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An Arabidopsis abc transporter Mediates Phosphate Deficiency-Induced Remodeling of Root Architecture by Modulating Iron Homeostasis in Roots

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Molecular Plant 2017年第2期10卷 244-259页

作者： Jinsong Dong Miguel A. PiSeros Xiaoxuan Li Haibing Yang Yu Liu Angus S. Murphy Leon V. Kochian Dong Liu Ministry of Education Key Laboratory of Bioinformatics Center for Plant Biology School of Life Sciences Tsinghua University Beijing 100084 China USDA-ARS Robert Holley Center for Agriculture and Health Cornell University ithaca NY 14580 USA Department of Horticulture Purdue University West Lafayette IN 47907-2010 USA State Key Laboratory of Plant Physiology and Biochemistry College of Life Science Zhejiang University Hangzhou 310058 China Department of Plant Science and Landscape Architecture University of Maryland College Park MD 20742 USA GIobal Institute for Food Security University of Saskatchewan Saskatoon S7N 4J8 Canada

The remodeling of root architecture is a major developmental response of plants to phosphate （Pi） deficiency and is thought to enhance a plant＇s ability to forage for the available Pi in topsoil. The underlying mechanism controlling this response, however, is poorly understood. In this study, we identified an Arabidopsis mutant, hps 10 （hypersensitive to Pi starvation 10）, which is morphologically normal under Pi sufficient condition but shows increased inhibition of primary root growth and enhanced production of lateral roots under Pi defi- ciency, hpslO is a previously identified allele （als3-3） of the ALUMINUM SENSITIVE3 （ALS3） gene, which is involved in plant tolerance to aluminum toxicity. Our results show that ALS3 and its interacting protein AtSTAR1 form an abc transporter complex in the tonoplast. This protein complex mediates a highly electro- genic transport in Xenopus oocytes. Under Pi deficiency, als3 accumulates higher levels of Fe3＋ in its roots than the wild type does. In Arabidopsis, LPR1 （LOW PHOSPHATE ROOT1） and LPR2 encode ferroxidases, which when mutated, reduce Fe3＋ accumulation in roots and cause root growth to be insensitive to Pi defi- ciency. Here, we provide compelling evidence showing that ALS3 cooperates with LPR1/2 to regulate Pi deficiency-induced remodeling of root architecture by modulating Fe homeostasis in roots.

关键词： phosphate deficiency root architecture iron homeostasis abc transporter ALUMINUM SENSI-TIVE3 AtS TAR1

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Single-molecule fluorescence studies on the conformational change of the abc transporter MsbA

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Biophysics Reports 2018年第3期4卷 153-165页

作者： Yanqing Liu Yue Liu Lingli He Yongfang Zhao Xuejun C.Zhang National Laboratory of Biomacromolecules National CAS Center for Excellence in Biomacromolecules Institute of Biophysics Chinese Academy of Sciences College of Life Science University of Chinese Academy of Sciences

ATP-binding cassette(abc) transporters are found in all forms of life from microbes to humans, and transport a wide variety of substrates across the cell membrane using the energy released from ATP hydrolysis and an alternating-access mechanism. Msb A is a homodimeric abc exporter from Gramnegative bacteria, and transports amphipathic substrates including precursors of lipopolysaccharides from the inner leaflet to the outer leaflet of the cytoplasmic membrane. Despite extensive structural and functional studies, controversies remain regarding the dynamic properties of the conformational changes of Msb A during its transport cycle in the lipid environment. Here, we used single-molecule fluorescence resonance energy transfer(sm FRET) to explore the dynamic behaviors of Msb A in detergent micelles, nanodiscs, and proteoliposomes. Msb A reconstituted into liposomes showed higher transition frequency between different states on the cytoplasmic side, whereas detergent-solubilized Msb A showed higher transition frequency on the periplasmic side. Three major states were identified from this sm FRET study in the functional cycle of Msb A, including an intermediate conformation between the fully opened and fully closed cytoplasmic conformations, associated with both ATP binding and hydrolysis.

关键词： abc transporter Conformational change Single-molecule fluorescence resonance energy transfer (smFRET)

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Cryo-EM structures for the Mycobacterium tuberculosis iron-loaded siderophore transporter IrtAB

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Protein & Cell 2023年第6期14卷 448-458页

作者： Shan Sun Yan Gao Xiaolin Yang Xiuna Yang Tianyu Hu Jingxi Liang Zhiqi Xiong Yuting Ran Pengxuan Ren Fang Bai Luke WGuddat Haitao Yang Zihe Rao Bing Zhang Shanghai Institute for Advanced Immunochemical Studies and School of Life Science and Technology ShanghaiTech UniversityShanghai 201210China State Key Laboratory of Medicinal Chemical Biology Nankai UniversityTianjin 300353China Laboratory of Structural Biology Tsinghua UniversityBeijing 100084China National Laboratory of Biomacromolecules CAS Center for Excellence in BiomacromoleculesInstitute of BiophysicsChinese Academy of SciencesBeijing 100101China School of Chemistry and Molecular Biosciences The University of QueenslandBrisbaneQueensland 4072Australia CAS Center for Excellence in Molecular Cell Science Shanghai Institute of Biochemistry and Cell BiologyChinese Academy of SciencesShanghai 200031China University of Chinese Academy of Sciences Beijing 100101China Shanghai Clinical Research and Trial Center Shanghai 201210China

The adenosine 5'-triphosphate(ATP)-binding cassette(abc)transporter,IrtAB,plays a vital role in the replication and viability of Mycobacterium tuberculosis(Mtb),where its function is to import iron-loaded siderophores.Unusually,it adopts the canonical type IV exporter fold.Herein,we report the structure of unliganded Mtb IrtAB and its structure in complex with ATP,ADP,or ATP analogue(AMP-PNP)at resolutions ranging from 2.8 to 3.5Å.The structure of IrtAB bound ATP-Mg2+shows a“head-to-tail”dimer of nucleotide-binding domains(NBDs),a closed amphipathic cavity within the transmembrane domains(TMDs),and a metal ion liganded to three histidine residues of IrtA in the cavity.Cryo-electron microscopy(Cryo-EM)structures and ATP hydrolysis assays show that the NBD of IrtA has a higher affinity for nucleotides and increased ATPase activity compared with IrtB.Moreover,the metal ion located in the TM region of IrtA is critical for the stabilization of the conformation of IrtAB during the transport cycle.This study provides a structural basis to explain the ATP-driven conformational changes that occur in IrtAB.

关键词： abc exporter-like importer iron-loaded siderophore IrtAB Mycobacterium tuberculosis abc transporter

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苏云金芽胞杆菌类abc transporter基因zwa-FEG能提高双效菌素的抗性

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农业生物技术学报 2008年第6期16卷 1006-1011页

作者：李卉罗毅喻子牛孙明华中农业大学生命科学技术学院农业微生物学国家重点实验室

双效菌素(zwittermicin A,ZwA)是一种氨基多元醇类新型广谱抗生素,zmaR为其抗性基因。在苏云金芽胞杆菌(Bacillus thuringiensis)YBT-1520菌株ZwA合成基因簇末端存在一个类似abc transporter的序列(命名为zwa-FEG)。将zwa-FEG基因在大肠杆菌(Escherichia coli)中表达,大肠杆菌能获得ZwA的抗性;将zwa-FEG转移到产ZwA的蜡状芽胞杆菌(Bacillus cereus)菌株UW85中,能使其ZwA产量显著提高。推测zwa-FEG是一种ZwA专一性的abc transporter,它能将ZwA分泌到胞外,从而增强ZwA的合成和ZwA的抗性。

关键词：双效菌素蜡状芽胞杆菌UW85 苏云金芽胞杆菌YBT-1520 abc transporter zwa-FEG

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嗜酸氧化亚铁硫杆菌中四个abc transporter基因的鉴定与分析

嗜酸氧化亚铁硫杆菌中四个ABC transporter基因的鉴定与分析

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作者：侯冬梅中南大学

学位级别：硕士

作为一种重要的浸矿菌种,嗜酸氧化亚铁硫杆菌对于很多重金属离子都具有较高的抗性。研究清楚这种在极端环境下生长的细菌的抗性机理,对于提高微生物的浸矿能力,改良和优化微生物冶金工艺具有重要的理论和实践意义。本文探究了嗜酸... 详细信息

作为一种重要的浸矿菌种,嗜酸氧化亚铁硫杆菌对于很多重金属离子都具有较高的抗性。研究清楚这种在极端环境下生长的细菌的抗性机理,对于提高微生物的浸矿能力,改良和优化微生物冶金工艺具有重要的理论和实践意义。本文探究了嗜酸氧化亚铁硫杆菌DC对于不同种类的重金属离子（Ni2+.Mn2+.Al3+.Zn2+.Cd2+）的耐受能力,并首次克隆鉴定了DC菌中与金属离子转运密切相关的四个相连的catiOn ATP-binding cassette（abc）transpoIrter基因。然后应用实时荧光定量PCR技术检测了不同浓度的锌离子刺激时四个基因在转录水平上的差异表达情况,并应用逆转录PCR技术鉴定了四个基因的共转录情况。最后利用生物信息学分析技术对四个基因及其编码的蛋白做了进一步的结构与功能的预测。实验结果如下： At.ferrooxidans DC对Ni2+的最大耐受能力为0.7 mol/L,对Mn2+和Al3+的最大耐受能力为0.4 mol/L,对Zn2+最大耐受能力为0.6 mol/L,Cd2+为0.75 mol/L. 经NCBI序列比对,At.ferrooxidans DC中与重金属离子转运相关的四个cation abc transporter基因（Afe2435,Aye2436,Afe2437, Afe2438）的基因序列与标准菌株ATCC23270中这四个基因的序列完全相同。基因Aye2435,Aye2436,Aye2437,Afe2438对于锌离子的胁迫非常敏感,具体表现为：在不同浓度的锌离子刺激下,四个基因在转录水平上的表达量均呈上调趋势,且随着锌离子浓度的增加,上调倍数也随之增加。共转录鉴定结果为：在At.ferrooxidans DC中,基因Afe2435, Afe2436,Afe2437,Afe2438存在共转录现象,他们很可能存在于同一个转录元件中。生物信息学分析结果表明：基因Afe2435,Afe2436编码的位于细胞质膜上的透性酶,基因Afe2437编码位于细胞质膜上的ATP结合蛋白,基因Afe2438编码周质空间上的锌离子结合蛋白。综上所述,At.ferrooxidans DC中的这四个cation ATP-binding cassette（abc）transporter基因（Afe2435,Afe2436,Afe2437,Afe2438）共同组成了一个转运锌离子的abc转运子,它们对于At. ferrooxidans DC能够耐受较高浓度的锌离子环境起到了非常重要的作用。

关键词：嗜酸氧化亚铁硫杆菌 abc transporter RT-qPCR 锌离子胁迫共转录

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Rice Stomatal Closure Requires Guard Cell Plasma Membrane ATP-Binding Cassette transporter RCN1/OsabcG5

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Molecular Plant 2016年第3期9卷 417-427页

作者： Shuichi Matsuda Sho Takano Moeko Sato Kaoru Furukawa Hidetaka Nagasawa Shoko Yoshikawa Jun Kasuga Yoshihiko Tokuji Kazufumi Yazaki Mikio Nakazono Itsuro Takamure Kiyoaki Kato Department of Agro-environmental Science Obihiro University of Agricultural and Veterinary Medicine 2-11 Nishi Inada Obihiro Hokkaido 080-0834 Japan Department of Food Science Obihiro University of Agricultural and Veterinary Medicine 2-11 Nishi Inada Obihiro Hokkaido 080-0834 Japan Research Institute for Sustainable Humanosphere Kyoto University Gokasho Uji Kyoto 611-0011 Japan Graduate School of Bioagricultural Sciences Nagoya University Furo-cho Chikusa Nagoya Aichi 464-8601 Japan Graduate School of Agriculture Hokkaido University Kita 9 Nishi 9 Kita-ku Sapporo Hokkaido 060-8589 Japan

Water stress is one of the major environmental stresses that affect agricultural production worldwide. Water loss from plants occurs primarily through stomatal pores. Here, we report that an Oryza sativa half-size ATP-binding cassette （abc） subfamily G protein, RCN 1/OsabcG5, is involved in stomatal closure mediated by phytohormone abscisic acid （ABA） accumulation in guard cells. We found that the GFP-RCN1/ OsabcG5-fusion protein was localized at the plasma membrane in guard cells. The percentage of guard cell pairs containing both ABA and GFP-RCN1/OsabcG5 increased after exogenous ABA treatment, whereas they were co-localized in guard cell pairs regardless of whether exogenous ABA was applied. ABA application resulted in a smaller increase in the percentage of guard cell pairs containing ABA in rcnl mutant （A684P） and RCN1-RNAi than in wild-type plants. Furthermore, polyethylene glycol （drought stress）-inducible ABA accumulation in guard cells did not occur in rcnl mutants. Stomata closure mediated by exogenous ABA application was strongly reduced in rcnl mutants. Finally, rcnl mutant plants had more rapid water loss from detached leaves than the wild-type plants. These results indicate that in response to drought stress, RCN1/OsabcG5 is involved in accumulation of ABA in guard cells, which is indispensable for stomatal closure.

关键词： stomatal closure abscisic acid abc transporter rice drought stress

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New xylose transporters support the simultaneous consumption of glucose and xylose in Escherichia coli

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mLife 2022年第2期1卷 156-170页

作者： Xinna Zhu Feiyu Fan Huanna Qiu Mengyao Shao Di Li Yong Yu Changhao Bi Xueli Zhang Tianjin Institute of Industrial Biotechnology Chinese Academy of SciencesTianjinChina Key Laboratory of Systems Microbial Biotechnology Chinese Academy of SciencesTianjinChina College of Biotechnology Tianjin University of Sciences and TechnologyTianjinChina University of Chinese Academy of Sciences BeijingChina

Glucose and xylose are two major components of lignocellulose.Simultaneous consumption of glucose and xylose is critical for engineered microorganisms to produce fuels and chemicals from lignocellulosic biomass.Although many production limitations have been resolved,glucose‐induced inhibition of xylose transport remains a challenge.In this study,a cell growthbased screening strategy was designed to identify xylose transporters uninhibited by glucose.The glucose pathway was genetically blocked in Escherichia coli so that glucose functions only as an inhibitor and cells need xylose as the carbon source for survival.Through adaptive evolution,omics analysis and reverse metabolic engineering,a new phosphoenolpyruvate:carbohydrate phosphotransferase system(PTS)galactitol transporter(Galabc,encoded by EcolC_1640,EcolC_1641,and EcolC_1642 genes)that is not inhibited by glucose was identified.Inactivation of adenylate cyclase led to increased expression of the EcolC_1642 gene,and a point mutation in gene EcolC_1642(N13S)further enhanced xylose transport.During the second round of gene mining,AraE and a new abc transporter(AraFGH)of xylose were identified.A point mutation in the transcription regulator araC(L156I)caused increased expression of araE and araFGH genes without arabinose induction,and a point mutation in araE(D223Y)further enhanced xylose transport.These newly identified xylose transporters can support the simultaneous consumption of glucose and xylose and have potential use in producing chemicals from lignocellulose.

关键词： abc transporter glucose PTS xylose xylose transporter

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Emerging consensus on the mechanism of polyspecific substrate recognition by the multidrug transporter P-glycoprotein

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Cancer Drug Resistance 2019年第3期2卷 471-489页

作者： Di Xia Fei Zhou Lothar Esser Laboratory of Cell Biology National Cancer InstituteCenter for Cancer ResearchNational Institutes of HealthBethesdaMD 20892USA

P-glycoprotein(P-gp or abcB1)is a member of the broad family of abc transporters.P-gp participates in the establishment of physiological barriers limiting cellular access of a large number of toxic compounds.It thus plays important roles in the pharmacokinetics of these compounds.Cancer cells and cells infected by viruses exploit the presence of P-gp to fend off drug treatment,rendering them multidrug-resistant.Overcoming multidrug resistance caused by expression of abc transporters has gained increasing attention in the field of drug development.Recently,studies of P-gp,especially from structural investigations by both cryo-electron microscopy and X-ray crystallography,have provided high-resolution mechanistic details for the function of this transporter.Structures with increasing resolution and accuracy in various substrate-and inhibitor-bound forms are available for analysis and a consensus on the mechanism of substrate polyspecificity is emerging.The use of new structural information may aid development of P-gp inhibitors as well as compounds that may bypass P-gp action.

关键词： P-glycoprotein multidrug resistance substrate polyspecificity structure abc transporter

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Ligand binding and conformational changes of SUR1 subunit in pancreatic ATP-sensitive potassium channels

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Protein & Cell 2018年第6期9卷 553-567页

作者： Jing-Xiang Wu Dian Ding Mengmeng Wang Yunlu Kang Xin Zeng Lei Chen State Key Laboratory of Membrane Biology Institute of Molecular Medicine Peking University Beijing Key Laboratory of Cardiometabolic Molecular Medicine Beijing 100871 China Peking-Tsinghua Center for Life Sciences Peking University Beijing 100871 China Academy for Advanced Interdisciplinary Studies Peking University Beijing 100871 China

ATe-sensitive potassium channels （KATP） are energy sensors on the plasma membrane. By sensing the intracellular ADP/ATP ratio of β-cells, pancreatic KATe channels control insulin release and regulate metabo- lism at the whole body level. They are implicated in many metabolic disorders and diseases and are there- fore important drug targets. Here, we present three structures of pancreatic KATe channels solved by cryo- electron microscopy （cryo-EM）, at resolutions ranging from 4.1 to 4.5 A. These structures depict the binding site of the antidiabetic drug glibenclamide, indicate how Kir6.2 （inward-rectifying potassium channel 6.2） N-ter- minus participates in the coupling between the periph- eral SUR1 （sulfonylurea receptor 1） subunit and the central Kir6.2 channel, reveal the binding mode of acti- vating nucleotides, and suggest the mechanism of how Mg-ADP binding on nucleotide binding domains （NBDs） drives a conformational change of the SUR1 subunit.

关键词： KATP SUR abc transporter glibenclamide sulfonylurea diabetes

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An Arabidopsis Lipid Flippase Is Required for Timely Recruitment of Defenses to the Host- Pathogen Interface at the Plant Cell Surface

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Molecular Plant 2017年第6期10卷 805-820页

作者： William Underwood Andrew Ryan Shauna C. Somerville Energy Biosciences Institute Department of Plant and Microbial Biology University of California Berkeley CA 94720 USA USDA-ARS Red River Valley Agricultural Research Center Sunflower and Plant Biology Research Unit Fargo ND 58102-2765 USA Division of Biological Sciences University of California San Diego CA 92161 USA

Deposition of cell wall-reinforcing papillae is an integral component of the plant immune response. TheArabidopsis PENETRATION 3 （PEN3） ATP binding cassette （abc） transporter plays a role in defense against numerous pathogens and is recruited to sites of pathogen detection where it accumulates within papillae. However, the trafficking pathways and regulatory mechanisms contributing to recruitment of PEN3 and other defenses to the host-pathogen interface are poorly understood. Here, we report a confocal microscopy-based screen to identify mutants with altered localization of PEN3-GFP after inoculation with powdery mildew fungi. We identified a mutant, aberrant localization of PEN3 3 （alp3）, displaying accumulation of the normally plasma membrane （PM）-Iocalized PEN3-GFP in endomembrane compartments. The mutant was found to be disrupted in the P4-ATPase AMINOPHOSPHOLIPID ATPASE 3 （ALA3）, a lipid flippase that plays a critical role in vesicle formation. We provide evidence that PEN3 undergoes continuous endocytic cycling from the PM to the trans-Golgi network （TGN）. In alp3, PEN3 accumulates in the TGN, causing delays in recruitment to the host-pathogen interface. Our results indicate that PEN3 and other defense proteins continuously cycle through the TGN and that timely exit of these proteins from the TGN is critical for effective pre-invasive immune responses against powdery mildews.

关键词： plant-microbe interactions defense responses protein traffic and secretion macromolecular trafficking papilla abc transporter

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