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Molecular Energetics of Protein Motors

Research Project

Project/Area Number 06304052
Research Category

Grant-in-Aid for Scientific Research (A)

Allocation TypeSingle-year Grants
Section総合
Research Field Biophysics
Research InstitutionKYUSHU INSTITUTE OF TECHNOLOGY

Principal Investigator

KODAMA Takao  KYUSHU INSTITUTE OF TECHNOLOGY,FACULTY OF COMPUTER SCIENCE AND ENGINEERING,PROFESSOR, 情報工学部, 教授 (30034200)

Co-Investigator(Kenkyū-buntansha) TAWADA Katsuhisa  KYUSHU UNIVERSITY,FACULTY OF SCIENCE,ASSOCIATE PROFESSOR, 理学部, 助教授 (20029507)
KATAYAMA Eisaku  UNIVERSITY OF TOKYO,BIOMEDICAL INSTITUTE,ASSOCIATE PROFESSOR, 医科学研究所, 助教授 (50111505)
WAKABAYASHI Katsuzo  OSAKA UNIVERSITY,FACULTY OF ENGINEERING SCIENCE,ASSOCIATE PROFESSOR, 基礎工学部, 助教授 (00029521)
WAKABAYASHI Takeyuki  UNIVERSITY OF TOKYO,GRADUATE SCHOOL OF SCIENCE,PROFESSOR, 大学院・理学系研究科, 教授 (90011717)
YANAGIDA Toshio  OSAKA UNIVERSITY,FACULTY OF ENGINEERING SCIENCE,PROFESSOR, 基礎工学部, 教授 (30089883)
安藤 敏夫  金沢大学, 理学部, 助教授 (50184320)
三木 正雄  福井大学, 工学部, 助教授 (30242580)
Project Period (FY) 1994 – 1996
Project Status Completed (Fiscal Year 1996)
Budget Amount *help
¥16,400,000 (Direct Cost: ¥16,400,000)
Fiscal Year 1996: ¥2,500,000 (Direct Cost: ¥2,500,000)
Fiscal Year 1995: ¥6,700,000 (Direct Cost: ¥6,700,000)
Fiscal Year 1994: ¥7,200,000 (Direct Cost: ¥7,200,000)
Keywordschemomechanical coupling / hydrophobic / hydrophilc transition / single molecule physiology / thermal fluctuation / ATP ase / vectorial motion / intramolecular hydrogen-bond / motor molecule / エナジェティックス / X線小角散乱 / 誘電分散 / 急速凍結法 / in vitro 運動系 / 張力ゆらぎ / 1分子可視化
Research Abstract

Energetic aspects of protein motors were investigated by various methods including microwave-dielectric spectroscopy and calorimetry of myosin motors hydrolyzind ATP,direct observation of simgle kinesin molecules moving along microtubules, imaging of individual ATP turnovers by single myosin molecules, small-angle X-ray diffeaction of myosin molecules with diffrrent bound nucleotides, X-ray diffraction of muscle, X-ray crystallography of myosin complexed with different nucleotides, diffusion-enhanced fluorescence resonance energy transfer of actin molecules, simulation of solvation free-energy of protein motors, fluctuation analysis of kinesin sliding along microtubule, stereo-photogramtry of quick-freeze deep-etch replica images of motor proteins, and site-directed mutagenesis of motor proteins. These studies indicate that :
1.the myosin surface hydrophobicity change plays a crucial role in the enthalpy-entropy compensation effectc observed in the steps of myosin ATP hydrolysis ;
2.protein motors can modulate the mode of coupling between chemical change (ATP hydrolysis) and mechanical output depending on load imposed on them. Thus, the energy of ATP hydrolys is somehow stored in the motor protein, which is used fractionally at each power stroke cycle. This would mean that the protein motor operate with energy conversion efficiency as high as more than 50% using the energy input comparable to or marginally above the thermal energy ;
3.Of two negative potential sites of actin molecule surface, one around the myosin binding site while the other site around the phalloidin binding site is not significantly affected ;
4.an effective diffusion coefficient from displacement fluctuations of a sliding filament obtained from its single noisy trajectory is a useful parameters for constructing the models for mechanochemical coupling.

Report

(4 results)
  • 1996 Annual Research Report   Final Research Report Summary
  • 1995 Annual Research Report
  • 1994 Annual Research Report
  • Research Products

    (47 results)

All Other

All Publications (47 results)

  • [Publications] Suzuki,M.et al.: "Coupling of protein surface hydrophobicity change to ATP hydrolysis by myosin motor domain" Biophys.J.72. 18-23 (1997)

    • Description
      「研究成果報告書概要(和文)」より
    • Related Report
      1996 Final Research Report Summary
  • [Publications] Higuchi,H.et al.: "Kinetics of force generation by single kinesin molecules activated by laser photolysis of caged ATP" Proc.Natl.Acad.Sci.USA. (印刷中).

    • Description
      「研究成果報告書概要(和文)」より
    • Related Report
      1996 Final Research Report Summary
  • [Publications] Nakajima,H.et al.: "Scanning Force Microscope of the Interaction Events between a Single Molecule of Heavy Meromyosin and Actin" Nature. (印刷中).

    • Description
      「研究成果報告書概要(和文)」より
    • Related Report
      1996 Final Research Report Summary
  • [Publications] Yamashita,T.et al.: "Micellar Catalytic Effects on the Kinetics of the Ionization of Basic Amino Acid and Acidic Amino Acid Studied by the Ultrasonic Absorption Method" Langumuir. 11. 1477-1481 (1995)

    • Description
      「研究成果報告書概要(和文)」より
    • Related Report
      1996 Final Research Report Summary
  • [Publications] Hozumi,T.et al.: "Maleimidobenzoyl Actin : Its Biochemical Properties with Heavy Meromyosin and In Vitro Motility" J.Biochem.119. 151-156 (1996)

    • Description
      「研究成果報告書概要(和文)」より
    • Related Report
      1996 Final Research Report Summary
  • [Publications] Saeki,K.et al.: "Tropomyosin-Binding Site (s) on the Dictyostelium Actin Surface As Identified by Site-Directed Mutagenesis" Biochemistry. 35. 14465-14472 (1996)

    • Description
      「研究成果報告書概要(和文)」より
    • Related Report
      1996 Final Research Report Summary
  • [Publications] Fujita,H.et al.: "Characterization of mutant myosins equivalent to human familial hypertophic cardiomyopathy mutants" J.Clinc.Invest.(印刷中).

    • Description
      「研究成果報告書概要(和文)」より
    • Related Report
      1996 Final Research Report Summary
  • [Publications] Emoto,Y.et al.: "Force production by chemically crosslinked myosin-actin cross-bridges in rabbit skinned fibers in response to MgATP depletion" Biophys.Chem.61. 85-92 (1996)

    • Description
      「研究成果報告書概要(和文)」より
    • Related Report
      1996 Final Research Report Summary
  • [Publications] Katayama,E.et al.: "Geometry of the flagellar motor in the cytoplasmic membrane of Salmonella typhimurium as determined by stereo-photogrammetry of quick-freeze deep-etch replica images" J.Mol.Biol.255. 458-475 (1996)

    • Description
      「研究成果報告書概要(和文)」より
    • Related Report
      1996 Final Research Report Summary
  • [Publications] Suzuki, M., Shigematsu, J., Harada, Y., Yanagida, T.and Kodama, T.: "Coupling of protein surface hydrophobicity change to ATP hydrolysis by myosin motor domain." Biophys.J.72. 18-23 (1997)

    • Description
      「研究成果報告書概要(欧文)」より
    • Related Report
      1996 Final Research Report Summary
  • [Publications] H.Higuchi, E.Mutoh, Y.Inoue&T.Yanagida: "Kinetics of force generation by single kinesin molecules activated by laser photolysis of caged ATP" Proc.Natl.Acad.Sci.USA. (in press).

    • Description
      「研究成果報告書概要(欧文)」より
    • Related Report
      1996 Final Research Report Summary
  • [Publications] Nakajima, H.et al: "Scanning Force Microscope of the Interaction Events between a Single Molecule of Heavy Meromyosin and Actin" Nature. (submitted).

    • Description
      「研究成果報告書概要(欧文)」より
    • Related Report
      1996 Final Research Report Summary
  • [Publications] Yamashita, T.et al: "Micellar Catalytic Effects on the Kinetics of the Ionization of Basic Amino Acid and Acidic Amino Acid Studied by the Ultrasonic Absorption Method" Langumuir. 11. 1477-1481 (1995)

    • Description
      「研究成果報告書概要(欧文)」より
    • Related Report
      1996 Final Research Report Summary
  • [Publications] Hozumi, T.et al: "Maleimidobenzoyl Actin : Its Biochemical Properties with Heavy Meromyosin and In Vitro Motility" J.Biochem. 119. 151-156 (1996)

    • Description
      「研究成果報告書概要(欧文)」より
    • Related Report
      1996 Final Research Report Summary
  • [Publications] Saeki, K.et al: "Tropomyosin-Binding Site (s) on the Dictyostelium Actin Surface As Identified by Site-Directed Mutagenesis" Biochemistry. 35. 14465-14472 (1996)

    • Description
      「研究成果報告書概要(欧文)」より
    • Related Report
      1996 Final Research Report Summary
  • [Publications] Fujita, H.et al: "Characterization of mutant myosins equivalent to human familial hypertophic cardiomyopathy mutants" J.Clinc.Invest. (in press).

    • Description
      「研究成果報告書概要(欧文)」より
    • Related Report
      1996 Final Research Report Summary
  • [Publications] Emoto, Y.et al: "Force production by chemically crosslinked myosin-actin cross-bridges in rabbit skinned fibers in response to MgATP depletion" Biophys.Chem. 61. 85-92 (1996)

    • Description
      「研究成果報告書概要(欧文)」より
    • Related Report
      1996 Final Research Report Summary
  • [Publications] Katayama, E.et al: "Geometry of the flagellar motor in the cytoplasmic membrane of Salmonella typhimurium as determined by stereo-photogramtry of quick-freeze deep-etch replica images" J.Mol.Biol. 255. 458-475 (1996)

    • Description
      「研究成果報告書概要(欧文)」より
    • Related Report
      1996 Final Research Report Summary
  • [Publications] Suzuki,M.,Shigematsu,J.and Kodama,T.: "Hydration of proteins studied by microwave dielectric analysis." J.Phys.Chem.100. 7279-7282 (1996)

    • Related Report
      1996 Annual Research Report
  • [Publications] Suzuki,M.,Shigematsu,J.,Harada,Y.,Yanagida,T.and Kodama,T.: "Coupling of protein surface hydrophobicity change to ATP hydrolysis by myosin motor domain." Biophys.J.72. 18-23 (1997)

    • Related Report
      1996 Annual Research Report
  • [Publications] Ronald D.Vale,Funatsu,T.,Daniel W.Pierce,Laura Romberg,Harada,Y.& Yanagida,T.: "Direct observation of single kinesin molecules moving along microtubules" Nature. 380. 451-453 (1996)

    • Related Report
      1996 Annual Research Report
  • [Publications] Saeki,K.,Sutoh,K.& Wakabayashi,T.: "Tropomyosin-Binding Site(s) on the Dictyostelium Actin Surface As Identified by Site-Directed Mutagenesis." Biochemistry. 35. 14465-14472 (1996)

    • Related Report
      1996 Annual Research Report
  • [Publications] Yagi,N.,Wakabayashi,K.,Iwamoto,H.,Horiuti,K.,Kojima,I.,et al.: "Small-Angle X-ray Diffraction of Muscle Using Undulator Radiation from the Tristan Main Ring at KEK" J.Synchrotron Rad.3. 305-312 (1996)

    • Related Report
      1996 Annual Research Report
  • [Publications] Katayama,E.,Funabashi,H.,Michikawa,T.,Shiraishi,T.,Ikemoto,T.,Iino,M.and Mikoshiba,K.: "Native structure and arrangement of inositol-1,4,5-trisphosphate receptor molecules in bovine cerebellar Purkinje cells as studied by quick-freeze deep-etch electron microscopy." EMBO.J. 15. 4844-4851 (1996)

    • Related Report
      1996 Annual Research Report
  • [Publications] M.Suzuki,J.Shigematsu & T.Kodama: "A hydration study of proteins in solution by Microwave dielectlic analysis" J.Phys.Chem.(in press).

    • Related Report
      1995 Annual Research Report
  • [Publications] A.Ishijima,Y.Harada,H.Kojima,T.Funatsu,H.Higuchi & T.Yanagida: "Multiple-and Single-molecule analysis of the actomyosin motor using nanometer-piconewton manipulation with a microneedle : Unitary step and force." Biophys.J.70. 383-400 (1996)

    • Related Report
      1995 Annual Research Report
  • [Publications] R.V.Vale,T.Funatsu,L.Romberg,D.W.Pierce,Y.Harada & T.Yanagida: "Direct observation of single kinesin molecules moving along microtubules." Nature. (in press). (1996)

    • Related Report
      1995 Annual Research Report
  • [Publications] Kikkawa,M.et al.: "Three-dimensional structure of the kinesin head-microtubule complex" Nature. 376. 274-277 (1995)

    • Related Report
      1995 Annual Research Report
  • [Publications] Yasunaga,T.& Wakabayashi,T.: "Extensible and Object-oriented System (Fos) Supplies a New Environment for Image Analysis of Electron Micrographs of Macromolecules" J.Struct.Biol.(in press). (1996)

    • Related Report
      1995 Annual Research Report
  • [Publications] Y.Amemiya: "Large-apeature TV detector with a beryllium-windowed image intensifier for X-ray diffraction" Rev.Sci.Instrum.68(2). 2290-2294 (1995)

    • Related Report
      1995 Annual Research Report
  • [Publications] N.Yagi: "A real-time observation of X-ray diffraction from frog skeletal muscle during and after slow length changes" Japan.J.Physiol.45. 583-606 (1995)

    • Related Report
      1995 Annual Research Report
  • [Publications] E.Katayama: "Mode of caldesmon binding to smooth muscle thin filament : Possible projection of the amino-terminal domain of caldesmon from native thin filament" Biophysical Journal. 68. 2419-2428 (1995)

    • Related Report
      1995 Annual Research Report
  • [Publications] K.Yamamoto: "Myosin from alga Chara : Unique structure revealed by electron microscopy" Journal of Molecular Biology. 254. 109-112 (1995)

    • Related Report
      1995 Annual Research Report
  • [Publications] Y.Imafuku,Y.Y.Toyoshima & K.Tawada: "Monte Carlo study for fluctuation analysis of the in vitro sliding motility driven by protein motors" Biophys.Chem.59(in press). (1996)

    • Related Report
      1995 Annual Research Report
  • [Publications] Y.Imafuku,Y.Y.Toyoshima & K.Tawada: "Fluctuation in the microtubule sliding movement driven by kinesin in vitro" Biophys.J.70. 878-886 (1996)

    • Related Report
      1995 Annual Research Report
  • [Publications] Y.Emoto & K.Tawada: "Force production by chemically crosslinked myosin-actin cross-bridges in rabbit skinned fibers in rseponse to MgATP depletion" Biophys.Chem.,. (in press). (1996)

    • Related Report
      1995 Annual Research Report
  • [Publications] A.Miyagi,H.Ohta,T.Kodama,K.Fukui,K.Kato & T.Shimono: "Metabolic and energetic aspects of the growth response of Streptococcus rattus to environmental acidification in anaerobic continuous culture" Microbiology. 140. 1945-1952 (1994)

    • Related Report
      1994 Annual Research Report
  • [Publications] K.Wakabayashi,Y.Sugimoto,H.Tanaka,Y.Ueno,Y.Takezawa & Y.Amemiya: "X-ray diffraction evidence for the extensibility of actin and myosin filaments during muscle contraction" Biophysical Journal. 67. 2422-2435 (1994)

    • Related Report
      1994 Annual Research Report
  • [Publications] K.Saito & T.Yanagida: "Movement of Single Myosin Filaments and Myosin Step Size on an Actin Filament Suspended in Solution by a Laser Trap" Biophysical Journal. 66. 769-777 (1994)

    • Related Report
      1994 Annual Research Report
  • [Publications] A.Ishijima,Y.Harada,H.Kojima,T.Funatsu,H.Higuchi & T.Yanagida: "Single-Molecule Analysis of the Actomyosin Motor Using Nano-Manipulation" Biochemical and Biophysical Reserch Communications. 199. 1057-1063 (1994)

    • Related Report
      1994 Annual Research Report
  • [Publications] H.Kojima,A.Ishijima & T.Yanagida: "Direct Measurement of Stiffness of Single Actin Filaments with and without Tropomyosin by in vitro Nanomanipulation" Proc.Natl.Acad.Sci.USA. 91. 12962-12966 (1994)

    • Related Report
      1994 Annual Research Report
  • [Publications] M.Miki & T.Kouyama: "Domain motion in Actin Observed by Fluorescence Resonance Energy Transfer." Biochemistry. 33. 10171-10177 (1994)

    • Related Report
      1994 Annual Research Report
  • [Publications] M.Miki & T.Kouyama: "Domain motion in Actin:Determination of Interdomain Distance Distributions by Time-Resolved Fluorescence Energy Transfer." Biophys.J.(印刷中).

    • Related Report
      1994 Annual Research Report
  • [Publications] E.P.Morris,E.Katayama & J.M.Squire: "Evaluation of high resolution shadowing applied to freeze-fractured,deep-etched particles:3-D helical reconstruction of shadowed actin-filaments" J.Struct.Biol.113. 47-55 (1994)

    • Related Report
      1994 Annual Research Report
  • [Publications] E.Katayama,G.Scott-Woo & M.Ikebe: "Effect of caldesmon on the assembly of smooth muscle myosin" J.Biol.Chem.270. 3319-3925 (1995)

    • Related Report
      1994 Annual Research Report
  • [Publications] E.Katayama & M.Ikebe: "Mode of caldesmon binding to smooth muscle thin filament:Possible projection of the amino-terminal domain of caldesmon from native thin filament" Biophys.J.(印刷中).

    • Related Report
      1994 Annual Research Report
  • [Publications] T.Yamamoto,S.Nakayama,N.Kobayashi & T.Ando: "Determination of Electrostatic Potential around Specific Locations on the Surface of Actin by Diffusionenhanced Fluorescence Resonance Energy Transfer." J.Mol.Biol.241. 714-731 (1994)

    • Related Report
      1994 Annual Research Report

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Published: 1994-04-01   Modified: 2016-04-21  

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