Research Topics
| Shinsaku MarutaSummaryAffiliation: Soka University Country: Japan Publications
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Detail Information
Publications
Analysis of stress in the active site of myosin accompanied by conformational changes in transient state intermediate complexes using photoaffinity labeling and 19F-NMR spectroscopyS Maruta
Department of Bioengineering, Soka University, Hachioji, Tokyo, Japan
Eur J Biochem 252:520-9. 1998....- Interaction of myosin.ADP.fluorometal complexes with fluorescent probes and direct observation using quick-freeze deep-etch electron microscopyShinsaku 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... - Interaction of a new fluorescent ATP analogue with skeletal muscle myosin subfragment-1Shinsaku 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... - Conformational changes in the unique loops bordering the ATP binding cleft of skeletal muscle myosin mediate energy transductionS 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... - Solution structure of myosin-ADP-MgFn ternary complex by fluorescent probes and small-angle synchrotron X-ray scatteringS 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... - Analysis of conformational changes at the unique loop adjacent to the ATP binding site of smooth muscle myosin using a fluorescent probeS Maruta
Department of Bioengineering, Faculty of Engineering, Soka University, Hachioji, Tokyo 192 8577, Japan
J Biochem 127:199-204. 2000.... - Formation of the myosin.ADP.gallium fluoride complex and its solution structure by small-angle synchrotron X-ray scatteringS 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... - A unique loop contributing to the structure of the ATP-binding cleft of skeletal muscle myosin communicates with the actin-binding siteS 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... - ADP/vanadate mediated photocleavage of myosin light chain kinase at the autoinhibitory regionS 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... - Conformational changes at the highly reactive cystein and lysine regions of skeletal muscle myosin induced by formation of transition state analoguesS 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... - Characterization of the interaction of myosin with ATP analogues having the syn conformation with respect to the adenine-ribose bondS 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... 
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 analogueNozomi 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...- Synthesis of a novel fluorescent non-nucleotide ATP analogue and its interaction with myosin ATPaseKeiko 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... - Characterization of a novel rice kinesin O12 with a calponin homology domainNozomi 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... - Incorporation of an azobenzene derivative into the energy transducing site of skeletal muscle myosin results in photo-induced conformational changesNobuhisa Umeki
Division of Bioengineering, Graduate School of Engineering, Soka University, Hachioji, Tokyo 192-8577, Japan
J Biochem (Tokyo) 136:839-46. 2004.... - Conformational dynamics of loops L11 and L12 of kinesin as revealed by spin-labeling EPRMasafumi 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... - Photocontrol of calmodulin interaction with target peptides using azobenzene derivativeHideki 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... - Analysis of the conformational change of myosin during ATP hydrolysis using fluorescence resonance energy transferYoshiaki Mizukura
Department of Bioengineering, Faculty of Engineering, Soka University, Hachioji, Tokyo 192-8577, Japan
J Biochem (Tokyo) 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... - Kinesin-Calmodulin fusion protein as a molecular shuttleHideki 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+)... - Formation and characterization of kinesin.ADP.fluorometal complexesHideka Shibuya
Department of Bioengineering, Faculty of Engineering, Soka University, Hachioji, Tokyo 192-8577, Japan
J Biochem (Tokyo) 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... - Crystallographic analysis reveals a unique conformation of the ADP-bound novel rice kinesin K16Keiko 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... - Engineering of a novel Ca²⁺-regulated kinesin molecular motor using a calmodulin dimer linkerHideki 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... - Photocontrol of kinesin ATPase activity using an azobenzene derivativeMasafumi 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... - Conformational change of the loop L5 in rice kinesin motor domain induced by nucleotide bindingNobuhisa Umeki
Laboratories of Plant and Microbial Genome Control, Graduate School of Science and Technology, Niigata University, Niigata 950-2181
J Biochem (Tokyo) 139:857-64. 2006..These results suggest that L5 of rice kinesin significantly changes its conformation during ATP hydrolysis... - Three-dimensional structural analysis of individual myosin heads under various functional statesEisaku 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 - Preparation and characterization of a novel rice plant-specific kinesinNobuhisa Umeki
Laboratories of Plant and Microbial Genome Control, Graduate School of Science and Technology, Niigata University, Niigata 950-2181
J Biochem (Tokyo) 139:645-54. 2006..Our findings demonstrated that the rice kinesin motor domain has different enzymatic properties from those of well known kinesin 1... - Intermolecular cross-linking of a novel rice Kinesin k16 motor domain with a photoreactive ATP derivativeNobuhisa Umeki
Laboratories of Plant and Microbial Genome Control, Graduate School of Science and Technology, Niigata University, Niigata 950-2181
J Biochem (Tokyo) 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...