Faculty Profiles - OMOTE Hiroshi

MISC - OMOTE Hiroshi

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Functional characterization of mouse MATE2: a class 3 MATE-type polyspecific H+/organic cation exporter

Miki Hiasa, Takuya Matsumoto, Toshinori Komatsu, Kojiro Ishikawa, Hiroshi Omote, Yoshinori Moriyama

YAKUGAKU ZASSHI-JOURNAL OF THE PHARMACEUTICAL SOCIETY OF JAPAN 127 39 - 40 2007

A novel variant of mouse MATE-1 H+/organic cation exporter

Ayumi Kobara, Miki Hiasa, Takuya Matsumoto, Masato Otsuka, Hiroshi Omote, Yoshinori Moriyama

YAKUGAKU ZASSHI-JOURNAL OF THE PHARMACEUTICAL SOCIETY OF JAPAN 127 37 - 38 2007

L-glutamate signaling regulates transcytotic vesicle function in osteoclasts.

S. Uehara, R. Morimoto, S. Yatsushiro, N. Juge, M. Hayashi, S. Senoh, T. Mizoguchi, T. Ninomiya, N. Udagawa, Z. Hua, H. Omote, A. Yamamoto, R. H. Edwards, Y. Moriyama

JOURNAL OF BONE AND MINERAL RESEARCH 21 S401 - S401 2006.9

Molecular dynamics and essential dynamics studies of the interaction of transported drugs with p-glycoprotein

MK Al-Shawi, H Omote

BIOPHYSICAL JOURNAL 88 ( 1 ) 25A - 25A 2005.1

Interaction of transported drugs with the lipid bilayer and pglycoprotein: Drug transport is mediated by a hydration exchange mechanism

H Omote, MK Al-Shawi

BIOPHYSICAL JOURNAL 86 ( 1 ) 610A - 610A 2004.1

A novel EPR approach to determine the mechanism of drug transport by P-glycoprotein

MK Al-Shawi, H Omote

BIOPHYSICAL JOURNAL 82 ( 1 ) 563A - 563A 2002.1

Coupling of drug transport to ATP hydrolysis by P-glycoprotein

MK Al-Shawi, MK Polar, H Omote, RA Figler

BIOPHYSICAL JOURNAL 80 ( 1 ) 18A - 19A 2001.1

Synthase (H+ ATPase): coupling between catalysis, mechanical work, and proton translocation

M Futai, H Omote, Y Sambongi, Y Wada

BIOCHIMICA ET BIOPHYSICA ACTA-BIOENERGETICS 1458 ( 2-3 ) 276 - 288 2000.5

Language：English Publishing type：Book review, literature introduction, etc. Publisher：ELSEVIER SCIENCE BV

Coupling with electrochemical proton gradient, ATP synthase (F0F1) synthesizes ATP from ADP and phosphate. Mutational studies on high-resolution structure have been useful in understanding this complicated membrane enzyme. We discuss mainly the mechanism of catalysis in the beta subunit of F-1 sector and roles of the gamma subunit in energy coupling. The gamma-subunit rotation during catalysis is also discussed. (C) 2000 Elsevier Science B.V. All rights reserved.

DOI： 10.1016/S0005-2728(00)00080-3

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Escherichia coli ATP synthase alpha subunit Arg-376: The catalytic site arginine does not participate in the hydrolysis/synthesis reaction but is required for promotion to the steady state

NP Le, H Omote, Y Wada, MK Al-Shawi, RK Nakamoto, M Futai

BIOCHEMISTRY 39 ( 10 ) 2778 - 2783 2000.3

Language：English Publisher：AMER CHEMICAL SOC

The three catalytic sites of the FOF1 ATP synthase interact through a cooperative mechanism that is required for the promotion of catalysis. Replacement of the conserved alpha subunit Arg-376 in the Escherichia coli F-1 catalytic site with Ala or Lys resulted in turnover rates of ATP hydrolysis that were 2 x 10(3)-fold lower than that of the wild type. Mutant enzymes catalyzed hydrolysis at a single site with kinetics similar to that of the wild type; however, addition of excess ATP did not chase bound ATP, ADP, or Pi from the catalytic site, indicating that binding of ATP to the second and third sites failed to promote release of products from the first site. Direct monitoring of nucleotide binding in the alpha R376A and alpha R376K mutant F-1 by a tryptophan in place of beta Tyr-331 (Weber et al. (1993) J. Biol. Chem. 268, 20126-20133) showed that the catalytic sites of the mutant enzymes, like the wild type, have different affinities and therefore, are structurally asymmetric. These results indicate that alpha Arg-376, which is close to the beta- or gamma-phosphate group of bound ADP or ATP, respectively, does not make a significant contribution to the catalytic reaction, but coordination of the arginine to nucleotide filling the low-affinity sites is essential for promotion of rotational catalysis to steady-state turnover.

DOI： 10.1021/bi992530h

Regulation and reversibility of vacuolar H+-ATPase

T Hirata, N Nakamura, H Omote, Y Wade, M Futai

JOURNAL OF BIOLOGICAL CHEMISTRY 275 ( 1 ) 386 - 389 2000.1

Language：English Publisher：AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC

Arabidopsis thaliana vacuolar H+-translocating pyrophosphatase (V-PPase) was expressed functionally in yeast vacuoles with endogenous vacuolar H+-ATPase (V-ATPase), and the regulation and reversibility of V-ATPase were studied using these vacuoles. Analysis of electrochemical proton gradient (Delta mu H) formation with ATP and pyrophosphate indicated that the proton transport by V-ATPase or V-PPase is not regulated strictly by the proton chemical gradient (Delta pH). On the other hand, vacuolar membranes may have a regulatory mechanism for maintaining a constant membrane potential (Delta Psi). Chimeric vacuolar membranes showed ATP synthesis coupled with Delta mu H established by V-PPase. The ATP synthesis was sensitive to bafilomycin A(1) and exhibited two apparent K-m values for ADP. These results indicate that V-ATPase is a reversible enzyme. The ATP synthesis was not observed in the presence of nigericin, which dissipates Delta pH but not Delta Psi, suggesting that Delta pH is essential for ATP synthesis.

DOI： 10.1074/jbc.275.1.386

The gamma-subunit rotation and torque generation in F-1-ATPase from wild-type or uncoupled mutant Escherichia coli

H Omote, N Sambonmatsu, K Saito, Y Sambongi, A Iwamoto-Kihara, T Yanagida, Y Wada, M Futai

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA 96 ( 14 ) 7780 - 7784 1999.7

Language：English Publisher：NATL ACAD SCIENCES

The rotation of the gamma-subunit has been included in the binding-change mechanism of ATP synthesis/hydrolysis by the proton ATP synthase (FOF1), The Escherichia coli ATP synthase was engineered for rotation studies such that its ATP hydrolysis and synthesis activity is similar to that of wild type. A fluorescently labeled actin filament connected to the gamma-subunit of the F-1 sector rotated on addition of ATP, This progress enabled us to analyze the gamma M23K (the gamma-subunit Met-23 replaced by Lys) mutant, which is defective in energy coupling between catalysis and proton translocation. We found that the F-1 sector produced essentially the same frictional torque, regardless of the mutation. These results suggest that the gamma M23K mutant is defective in the transformation of the mechanical work into proton translocation or vice versa.

DOI： 10.1073/pnas.96.14.7780

Mutations in the ATP synthase gene suppress the lethal effect by human Bax against bacteria

NISHIMAKI Kiyomi, ASOH Sadamitu, OMOTE Hiroshi, HUTAI Masamitu, OHTA Shigeo

21 570 - 570 1998.12