabidopsis;Arabidopsis - enzymology;Arabidopsis - genetics;Arabidopsis Proteins - chemistry;Arabidopsis Proteins - genetics;Arabidopsis Proteins - metabolism;Bacteria;BIOCHEMISTRY AND METABOLISM;Chloroplasts;Conserved Sequence;Cyanobacteria;Cyanobacteria - enzymology;Diphosphates - metabolism;Enzymes;Escherichia coli Proteins - chemistry;Escherichia coli Proteins - genetics;Escherichia coli Proteins - metabolism;Gene Silencing;Molecular Docking Simulation;Molecular Sequence Data;Oxidoreductases - chemistry;Oxidoreductases - genetics;Oxidoreductases - metabolism;Plants;Plants, Genetically Modified;Seedlings;Sequence Analysis, DNA;Structural Homology, Protein;Terpenoids;Transgenes;Transgenic plants
Date:	2014-09-01
Issue Date:	2026-04-23 11:12:48 (UTC+8)
Publisher:	American Society of Plant Biologists;United States: American Society of Plant Biologists
Abstract:	摘要： The plant 4-HYDROXY-3-METHYLBUT-2-ENYL DIPHOSPHATE REDUCTASE (HDR) catalyzes the last step of the methylerythritol phosphate pathway to synthesize isopentenyl diphosphate and its allyl isomer dimethylallyl diphosphate, which are common precursors for the synthesis of plastid isoprenoids. The Arabidopsis (Arabidopsis thaliana) genomic HDR transgene-induced gene-silencing lines are albino, variegated, or pale green, confirming that HDR is essential for plants. We used Escherichia coli isoprenoid synthesis H (Protein Data Bank code 3F7T) as a template for homology modeling to identify key amino acids of Arabidopsis HDR. The predicted model reveals that cysteine (Cys)-122, Cys-213, and Cys-350 are involved in iron-sulfur cluster formation and that histidine (His)-152, His-241, glutamate (Glu)-242, Glu-243, threonine (Thr)-244, Thr-312, serine-379, and asparagine-381 are related to substrate binding or catalysis. Glu-242 and Thr-244 are conserved only in cyanobacteria, green algae, and land plants, whereas the other key amino acids are absolutely conserved from bacteria to plants. We used sitedirected mutagenesis and complementation assay to confirm that these amino acids, except His-152 and His-241, were critical for Arabidopsis HDR function. Furthermore, the Arabidopsis HDR contains an extra amino-terminal domain following the transit peptide that is highly conserved from cyanobacteria, and green algae to land plants but not existing in the other bacteria. We demonstrated that the amino-terminal conserved domain was essential for Arabidopsis and cyanobacterial HDR function. Further analysis of conserved amino acids in the amino-terminal conserved domain revealed that the tyrosine-72 residue was critical for Arabidopsis HDR. These results suggest that the structure and reaction mechanism of HDR evolution have become specific for oxygen-evolving photosynthesis organisms and that HDR probably evolved independently in cyanobacteria versus other prokaryotes. 其他題名： Plant Physiol 出版者： United States: American Society of Plant Biologists 出版日期： 2014-09-01 出處： Plant physiology (Bethesda), 2014-09, Vol.166 (1), p.57-69 資源來源： JSTOR Life Sciences Collection 版權： 2014 American Society of Plant Biologists 版權： 2014 American Society of Plant Biologists. All Rights Reserved. 版權： 2014 American Society of Plant Biologists. All Rights Reserved. 2014 識別號： ISSN: 0032-0889 識別號： ISSN: 1532-2548 識別號： EISSN: 1532-2548 識別號： DOI: 10.1104/pp.114.243642 識別號： PMID: 25037211
Appears in Collections:	[Department of Life Science] journal & Dissertation

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