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Redox regulation of the rotation of F₁-ATP synthase

JOURNAL OF BIOLOGICAL CHEMISTRY 2001年第43期276卷 39505-39507页

作者： Bald, D Noji, H Yoshida, M Hirono-Hara, Y Hisabori, T Tokyo Inst Technol Chem Resources Lab Midori Ku Yokohama Kanagawa 2268503 Japan Tokyo Inst Technol PRESTO Midori Ku Yokohama Kanagawa 2268503 Japan Teikyo Univ Biotechnol Res Ctr 3F CREST Genet Programming Team 13 Miyamae Ku Kawasaki Kanagawa 2160001 Japan

In F-1-ATPase, the smallest known motor enzyme, unidirectional rotation of the central axis subunit gamma is coupled to ATP hydrolysis. In the present study, we report the redox switching of the rotation of this enzyme. For this purpose, the switch region from the gamma subunit of the redox-sensitive chloroplast F-1-ATPase was introduced into the bacterial F-1-ATPase. The ATPase activity of the obtained complex was increased up to 3-fold upon reduction (Bald, D., Noji, H., Stumpp, M. T., Yoshida, M. & Hisabori, T. (2000) J. Biol. Chem. 275,12757-12762). Here, we successfully observed the modulation of rotation of gamma in this chimeric complex by changes in the redox conditions. In addition we revealed that the suppressed enzymatic activity of the oxidized F-1-ATPase complex was characterized by more frequent long pauses in the rotation of the gamma subunit. These findings obtained by the single molecule analysis therefore provide new insights into the mechanisms of enzyme regulation.

关键词： Biochemistry

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Rotation of the c subunit oligomer in fully functional F₁F_o ATP synthase

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PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA 2001年第3期98卷 898-902页

作者： Tsunoda, SP Aggeler, R Yoshida, M Capaldi, RA Univ Oregon Inst Mol Biol Eugene OR 97403 USA Tokyo Inst Technol Res Lab Resources Utilizat Yokohama Kanagawa 2268503 Japan Teikyo Univ Biotechnol Res Ctr 3F Core Res Evolut Sci & Technol Genet Programming Kawasaki Kanagawa 2160001 Japan

The F1F0-type ATP synthase is the smallest motor enzyme known. Previous studies had established that the central gamma and epsilon subunits of the F-1 part rotate relative to a stator of alpha (3)beta (3) and delta subunits during catalysis. We now show that the ring of c subunits in the F-0 part moves along with the gamma and epsilon subunits. This was demonstrated by linking the three rotor subunits with disulfide bridges between cysteine residues introduced genetically at the interfaces between the gamma, epsilon, and c subunits. Essentially complete cross-linking of the gamma, epsilon, and c subunits was achieved by using CuCl2 to induce oxidation. This fixing of the three subunits together had no significant effect on ATP hydrolysis, proton translocation, or ATP synthesis, and each of these functions retained inhibitor sensitivity. These results unequivocally place the c subunit oligomer in the rotor part of this molecular machine.

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The rotary machine in the cell, ATP synthase

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JOURNAL OF BIOLOGICAL CHEMISTRY 2001年第3期276卷 1665-1668页

作者： Noji, H Yoshida, M Tokyo Inst Technol Chem Resource Lab Yokohama Kanagawa 2268503 Japan Teikyo Univ Biotechnol Res Ctr 3F Genet Programming Team 13 CRESTMiyamae Ku Kawasaki Kanagawa 2160001 Japan

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On objects and events

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ACM SIGPLAN NOTICES 2001年第11期36卷 254-269页

作者： Eugster, PT Guerraoui, R Damm, CH Swiss Fed Inst Technol Distributed Programming Lab CH-1015 Lausanne Switzerland Univ Aarhus Dept Comp Sci DK-8200 Aarhus N Denmark

This paper presents linguistic primitives for publish/subscribe programming using events and objects. We integrate our primitives into a strongly typed object-oriented language through four mechanisms: (1) serialization, (2) multiple subtyping, (3) closures, and (4) deferred code evaluation. We illustrate our primitives through Java, showing how we have overcome its respective lacks. A precompiler transforms statements based on our publish/subscribe primitives into calls to specifically generated typed adapters, which resemble the typed stubs and skeletons generated by the rmic precompiler for remote method invocations in Java.

关键词： Java type publish/subscribe event linguistic support

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Direct observation of DNA rotation during transcription by Escherichia coli RNA polymerase

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NATURE 2001年第6816期409卷 113-115页

作者： Harada, Y Ohara, O Takatsuki, A Itoh, H Shimamoto, N Kinosita, K Keio Univ Fac Sci & Technol Dept Phys Kohoku Ku Yokohama Kanagawa 2238522 Japan CREST Genet Programming Miyamae Ku Kawasaki Kanagawa 2160001 Japan Kazusa DNA Res Inst Kisarazu 2920812 Japan Hamamatsu Photon KK Tsukuba Res Lab Tsukuba Ibaraki 3002635 Japan Natl Inst Genet Struct Biol Ctr Mishima Shizuoka 4118540 Japan

Helical filaments driven by linear molecular motors are anticipated to rotate around their axis, but rotation consistent with the helical pitch has not been observed. 14S dynein(1) and non-claret disjunctional protein (ncd)(2) rotated a microtubule more efficiently than expected for its helical pitch, and myosin rotated an actin filament only poorly(3). For DNA-based motors such as RNA polymerase, transcription-induced supercoiling of DNA(4) supports the general picture of tracking along the DNA helix(5). Here we report direct and real-time optical microscopy measurements of rotation rate that are consistent with high-fidelity tracking. Single RNA polymerase molecules attached to a glass surface rotated DNA for >100 revolutions around the right-handed screw axis of the double helix with a rotary torque of >5 pN nm. This real-time observation of rotation opens the possibility of resolving individual transcription steps.

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Comprehensive survey of proteins targeted by chloroplast thioredoxin

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PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA 2001年第20期98卷 11224-11229页

作者： Motohashi, K Kondoh, A Stumpp, MT Hisabori, T Tokyo Inst Technol Chem Resources Lab Midori Ku Yokohama Kanagawa 2268503 Japan Core Res Evolut Sci & Technol Genet Programming Team 13 Miyamae Ku Kawasaki Kanagawa 2160001 Japan

Possible target proteins of chloroplast thioredoxin (Trx) have been investigated in the stroma lysate of spinach chloroplasts. For that purpose, we immobilized a mutant of m-type Trx in which an internal cysteine at the active site was substituted with serine, on cyanogen bromide-activated resin. By using this resin, the target proteins in chloroplast were efficiently acquired when they formed the mixed-disulfide intermediates with the immobilized Trxs. We could acquire Rubisco activase (45 kDa) and 2-Cys-type peroxiredoxin (Prx), which were recently identified as targets of chloroplast Trxs. Glyceraldehyde-3-phosphate dehydrogenase and sedoheputulose 1,7-bisphosphatase, well-known thiol enzymes in the Calvin cycle, also were recognized among the collected proteins, suggesting the method is applicable for our purpose. Furthermore, four proteins were identified from a homology search of the NH2-terminal sequence of the acquired proteins: glutamine synthetase, a protein homologous to chloroplast cyclophilin, a homolog of Prx-Q, and the Rubisco small subunit. The Trx susceptibilities of the recombinant cyclophilin and Prx-Q of Arabidopsis thaliana were then examined. The method developed in the present study is thus applicable to investigate the various redox networks via Trxs and the related enzymes in the cell.

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Thermal activation of single kinesin molecules with temperature pulse microscopy

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CELL MOTILITY AND THE CYTOSKELETON 2001年第1期49卷 41-47页

作者： Kawaguchi, K Ishiwata, S Waseda Univ Sch Sci & Engn Dept Phys Shinjuku Ku Tokyo 1698555 Japan Waseda Univ Adv Res Inst Sci & Engn Tokyo 1698555 Japan Waseda Univ Mat Res Lab Biosci & Photon Tokyo 1698555 Japan Core Res Evolut Sci & Technol Genet Programming Team 13 Kawasaki Kanagawa Japan

Conventional kinesin is a processive motor protein that keeps "walking" along a microtubule using chemical energy released by ATP hydrolysis. We previously studied the effects of temperature between 15 degrees and 35 degreesC on the moving velocity, force, and processivity of single kinesin molecules using a bead assay [Kawaguchi and Ishiwata, 2000b: Biochem Biophys Res Commun 272:895-899]. However, we could not examine the effects of temperature higher than 35 degreesC because of the thermal damage to proteins. Here, using temperature pulse microscopy (TPM) [Kato et al., 1999: Proc Natl Acad Sci USA 96:9602-9606], we could examine the temperature dependence of the gliding velocity of single kinesin molecules interacting with a microtubule above 35 degreesC up to 50 degreesC (instantaneously, similar to 60 degreesC), where the velocity reached 3.68 mum/s, the highest ever reported. The Arrhenius plot showed no breaks between 15 degrees and 50 degreesC with a unique activation energy of about 50 kJ/mol, suggesting that the molecular mechanism of kinesin motility is common over a broad temperature range including physiological temperature. Cell Motil. Cytoskeleton 49:41-47, 2001. (C) 2001 Wiley-Liss, Inc.

关键词： Arrhenius plot motor protein microtubule temperature effect on kinesin single molecule assay

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Pause and rotation of F₁-ATPase during catalysis

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PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA 2001年第24期98卷 13649-13654页

作者： Hirono-Hara, Y Noji, H Nishiura, M Muneyuki, E Hara, KY Yasuda, R Kinosita, K Yoshida, M Tokyo Inst Technol Chem Resources Lab Yokohama Kanagawa 2268503 Japan Tokyo Inst Technol PRESTO Yokohama Kanagawa 2268503 Japan Tokyo Inst Technol ERATO Yokohama Kanagawa 2268503 Japan Univ Tokyo Grad Sch Arts & Sci Dept Life Sci Meguro Ku Tokyo 1538902 Japan Teikyo Univ Biotechnol Res Ctr 3F CREST Genet Programming Team 13 Kawasaki Kanagawa 2160001 Japan Keio Univ Fac Sci & Technol Dept Phys Kohoku Ku Yokohama Kanagawa 223 Japan

FI-ATPase is a rotary motor enzyme in which a single ATP molecule drives a 120 degrees rotation of the central gamma subunit relative to the surrounding alpha (3)beta (3) ring. Here, we show that the rotation of F-1-ATPase spontaneously lapses into long (approximate to 30 s) pauses during steady-state catalysis. The effects of ADP-Mg and mutation on the pauses, as well as kinetic comparison with bulk-phase catalysis, strongly indicate that the paused enzyme corresponds to the inactive state of F-1-ATPase previously known as the ADP-Mg inhibited form in which F-1-ATPase fails to release ADP-Mg from catalytic sites. The pausing position of the gamma subunit deviates from the ATP-waiting position and is most likely the recently found intermediate 90 degrees position.

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Conditional graph rewriting as a domain-independent formalism for software evolution

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International Workshop on Applications of Graph Transformations with Industrial Relevance (ACTIVE 99)

作者： Mens, T Free Univ Brussels Dept Comp Sci Programming Technol Lab B-1050 Brussels Belgium

ISBN: (纸本)3540676589

This paper presents a formal approach for managing unanticipated software evolution. labelled typed nested graphs are used to represent arbitrarily complex software artifacts, and conditional graph rewriting is used for managing evolution of these artifacts. More specifically, we detect structural and behavioural inconsistencies when merging parallel evolutions of the same software artifact. The approach is domain-independent, in the sense that it can be customised to many different domains, such as software architectures, UML analysis and design models, and software code.

关键词： Graph theory

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ATPase activity of a highly stable α₃β₃γ subcomplex of thermophilic F₁ can be regulated by the introduced regulatory region of γ subunit of chloroplast F₁

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JOURNAL OF BIOLOGICAL CHEMISTRY 2000年第17期275卷 12757-12762页

作者： Bald, D Noji, H Stumpp, MT Yoshida, M Hisabori, T Tokyo Inst Technol Chem Resources Lab Midori Ku Yokohama Kanagawa 2268503 Japan Teikyo Biotechnol Ctr CREST Genet Programming Team 13 Miyamae Ku Kawasaki Kanagawa 2160001 Japan

A mutant F-1-ATPase alpha(3)beta(3)gamma subcomplex from the thermophilic Bacillus PS3 was constructed, in which 111 amino acid residues (Val(92) to Phe(202)) from the central region of the gamma subunit were replaced by the 148 amino acid residues of the homologous region from spinach chloroplast F-1-ATPase gamma subunit, including the regulatory stretch, and were designated as alpha(3)beta(3)gamma((TCT)) (Thermophilic-Chloroplast-Thermophilic). By the insertion of this regulatory region into the gamma subunit of thermophilic F-1, we could confer the thiol modulation property to the thermophilic alpha(3)beta(3)gamma subcomplex. The overexpressed alpha(3)beta(3)gamma((TCT)) was easily purified in large scale, and the ATP hydrolyzing activity of the obtained complex was shown to increase up to 3-fold upon treatment with chloroplast thioredoxin-f and dithiothreitol. No loss of thermostability compared with the wild type subcomplex was found, and activation by dithiothreitol was functional at temperatures up to 80 degrees C. alpha(3)beta(3)gamma((TCT)) was inhibited by the epsilon subunit from chloroplast F-1-ATPase but not by the one from the thermophilic F-1-ATPase, indicating that the introduced amino acid residues from chloroplast F-1-gamma subunit are important for functional interaction with the epsilon subunit.

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