Shinsaku Maruta

Summary

Affiliation: Soka University
Country: Japan

Publications

  1. ncbi request reprint Analysis of stress in the active site of myosin accompanied by conformational changes in transient state intermediate complexes using photoaffinity labeling and 19F-NMR spectroscopy
    S Maruta
    Department of Bioengineering, Soka University, Hachioji, Tokyo, Japan
    Eur J Biochem 252:520-9. 1998
  2. ncbi request reprint Interaction of myosin.ADP.fluorometal complexes with fluorescent probes and direct observation using quick-freeze deep-etch electron microscopy
    Shinsaku Maruta
    Department of Bioengineering, Soka University, Hachioji, Tokyo 192 8577
    J Biochem 136:57-64. 2004
  3. ncbi request reprint Interaction of a new fluorescent ATP analogue with skeletal muscle myosin subfragment-1
    Shinsaku Maruta
    Department of Bioengineering, Faculty of Engineering, Soka University, Hachioji, Tokyo 192 8577, Japan
    J Biochem 131:905-11. 2002
  4. ncbi request reprint Conformational changes in the unique loops bordering the ATP binding cleft of skeletal muscle myosin mediate energy transduction
    S Maruta
    Department of Bioengineering, Faculty of Engineering, Soka University, Hachioji, Tokyo 192 8577, Japan
    J Biochem 128:695-704. 2000
  5. ncbi request reprint Solution structure of myosin-ADP-MgFn ternary complex by fluorescent probes and small-angle synchrotron X-ray scattering
    S Maruta
    Department of Bioengineering, Faculty of Engineering, Soka University, Hachioji, Tokyo 192 8577, Japan
    J Biochem 128:687-94. 2000
  6. ncbi request reprint Analysis of conformational changes at the unique loop adjacent to the ATP binding site of smooth muscle myosin using a fluorescent probe
    S Maruta
    Department of Bioengineering, Faculty of Engineering, Soka University, Hachioji, Tokyo 192 8577, Japan
    J Biochem 127:199-204. 2000
  7. ncbi request reprint Formation of the myosin.ADP.gallium fluoride complex and its solution structure by small-angle synchrotron X-ray scattering
    S Maruta
    Department of Bioengineering, Faculty of Engineering, Soka University, Hachioji, Tokyo, 192 8577, Japan
    J Biochem 125:177-85. 1999
  8. ncbi request reprint A unique loop contributing to the structure of the ATP-binding cleft of skeletal muscle myosin communicates with the actin-binding site
    S Maruta
    Department of Bioengineering, Faculty of Engineering, Soka University, Hachioji, Tokyo, 192 8577, Japan
    J Biochem 124:528-33. 1998
  9. ncbi request reprint ADP/vanadate mediated photocleavage of myosin light chain kinase at the autoinhibitory region
    S Maruta
    Department of Bioengineering, Soka University, Hachioji, Tokyo, 192 8577, Japan
    J Biochem 124:557-64. 1998
  10. ncbi request reprint Conformational changes at the highly reactive cystein and lysine regions of skeletal muscle myosin induced by formation of transition state analogues
    S Maruta
    Department of Bioengineering, Faculty of Engineering, Soka University, Hachioji, Tokyo, 192 8577, Japan
    J Biochem 124:578-84. 1998

Collaborators

Detail Information

Publications27

  1. ncbi request reprint Analysis of stress in the active site of myosin accompanied by conformational changes in transient state intermediate complexes using photoaffinity labeling and 19F-NMR spectroscopy
    S Maruta
    Department of Bioengineering, Soka University, Hachioji, Tokyo, Japan
    Eur J Biochem 252:520-9. 1998
    ....
  2. ncbi request reprint Interaction of myosin.ADP.fluorometal complexes with fluorescent probes and direct observation using quick-freeze deep-etch electron microscopy
    Shinsaku Maruta
    Department of Bioengineering, Soka University, Hachioji, Tokyo 192 8577
    J Biochem 136:57-64. 2004
    ..This is the first report of the direct observation of myosin-ADP-fluorometal ternary complexes, and the results suggest that these complexes indeed mimic the shape of the myosin head during ATP hydrolysis...
  3. ncbi request reprint Interaction of a new fluorescent ATP analogue with skeletal muscle myosin subfragment-1
    Shinsaku Maruta
    Department of Bioengineering, Faculty of Engineering, Soka University, Hachioji, Tokyo 192 8577, Japan
    J Biochem 131:905-11. 2002
    ..ADP.BeF(n) or AlF(4)(-) reported previously by our group. Our novel ATP analogue seems to be applicable to kinetic studies on myosin...
  4. ncbi request reprint Conformational changes in the unique loops bordering the ATP binding cleft of skeletal muscle myosin mediate energy transduction
    S Maruta
    Department of Bioengineering, Faculty of Engineering, Soka University, Hachioji, Tokyo 192 8577, Japan
    J Biochem 128:695-704. 2000
    ..Loop N, by contrast, is not significantly flexible...
  5. ncbi request reprint Solution structure of myosin-ADP-MgFn ternary complex by fluorescent probes and small-angle synchrotron X-ray scattering
    S Maruta
    Department of Bioengineering, Faculty of Engineering, Soka University, Hachioji, Tokyo 192 8577, Japan
    J Biochem 128:687-94. 2000
    ..The results suggest that the overall conformation and localized functional regions of the complex are quite similar to those in the presence of ATP, indicating that the complex mimics the M(**).ADP.P(i) steady state...
  6. ncbi request reprint Analysis of conformational changes at the unique loop adjacent to the ATP binding site of smooth muscle myosin using a fluorescent probe
    S Maruta
    Department of Bioengineering, Faculty of Engineering, Soka University, Hachioji, Tokyo 192 8577, Japan
    J Biochem 127:199-204. 2000
    ....
  7. ncbi request reprint Formation of the myosin.ADP.gallium fluoride complex and its solution structure by small-angle synchrotron X-ray scattering
    S Maruta
    Department of Bioengineering, Faculty of Engineering, Soka University, Hachioji, Tokyo, 192 8577, Japan
    J Biochem 125:177-85. 1999
    ..ADP.Pi state closely. The overall results may indicate that the complex mimics a somewhat different transient state from that of other complexes but has a similar global conformation along the ATPase kinetic pathway...
  8. ncbi request reprint A unique loop contributing to the structure of the ATP-binding cleft of skeletal muscle myosin communicates with the actin-binding site
    S Maruta
    Department of Bioengineering, Faculty of Engineering, Soka University, Hachioji, Tokyo, 192 8577, Japan
    J Biochem 124:528-33. 1998
    ..These results suggest that loop M acts as a signal transducer mediating communication between the ATP- and actin-binding sites...
  9. ncbi request reprint ADP/vanadate mediated photocleavage of myosin light chain kinase at the autoinhibitory region
    S Maruta
    Department of Bioengineering, Soka University, Hachioji, Tokyo, 192 8577, Japan
    J Biochem 124:557-64. 1998
    ..Moreover, the binding of Ca2+-CaM displaces the regulatory segment away from the catalytic site...
  10. ncbi request reprint Conformational changes at the highly reactive cystein and lysine regions of skeletal muscle myosin induced by formation of transition state analogues
    S Maruta
    Department of Bioengineering, Faculty of Engineering, Soka University, Hachioji, Tokyo, 192 8577, Japan
    J Biochem 124:578-84. 1998
    ..ADP.AlF4- or ScFn. These results suggest that SH1 and SH2 move distinctly during ATP hydrolysis and that the local conformations of the SH2 and RLR regions more sensitively reflect different transient states...
  11. ncbi request reprint Characterization of the interaction of myosin with ATP analogues having the syn conformation with respect to the adenine-ribose bond
    S Maruta
    Department of Bioengineering, Faculty of Engineering, Soka University, Tokyo, Japan
    Eur J Biochem 256:229-37. 1998
    ..This reflects the likely differences in the structures of their respective ATPase sites...
  12. doi request reprint Biochemical characterization of the novel rice kinesin K23 and its kinetic study using fluorescence resonance energy transfer between an intrinsic tryptophan residue and a fluorescent ATP analogue
    Nozomi Umezu
    Division of Bioengineering, Graduate School of Engineering, Soka University, Hachioji, Tokyo 192 8577, Japan
    J Biochem 149:539-50. 2011
    ..The kinetic study using FRET revealed that K23 has unique kinetic characteristics when compared with other kinesins...
  13. doi request reprint Synthesis of a novel fluorescent non-nucleotide ATP analogue and its interaction with myosin ATPase
    Keiko Tanaka
    Division of Bioinformatics, Graduate School of Engineering, Soka University, Hachioji, Tokyo 192 8577, Japan
    J Biochem 149:395-403. 2011
    ..This novel fluorescent ATP analogue was shown to be applicable for kinetic analysis of ATPases...
  14. doi request reprint Characterization of a novel rice kinesin O12 with a calponin homology domain
    Nozomi Umezu
    Division of Bioengineering, Graduate School of Engineering, Soka University, Hachioji, Tokyo 192 8577, Japan
    J Biochem 149:91-101. 2011
    ..Our findings suggest that the motor activity of the rice plant-specific kinesin O12 may be regulated by actin...
  15. ncbi request reprint Incorporation of an azobenzene derivative into the energy transducing site of skeletal muscle myosin results in photo-induced conformational changes
    Nobuhisa Umeki
    Division of Bioengineering, Graduate School of Engineering, Soka University, Hachioji, Tokyo 192 8577, Japan
    J Biochem 136:839-46. 2004
    ....
  16. ncbi request reprint Conformational dynamics of loops L11 and L12 of kinesin as revealed by spin-labeling EPR
    Masafumi D Yamada
    Division of Bioengineering, Graduate School of Engineering, Soka University, Hachioji, Tokyo 192 8577, Japan
    Biochem Biophys Res Commun 364:620-6. 2007
    ..These results suggested that the L11 residues undergo conformational transition on the binding of nucleotides and MT, while these residues remained to fluctuate over a nanometer range...
  17. doi request reprint Photocontrol of calmodulin interaction with target peptides using azobenzene derivative
    Hideki Shishido
    Division of Bioinformatics, Graduate School of Engineering, Soka University, Hachioji, Tokyo 192 8577, Japan
    J Biochem 146:581-90. 2009
    ..The binding of the PAM-CaM mutants, N60C, D64C and M124C, to M13-YFP was reversibly photocontrolled upon UV-VIS light irradiation at appropriate Ca(2+) concentrations...
  18. ncbi request reprint Analysis of the conformational change of myosin during ATP hydrolysis using fluorescence resonance energy transfer
    Yoshiaki Mizukura
    Department of Bioengineering, Faculty of Engineering, Soka University, Hachioji, Tokyo 192 8577, Japan
    J Biochem 132:471-82. 2002
    ..Assuming the efficiency at different states, myosin adopts a conformation such that the light chain moves closer to the active site by approximately 9 A during the hydrolysis of ATP...
  19. doi request reprint Kinesin-Calmodulin fusion protein as a molecular shuttle
    Hideki Shishido
    Department of Bioinformatics, Graduate School of Engineering, Soka University, Hachioji, Tokyo 192 8577, Japan
    J Biochem 147:213-23. 2010
    ..Finally, by total internal reflection fluorescence microscopy, we successfully observed that K560-CaM transported quantum dot-conjugated M13 peptide along the microtubule in the presence of Ca(2+)...
  20. ncbi request reprint Formation and characterization of kinesin.ADP.fluorometal complexes
    Hideka Shibuya
    Department of Bioengineering, Faculty of Engineering, Soka University, Hachioji, Tokyo 192 8577, Japan
    J Biochem 132:573-9. 2002
    ..Thus, the kinesin.ADP.AlF(4)(-) complex resembles the kinesin.ADP state, and the kinesin.ADP.BeF(n) complex mimics the kinesin.ADP.P(i) state...
  21. doi request reprint Crystallographic analysis reveals a unique conformation of the ADP-bound novel rice kinesin K16
    Keiko Tanaka
    Division of Bioinformatics, Graduate School of Engineering, Soka University, Hachioji, Tokyo 192 8577, Japan
    Biochem Biophys Res Commun 401:251-6. 2010
    ..These structural differences may reflect the unique enzymatic characteristics of rice kinesin K16...
  22. doi request reprint Engineering of a novel Ca²⁺-regulated kinesin molecular motor using a calmodulin dimer linker
    Hideki Shishido
    Department of Bioinformatics, Faculty of Engineering, Soka University, Hachioji, Tokyo 192 8577, Japan
    Biochem Biophys Res Commun 423:386-91. 2012
    ..These results suggest Ca(2+)-dependent dimerization of K355-M13 could be used as a novel molecular shuttle, equipped with an accelerator and brake system, for biochip applications...
  23. ncbi request reprint Photocontrol of kinesin ATPase activity using an azobenzene derivative
    Masafumi D Yamada
    Division of Bioengineering, Graduate School of Engineering, Soka University, Hachioji, Tokyo 192 8577, Japan
    J Biochem 142:691-8. 2007
    ..Using a photochromic azobenzene derivative, we have demonstrated that the ATPase activity of the motor protein kinesin is photoregulated...
  24. ncbi request reprint Conformational change of the loop L5 in rice kinesin motor domain induced by nucleotide binding
    Nobuhisa Umeki
    Laboratories of Plant and Microbial Genome Control, Graduate School of Science and Technology, Niigata University, Niigata 950 2181
    J Biochem 139:857-64. 2006
    ..These results suggest that L5 of rice kinesin significantly changes its conformation during ATP hydrolysis...
  25. ncbi request reprint Three-dimensional structural analysis of individual myosin heads under various functional states
    Eisaku Katayama
    Division of Biomolecular Imaging, Institute of Medical Science, The University of Tokyo, Minato ku, Tokyo 108 8639, Japan
    Adv Exp Med Biol 538:295-304. 2003
  26. ncbi request reprint Preparation and characterization of a novel rice plant-specific kinesin
    Nobuhisa Umeki
    Laboratories of Plant and Microbial Genome Control, Graduate School of Science and Technology, Niigata University, Niigata 950 2181
    J Biochem 139:645-54. 2006
    ..Our findings demonstrated that the rice kinesin motor domain has different enzymatic properties from those of well known kinesin 1...
  27. ncbi request reprint Intermolecular cross-linking of a novel rice Kinesin k16 motor domain with a photoreactive ATP derivative
    Nobuhisa Umeki
    Laboratories of Plant and Microbial Genome Control, Graduate School of Science and Technology, Niigata University, Niigata 950 2181
    J Biochem 139:831-6. 2006
    ..Our results indicate that Bz(2)-epsilonATP acts unusually as a photoreactive crosslinker to detect conformational changes in K16MD induced by nucleotide binding resulting in the formation of dimers...