title: Reversible control of F(1)-ATPase rotational motion using a photochromic ATP analog at the single molecule level.
abstract: Motor enzymes such as F1-ATPase and kinesin utilize energy from ATP for their motion. Molecular motions of these enzymes are critical to their catalytic mechanisms and were analyzed thoroughly using a single molecule observation technique. As a tool to analyze and control the ATP-driven motor enzyme motion, we recently synthesized a photoresponsive ATP analog with a p-tert-butylazobenzene tethered to the 2' position of the ribose ring. Using cis/trans isomerization of the azobenzene moiety, we achieved a successful reversible photochromic control over a kinesin-microtubule system in an in vitro motility assay. Here we succeeded to control the hydrolytic activity and rotation of the rotary motor enzyme, F1-ATPase, using this photosensitive ATP analog. Subsequent single molecule observations indicated a unique pause occurring at the ATP binding angle position in the presence of cis form of the analog.
authors.affiliation: Core Research for Evolutional Science and Technology (CREST), Japan Science and Technology Agency (JST), Chiyoda-Ku Tokyo 102-0076, Japan; Chemical Resources Laboratory, Tokyo Institute of Technology, Nagatsuta 4259-R1-8, Midori-Ku, Yokohama 226-8503, Japan.
authors.forename: Ei-Ichiro
authors.initials: E
authors.lastname: Sunamura
authors.affiliation: Research Institute for Electronic Science, Hokkaido University, N20, W10, Kita-Ku, Sapporo 001-0020, Japan.
authors.forename: Takashi
authors.initials: T
authors.lastname: Kamei
authors.affiliation: Imaging Research Division, Bio-AFM Frontier Research Center, Kanazawa University, Kakuma, Kanazawa 920-1192, Japan.
authors.forename: Hiroki
authors.initials: H
authors.lastname: Konno
authors.affiliation: Research Institute for Electronic Science, Hokkaido University, N20, W10, Kita-Ku, Sapporo 001-0020, Japan. Electronic address: tamaoki@es.hokudai.ac.jp.
authors.forename: Nobuyuki
authors.initials: N
authors.lastname: Tamaoki
authors.affiliation: Core Research for Evolutional Science and Technology (CREST), Japan Science and Technology Agency (JST), Chiyoda-Ku Tokyo 102-0076, Japan; Chemical Resources Laboratory, Tokyo Institute of Technology, Nagatsuta 4259-R1-8, Midori-Ku, Yokohama 226-8503, Japan. Electronic address: thisabor@res.titech.ac.jp.
authors.forename: Toru
authors.initials: T
authors.lastname: Hisabori
mesh_terms: D000255:Adenosine Triphosphate / Q000031:analogs & derivatives* / Q000378:metabolism; D001391:Azo Compounds / Q000378:metabolism*; D025243:Bacterial Proton-Translocating ATPases / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D000458:Cyanobacteria / Q000201:enzymology / Q000235:genetics; D016547:Kinesins / Q000378:metabolism; D007700:Kinetics; D008027:Light; D008870:Microtubules / Q000378:metabolism; D020409:Molecular Motor Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D009038:Motion; D055668:Photochemical Processes; D012399:Rotation; D013379:Substrate Specificity
chemical_list: D001391:Azo Compounds; D020409:Molecular Motor Proteins; D000255:Adenosine Triphosphate; D025243:Bacterial Proton-Translocating ATPases; D016547:Kinesins
keywords: ATP synthase; Molecular motors; Nucleotide analogs; Photo-regulation; Single molecule analysis