TAILIEUCHUNG - 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

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