tailieunhanh - Báo cáo khoa học: The proximity between C-termini of dimeric vacuolar H+-pyrophosphatase determined using atomic force microscopy and a gold nanoparticle technique

Vacuolar H + -translocating inorganic pyrophosphatase [vacuolar H + -pyro-phosphatase (V-PPase); EC ] is a homodimeric proton translocase; it plays a pivotal role in electrogenic translocation of protons from the cyto-sol to the vacuolar lumen, at the expense of PPi hydrolysis, for the storage of ions, sugars, and other metabolites. | The proximity between C-termini of dimeric vacuolar H -pyrophosphatase determined using atomic force microscopy and a gold nanoparticle technique Tseng-Huang Liu1 Shen-Hsing Hsu1 Yun-Tzu Huang1 Shih-Ming Lin1 Tsu-Wei Huang2 Tzu-Han Chuang3 Shih-Kang Fan4 Chien-Chung Fu3 Fan-Gang Tseng and Rong-Long Pan1 1 Department of Life Sciences and Institute of Bioinformatics and StructuralBiology College of Life Sciences NationalTsing Hua University Hsin Chu Taiwan ROC 2 Department of Engineering and System Science NationalTsing Hua University Hsin Chu Taiwan ROC 3 Institute of NanoEngineering and MicroSystems NationalTsing Hua University Hsin Chu Taiwan ROC 4 Institute of Nanotechnology NationalChiao Tung University Hsin Chu Taiwan ROC Keywords atomic force microscopy proton translocation tonoplast vacuolar H -pyrophosphatase vacuole Correspondence . Pan Department of Life Sciences and Institute of Bioinformatics and Structural Biology College of Life Sciences National Tsing Hua University Hsin Chu 30013 Taiwan ROC Fax 886 3 5742688 Tel 886 3 5742685 E-mail rlpan@ These authors contributed equally to this work Received 1 March 2009 revised 17 May 2009 accepted 10 June 2009 doi Vacuolar H -translocating inorganic pyrophosphatase vacuolar H -pyrophosphatase V-PPase EC is a homodimeric proton translocase it plays a pivotal role in electrogenic translocation of protons from the cytosol to the vacuolar lumen at the expense of PPi hydrolysis for the storage of ions sugars and other metabolites. Dimerization of V-PPase is necessary for full proton translocation function although the structural details of V-PPase within the vacuolar membrane remain uncertain. The C-termi-nus presumably plays a crucial role in sustaining enzymatic and protontranslocating reactions. We used atomic force microscopy to visualize V-PPases embedded in an artificial lipid bilayer under physiological conditions. V-PPases were randomly distributed

• Báo cáo khoa học
• medical report
• Scientific reports
• scientific research
• medical knowledge
• cytoplasm
• analysis of cytoplasmic
• BMC Plant Biology
• Upland cotton
• Restorer gene
• High throughput sequencing
• Cytoplasmic male sterility
• Plant Biology
• Multi omics analysis
• Brassica napus
• Naturally exists
• Mitochondrial genome functions
• BMC Genomics
• RNA sequencing
• Restorer of fertility
• Sterile phenotype
• Parental genes
• Binding miRNAs
• Triple hybrids
• Gossypium bickii
• Proteomic analysis
• Report medicine
• traditional medicine
• medical research
• biochemistry
• molecular Biology
• microRNA genes
• hemoglobin
• medical analysis
• environmental medicine
• human disease
• Crystal structure
• biochemical studies
• Gossypium hirsutum L
• Photosensitive genetic male sterile
• Differentially expressed genes
• Transcriptome analysis
• RNA Seq
• mammals
• tài liệu báo cáo nghiên cứu khoa học
• cách trình bày báo cáo
• kiến thức bệnh thú y
• báo cáo bệnh thú y
• các nghiên về bệnh thú ý
• Human telomeric
• Structural features
• hormone medicine
• under construction
• molecular
• biosynthesis
• genetics
• PPR protein
• Targeted mutagenesis
• Nuclear restorer gene
• Structure function relationship
• Rubber tree
• Hevea brasiliensis
• Genome sequencing
• Anther transcriptome
• Hybrid wheat
• Pistil like
• Skeletal muscle
• Wnt signaling pathway
• Enzyme activity
• Cytoplasmic surface
• Fertility restorer
• Plant breeders
• Nuclear genes