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Volumn 29, Issue 1, 2015, Pages 81-94

Kinetic mechanism of Nicotiana tabacum myosin-11 defines a new type of a processive motor

Author keywords

Homology modeling; Molecular mechanics; Plant; Processivity

Indexed keywords

ACTIN; ACTIN BINDING PROTEIN; ADENOSINE DIPHOSPHATE; ADENOSINE TRIPHOSPHATASE; ADENOSINE TRIPHOSPHATE; F ACTIN; MYOSIN; MYOSIN 11; MYOSIN VA; UNCLASSIFIED DRUG; VEGETABLE PROTEIN; MOLECULAR MOTOR; RECOMBINANT PROTEIN;

EID: 84928702978     PISSN: 08926638     EISSN: 15306860     Source Type: Journal    
DOI: 10.1096/fj.14-254763     Document Type: Article
Times cited : (9)

References (89)
  • 2
    • 84879907737 scopus 로고    scopus 로고
    • Plant-specific myosin XI, a molecular perspective
    • Tominaga, M., and Nakano, A. (2012) Plant-specific myosin XI, a molecular perspective. Front. Plant Sci. 3, 211
    • (2012) Front. Plant Sci. , vol.3 , pp. 211
    • Tominaga, M.1    Nakano, A.2
  • 3
    • 84869235755 scopus 로고    scopus 로고
    • Putting on the breaks: Regulating organelle movements in plant cells(f)
    • Vick, J. K., and Nebenführ, A. (2012) Putting on the breaks: regulating organelle movements in plant cells(f). J. Integr. Plant Biol. 54, 868-874
    • (2012) J. Integr. Plant Biol. , vol.54 , pp. 868-874
    • Vick, J.K.1    Nebenführ, A.2
  • 4
    • 71249131277 scopus 로고    scopus 로고
    • Myosin XI is required for actin-associated movement of plastid stromules
    • Natesan, S. K., Sullivan, J. A., and Gray, J. C. (2009) Myosin XI is required for actin-associated movement of plastid stromules. Mol. Plant 2, 1262-1272
    • (2009) Mol. Plant , vol.2 , pp. 1262-1272
    • Natesan, S.K.1    Sullivan, J.A.2    Gray, J.C.3
  • 5
    • 77955896359 scopus 로고    scopus 로고
    • Class XI myosins are required for development, cell expansion, and F-actin organization in Arabidopsis
    • Peremyslov, V. V., Prokhnevsky, A. I., and Dolja, V. V. (2010) Class XI myosins are required for development, cell expansion, and F-actin organization in Arabidopsis. Plant Cell 22, 1883-1897
    • (2010) Plant Cell , vol.22 , pp. 1883-1897
    • Peremyslov, V.V.1    Prokhnevsky, A.I.2    Dolja, V.V.3
  • 6
    • 58149382585 scopus 로고    scopus 로고
    • Overlapping functions of the four class XI myosins in Arabidopsis growth, root hair elongation, and organelle motility
    • Prokhnevsky, A. I., Peremyslov, V. V., and Dolja, V. V. (2008) Overlapping functions of the four class XI myosins in Arabidopsis growth, root hair elongation, and organelle motility. Proc. Natl. Acad. Sci. USA 105, 19744-19749
    • (2008) Proc. Natl. Acad. Sci. USA , vol.105 , pp. 19744-19749
    • Prokhnevsky, A.I.1    Peremyslov, V.V.2    Dolja, V.V.3
  • 8
    • 0036013394 scopus 로고    scopus 로고
    • Visualization of peroxisomes in living plant cells reveals acto-myosin-dependent cytoplasmic streaming and peroxisome budding
    • Jedd, G., and Chua, N. H. (2002) Visualization of peroxisomes in living plant cells reveals acto-myosin-dependent cytoplasmic streaming and peroxisome budding. Plant Cell Physiol. 43, 384-392
    • (2002) Plant Cell Physiol. , vol.43 , pp. 384-392
    • Jedd, G.1    Chua, N.H.2
  • 10
    • 84883341421 scopus 로고    scopus 로고
    • Cytoplasmic streaming in plant cells emerges naturally by microfilament self-organization
    • Woodhouse, F. G., and Goldstein, R. E. (2013) Cytoplasmic streaming in plant cells emerges naturally by microfilament self-organization. Proc. Natl. Acad. Sci. USA 110, 14132-14137
    • (2013) Proc. Natl. Acad. Sci. USA , vol.110 , pp. 14132-14137
    • Woodhouse, F.G.1    Goldstein, R.E.2
  • 11
    • 12444257811 scopus 로고    scopus 로고
    • Dynamic rearrangements of transvacuolar strands in BY-2 cells imply a role of myosin in remodeling the plant actin cytoskeleton
    • Hoffmann, A., and Nebenführ, A. (2004) Dynamic rearrangements of transvacuolar strands in BY-2 cells imply a role of myosin in remodeling the plant actin cytoskeleton. Protoplasma 224, 201-210
    • (2004) Protoplasma , vol.224 , pp. 201-210
    • Hoffmann, A.1    Nebenführ, A.2
  • 12
    • 79956049098 scopus 로고    scopus 로고
    • Myosin XI-dependent formation of tubular structures from endoplasmic reticulum isolated from tobacco cultured BY-2 cells
    • Yokota, E., Ueda, H., Hashimoto, K., Orii, H., Shimada, T., Hara-Nishimura, I., and Shimmen, T. (2011) Myosin XI-dependent formation of tubular structures from endoplasmic reticulum isolated from tobacco cultured BY-2 cells. Plant Physiol. 156, 129-143
    • (2011) Plant Physiol. , vol.156 , pp. 129-143
    • Yokota, E.1    Ueda, H.2    Hashimoto, K.3    Orii, H.4    Shimada, T.5    Hara-Nishimura, I.6    Shimmen, T.7
  • 13
    • 60149090338 scopus 로고    scopus 로고
    • An isoform of myosin XI is responsible for the translocation of endoplasmic reticulum in tobacco cultured BY-2 cells
    • Yokota, E., Ueda, S., Tamura, K., Orii, H., Uchi, S., Sonobe, S., Hara-Nishimura, I., and Shimmen, T. (2009) An isoform of myosin XI is responsible for the translocation of endoplasmic reticulum in tobacco cultured BY-2 cells. J. Exp. Bot. 60, 197-212
    • (2009) J. Exp. Bot. , vol.60 , pp. 197-212
    • Yokota, E.1    Ueda, S.2    Tamura, K.3    Orii, H.4    Uchi, S.5    Sonobe, S.6    Hara-Nishimura, I.7    Shimmen, T.8
  • 14
    • 0024007381 scopus 로고
    • The mechanism of cytoplasmic streaming in characean algal cells: Sliding of endoplasmic reticulum along actin filaments
    • Kachar, B., and Reese, T. S. (1988) The mechanism of cytoplasmic streaming in characean algal cells: sliding of endoplasmic reticulum along actin filaments. J. Cell Biol. 106, 1545-1552
    • (1988) J. Cell Biol. , vol.106 , pp. 1545-1552
    • Kachar, B.1    Reese, T.S.2
  • 19
  • 20
  • 22
    • 84899727649 scopus 로고    scopus 로고
    • Molecular characterization and subcellular localization of Arabidopsis class VIII myosin, ATM1
    • Haraguchi, T., Tominaga, M., Matsumoto, R., Sato, K., Nakano, A., Yamamoto, K., and Ito, K. (2014) Molecular characterization and subcellular localization of Arabidopsis class VIII myosin, ATM1. J. Biol. Chem. 289, 12343-12355
    • (2014) J. Biol. Chem. , vol.289 , pp. 12343-12355
    • Haraguchi, T.1    Tominaga, M.2    Matsumoto, R.3    Sato, K.4    Nakano, A.5    Yamamoto, K.6    Ito, K.7
  • 24
    • 0035943690 scopus 로고    scopus 로고
    • Kinetic mechanism and regulation of myosin VI
    • De La Cruz, E. M., Ostap, E. M., and Sweeney, H. L. (2001) Kinetic mechanism and regulation of myosin VI. J. Biol. Chem. 276, 32373-32381
    • (2001) J. Biol. Chem. , vol.276 , pp. 32373-32381
    • De La Cruz, E.M.1    Ostap, E.M.2    Sweeney, H.L.3
  • 25
    • 25444475796 scopus 로고    scopus 로고
    • Myosin VIIB from Drosophila is a high duty ratio motor
    • Yang, Y., Kovács, M., Xu, Q., Anderson, J. B., and Sellers, J. R. (2005) Myosin VIIB from Drosophila is a high duty ratio motor. J. Biol. Chem. 280, 32061-32068
    • (2005) J. Biol. Chem. , vol.280 , pp. 32061-32068
    • Yang, Y.1    Kovács, M.2    Xu, Q.3    Anderson, J.B.4    Sellers, J.R.5
  • 28
  • 31
    • 84878144032 scopus 로고    scopus 로고
    • Global fit analysis of myosin-5b motility reveals thermodynamics of Mg2+-sensitive acto-myosin-ADP states
    • Chizhov, I., Hartmann, F. K., Hundt, N., and Tsiavaliaris, G. (2013) Global fit analysis of myosin-5b motility reveals thermodynamics of Mg2+-sensitive acto-myosin-ADP states. PLoS ONE 8, e64797
    • (2013) PLoS ONE , vol.8
    • Chizhov, I.1    Hartmann, F.K.2    Hundt, N.3    Tsiavaliaris, G.4
  • 32
    • 77958098477 scopus 로고    scopus 로고
    • Efficient formulations for exact stochastic simulation of chemical systems
    • Mauch, S., and Stalzer, M. (2011) Efficient formulations for exact stochastic simulation of chemical systems. IEEE/ACM Trans. Comput. Biol. Bioinform. 8, 27-35
    • (2011) IEEE/ACM Trans. Comput. Biol. Bioinform. , vol.8 , pp. 27-35
    • Mauch, S.1    Stalzer, M.2
  • 33
    • 60549105802 scopus 로고    scopus 로고
    • Global kinetic explorer: A new computer program for dynamic simulation and fitting of kinetic data
    • Johnson, K. A., Simpson, Z. B., and Blom, T. (2009) Global kinetic explorer: a new computer program for dynamic simulation and fitting of kinetic data. Anal. Biochem. 387, 20-29
    • (2009) Anal. Biochem. , vol.387 , pp. 20-29
    • Johnson, K.A.1    Simpson, Z.B.2    Blom, T.3
  • 35
    • 0027136282 scopus 로고
    • Comparative protein modelling by satisfaction of spatial restraints
    • Sali, A., and Blundell, T. L. (1993) Comparative protein modelling by satisfaction of spatial restraints. J. Mol. Biol. 234, 779-815
    • (1993) J. Mol. Biol. , vol.234 , pp. 779-815
    • Sali, A.1    Blundell, T.L.2
  • 36
    • 0032559298 scopus 로고    scopus 로고
    • Simultaneous observation of individual ATPase and mechanical events by a single myosin molecule during interaction with actin
    • Ishijima, A., Kojima, H., Funatsu, T., Tokunaga, M., Higuchi, H., Tanaka, H., and Yanagida, T. (1998) Simultaneous observation of individual ATPase and mechanical events by a single myosin molecule during interaction with actin. Cell 92, 161-171
    • (1998) Cell , vol.92 , pp. 161-171
    • Ishijima, A.1    Kojima, H.2    Funatsu, T.3    Tokunaga, M.4    Higuchi, H.5    Tanaka, H.6    Yanagida, T.7
  • 37
    • 0031668720 scopus 로고    scopus 로고
    • Orientation dependence of displacements by a single one-headed myosin relative to the actin filament
    • Tanaka, H., Ishijima, A., Honda, M., Saito, K., and Yanagida, T. (1998) Orientation dependence of displacements by a single one-headed myosin relative to the actin filament. Biophys. J. 75, 1886-1894
    • (1998) Biophys. J. , vol.75 , pp. 1886-1894
    • Tanaka, H.1    Ishijima, A.2    Honda, M.3    Saito, K.4    Yanagida, T.5
  • 40
    • 0001903222 scopus 로고
    • Note sur la convergence des methodes de directions conjuguees
    • Polak, B., and Ribiere, G. (1969) Note sur la convergence des methodes de directions conjuguees. Rev. Fr. Inform. Rech. Oper. 16, 35-43
    • (1969) Rev. Fr. Inform. Rech. Oper. , vol.16 , pp. 35-43
    • Polak, B.1    Ribiere, G.2
  • 42
    • 14044259423 scopus 로고    scopus 로고
    • Changes in Mg2+ ion concentration and heavy chain phosphorylation regulate the motor activity of a class I myosin
    • Fujita-Becker, S., Dürrwang, U., Erent, M., Clark, R. J., Geeves, M. A., and Manstein, D. J. (2005) Changes in Mg2+ ion concentration and heavy chain phosphorylation regulate the motor activity of a class I myosin. J. Biol. Chem. 280, 6064-6071
    • (2005) J. Biol. Chem. , vol.280 , pp. 6064-6071
    • Fujita-Becker, S.1    Dürrwang, U.2    Erent, M.3    Clark, R.J.4    Geeves, M.A.5    Manstein, D.J.6
  • 44
    • 84880070665 scopus 로고    scopus 로고
    • Magnesium impacts myosin V motor activity by altering key conformational changes in the mechanochemical cycle
    • Trivedi, D. V., Muretta, J. M., Swenson, A. M., Thomas, D. D., and Yengo, C. M. (2013) Magnesium impacts myosin V motor activity by altering key conformational changes in the mechanochemical cycle. Biochemistry 52, 4710-4722
    • (2013) Biochemistry , vol.52 , pp. 4710-4722
    • Trivedi, D.V.1    Muretta, J.M.2    Swenson, A.M.3    Thomas, D.D.4    Yengo, C.M.5
  • 46
    • 0017731352 scopus 로고
    • The mechanism of adenosine triphosphate hydrolysis by myosin
    • proceedings
    • Bagshaw, C. R. (1977) The mechanism of adenosine triphosphate hydrolysis by myosin [proceedings]. Biochem. Soc. Trans. 5, 1272-1274
    • (1977) Biochem. Soc. Trans. , vol.5 , pp. 1272-1274
    • Bagshaw, C.R.1
  • 47
    • 0016161552 scopus 로고
    • The magnesium ion-dependent adenosine triphosphatase of myosin. Two-step processes of adenosine triphosphate association and adenosine diphosphate dissociation
    • Bagshaw, C. R., Eccleston, J. F., Eckstein, F., Goody, R. S., Gutfreund, H., and Trentham, D. R. (1974) The magnesium ion-dependent adenosine triphosphatase of myosin. Two-step processes of adenosine triphosphate association and adenosine diphosphate dissociation. Biochem. J. 141, 351-364
    • (1974) Biochem. J. , vol.141 , pp. 351-364
    • Bagshaw, C.R.1    Eccleston, J.F.2    Eckstein, F.3    Goody, R.S.4    Gutfreund, H.5    Trentham, D.R.6
  • 48
    • 0021201855 scopus 로고
    • Kinetics of acto-S1 interaction as a guide to a model for the crossbridge cycle
    • Geeves, M. A., Goody, R. S., and Gutfreund, H. (1984) Kinetics of acto-S1 interaction as a guide to a model for the crossbridge cycle. J. Muscle Res. Cell Motil. 5, 351-361
    • (1984) J. Muscle Res. Cell Motil. , vol.5 , pp. 351-361
    • Geeves, M.A.1    Goody, R.S.2    Gutfreund, H.3
  • 49
    • 0020501746 scopus 로고
    • The limiting rate of the ATP-mediated dissociation of actin from rabbit skeletal muscle myosin subfragment 1
    • Millar, N. C., and Geeves, M. A. (1983) The limiting rate of the ATP-mediated dissociation of actin from rabbit skeletal muscle myosin subfragment 1. FEBS Lett. 160, 141-148
    • (1983) FEBS Lett. , vol.160 , pp. 141-148
    • Millar, N.C.1    Geeves, M.A.2
  • 50
    • 0033709850 scopus 로고    scopus 로고
    • A flash photolysis fluorescence/light scattering apparatus for use with sub microgram quantities of muscle proteins
    • Weiss, S., Chizhov, I., and Geeves, M. A. (2000) A flash photolysis fluorescence/light scattering apparatus for use with sub microgram quantities of muscle proteins. J. Muscle Res. Cell Motil. 21, 423-432
    • (2000) J. Muscle Res. Cell Motil. , vol.21 , pp. 423-432
    • Weiss, S.1    Chizhov, I.2    Geeves, M.A.3
  • 51
    • 33646595393 scopus 로고    scopus 로고
    • Toward understanding actin activation of myosin ATPase: The role of myosin surface loops
    • Onishi, H., Mikhailenko, S. V., and Morales, M. F. (2006) Toward understanding actin activation of myosin ATPase: the role of myosin surface loops. Proc. Natl. Acad. Sci. USA 103, 6136-6141
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 6136-6141
    • Onishi, H.1    Mikhailenko, S.V.2    Morales, M.F.3
  • 52
    • 0033583079 scopus 로고    scopus 로고
    • Specialized conservation of surface loops of myosin: Evidence that loops are involved in determining functional characteristics
    • Goodson, H. V., Warrick, H. M., and Spudich, J. A. (1999) Specialized conservation of surface loops of myosin: evidence that loops are involved in determining functional characteristics. J. Mol. Biol. 287, 173-185
    • (1999) J. Mol. Biol. , vol.287 , pp. 173-185
    • Goodson, H.V.1    Warrick, H.M.2    Spudich, J.A.3
  • 53
    • 0032485859 scopus 로고    scopus 로고
    • Modulation of actin affinity and actomyosin adenosine triphosphatase by charge changes in the myosin motor domain
    • Furch, M., Geeves, M. A., and Manstein, D. J. (1998) Modulation of actin affinity and actomyosin adenosine triphosphatase by charge changes in the myosin motor domain. Biochemistry 37, 6317-6326
    • (1998) Biochemistry , vol.37 , pp. 6317-6326
    • Furch, M.1    Geeves, M.A.2    Manstein, D.J.3
  • 55
    • 0042165822 scopus 로고    scopus 로고
    • Addition of lysines to the 50/20 kDa junction of myosin strengthens weak binding to actin without affecting the maximum ATPase activity
    • Joel, P. B., Sweeney, H. L., and Trybus, K. M. (2003) Addition of lysines to the 50/20 kDa junction of myosin strengthens weak binding to actin without affecting the maximum ATPase activity. Biochemistry 42, 9160-9166
    • (2003) Biochemistry , vol.42 , pp. 9160-9166
    • Joel, P.B.1    Sweeney, H.L.2    Trybus, K.M.3
  • 56
    • 0034681913 scopus 로고    scopus 로고
    • Charge changes in loop 2 affect the thermal unfolding of the myosin motor domain bound to F-actin
    • Ponomarev, M. A., Furch, M., Levitsky, D. I., and Manstein, D. J. (2000) Charge changes in loop 2 affect the thermal unfolding of the myosin motor domain bound to F-actin. Biochemistry 39, 4527-4532
    • (2000) Biochemistry , vol.39 , pp. 4527-4532
    • Ponomarev, M.A.1    Furch, M.2    Levitsky, D.I.3    Manstein, D.J.4
  • 57
    • 0033596962 scopus 로고    scopus 로고
    • The sequence of the myosin 50-20K loop affects myosin's affinity for actin throughout the actin-myosin ATPase cycle and its maximum ATPase activity
    • Murphy, C. T., and Spudich, J. A. (1999) The sequence of the myosin 50-20K loop affects myosin's affinity for actin throughout the actin-myosin ATPase cycle and its maximum ATPase activity. Biochemistry 38, 3785-3792
    • (1999) Biochemistry , vol.38 , pp. 3785-3792
    • Murphy, C.T.1    Spudich, J.A.2
  • 58
    • 0035793563 scopus 로고    scopus 로고
    • Two conserved lysines at the 50/20-kDa junction of myosin are necessary for triggering actin activation
    • Joel, P. B., Trybus, K. M., and Sweeney, H. L. (2001) Two conserved lysines at the 50/20-kDa junction of myosin are necessary for triggering actin activation. J. Biol. Chem. 276, 2998-3003
    • (2001) J. Biol. Chem. , vol.276 , pp. 2998-3003
    • Joel, P.B.1    Trybus, K.M.2    Sweeney, H.L.3
  • 59
    • 34848896360 scopus 로고    scopus 로고
    • Engineering the processive run length of myosin V
    • Hodges, A. R., Krementsova, E. B., and Trybus, K. M. (2007) Engineering the processive run length of myosin V. J. Biol. Chem. 282, 27192-27197
    • (2007) J. Biol. Chem. , vol.282 , pp. 27192-27197
    • Hodges, A.R.1    Krementsova, E.B.2    Trybus, K.M.3
  • 60
    • 1542267772 scopus 로고    scopus 로고
    • Functional role of loop 2 in myosin V
    • Yengo, C. M., and Sweeney, H. L. (2004) Functional role of loop 2 in myosin V. Biochemistry 43, 2605-2612
    • (2004) Biochemistry , vol.43 , pp. 2605-2612
    • Yengo, C.M.1    Sweeney, H.L.2
  • 61
    • 0033576318 scopus 로고    scopus 로고
    • Functional characterization of the secondary actin binding site of myosin II
    • VanDijk, J., Furch, M., Lafont, C., Manstein, D. J., and Chaussepied, P. (1999) Functional characterization of the secondary actin binding site of myosin II. Biochemistry 38, 15078-15085
    • (1999) Biochemistry , vol.38 , pp. 15078-15085
    • VanDijk, J.1    Furch, M.2    Lafont, C.3    Manstein, D.J.4    Chaussepied, P.5
  • 62
    • 76049122706 scopus 로고    scopus 로고
    • Unique charge distribution in surface loops confers high velocity on the fast motor protein Chara myosin
    • Ito, K., Yamaguchi, Y., Yanase, K., Ichikawa, Y., and Yamamoto, K. (2009) Unique charge distribution in surface loops confers high velocity on the fast motor protein Chara myosin. Proc. Natl. Acad. Sci. USA 106, 21585-21590
    • (2009) Proc. Natl. Acad. Sci. USA , vol.106 , pp. 21585-21590
    • Ito, K.1    Yamaguchi, Y.2    Yanase, K.3    Ichikawa, Y.4    Yamamoto, K.5
  • 63
    • 0033621469 scopus 로고    scopus 로고
    • Deletion of the myopathy loop of Dictyostelium myosin II and its impact on motor functions
    • Sasaki, N., Asukagawa, H., Yasuda, R., Hiratsuka, T., and Sutoh, K. (1999) Deletion of the myopathy loop of Dictyostelium myosin II and its impact on motor functions. J. Biol. Chem. 274, 37840-37844
    • (1999) J. Biol. Chem. , vol.274 , pp. 37840-37844
    • Sasaki, N.1    Asukagawa, H.2    Yasuda, R.3    Hiratsuka, T.4    Sutoh, K.5
  • 65
    • 0027272935 scopus 로고
    • Smooth and skeletal muscle myosin both exhibit low duty cycles at zero load in vitro
    • Harris, D. E., and Warshaw, D. M. (1993) Smooth and skeletal muscle myosin both exhibit low duty cycles at zero load in vitro. J. Biol. Chem. 268, 14764-14768
    • (1993) J. Biol. Chem. , vol.268 , pp. 14764-14768
    • Harris, D.E.1    Warshaw, D.M.2
  • 66
    • 82755192841 scopus 로고    scopus 로고
    • Shaking the myosin family tree: Biochemical kinetics defines four types of myosin motor
    • Bloemink, M. J., and Geeves, M. A. (2011) Shaking the myosin family tree: biochemical kinetics defines four types of myosin motor. Semin. Cell Dev. Biol. 22, 961-967
    • (2011) Semin. Cell Dev. Biol. , vol.22 , pp. 961-967
    • Bloemink, M.J.1    Geeves, M.A.2
  • 67
    • 14044268874 scopus 로고    scopus 로고
    • Magnesium regulates ADP dissociation from myosin V
    • Rosenfeld, S. S., Houdusse, A., and Sweeney, H. L. (2005) Magnesium regulates ADP dissociation from myosin V. J. Biol. Chem. 280, 6072-6079
    • (2005) J. Biol. Chem. , vol.280 , pp. 6072-6079
    • Rosenfeld, S.S.1    Houdusse, A.2    Sweeney, H.L.3
  • 69
    • 33845894135 scopus 로고    scopus 로고
    • Regulation of myosin V processivity by calcium at the single molecule level
    • Lu, H., Krementsova, E. B., and Trybus, K. M. (2006) Regulation of myosin V processivity by calcium at the single molecule level. J. Biol. Chem. 281, 31987-31994
    • (2006) J. Biol. Chem. , vol.281 , pp. 31987-31994
    • Lu, H.1    Krementsova, E.B.2    Trybus, K.M.3
  • 71
    • 0033850082 scopus 로고    scopus 로고
    • ADP inhibition of myosin V ATPase activity
    • De La Cruz, E. M., Sweeney, H. L., and Ostap, E. M. (2000) ADP inhibition of myosin V ATPase activity. Biophys. J. 79, 1524-1529
    • (2000) Biophys. J. , vol.79 , pp. 1524-1529
    • De La Cruz, E.M.1    Sweeney, H.L.2    Ostap, E.M.3
  • 72
    • 0037444793 scopus 로고    scopus 로고
    • Interactions of the two heads of scallop (Argopecten irradians) heavy meromyosin with actin: Influence of calcium and nucleotides
    • Nyitrai, M., Szent-Györgyi, A. G., and Geeves, M. A. (2003) Interactions of the two heads of scallop (Argopecten irradians) heavy meromyosin with actin: influence of calcium and nucleotides. Biochem. J. 370, 839-848
    • (2003) Biochem. J. , vol.370 , pp. 839-848
    • Nyitrai, M.1    Szent-Györgyi, A.G.2    Geeves, M.A.3
  • 73
    • 84865734804 scopus 로고    scopus 로고
    • Calcium-induced mechanical change in the neck domain alters the activity of plant myosin XI
    • Tominaga, M., Kojima, H., Yokota, E., Nakamori, R., Anson, M., Shimmen, T., and Oiwa, K. (2012) Calcium-induced mechanical change in the neck domain alters the activity of plant myosin XI. J. Biol. Chem. 287, 30711-30718
    • (2012) J. Biol. Chem. , vol.287 , pp. 30711-30718
    • Tominaga, M.1    Kojima, H.2    Yokota, E.3    Nakamori, R.4    Anson, M.5    Shimmen, T.6    Oiwa, K.7
  • 74
    • 50749096982 scopus 로고
    • Changes in the intracellular levels of ATP, ADP, AMP and P1 and regulatory function of the adenylate system in leaf cells during photosynthesis
    • Santarius, K. A., and Heber, U. (1965) Changes in the intracellular levels of ATP, ADP, AMP and P1 and regulatory function of the adenylate system in leaf cells during photosynthesis. Biochim. Biophys. Acta 102, 39-54
    • (1965) Biochim. Biophys. Acta , vol.102 , pp. 39-54
    • Santarius, K.A.1    Heber, U.2
  • 75
    • 0022106034 scopus 로고
    • Relationships between the rate of synthesis of ATP and the concentrations of reactants and products of ATP hydrolysis in maize root tips, determined by 31P nuclear magnetic resonance
    • Roberts, J. K., Lane, A. N., Clark, R. A., and Nieman, R. H. (1985) Relationships between the rate of synthesis of ATP and the concentrations of reactants and products of ATP hydrolysis in maize root tips, determined by 31P nuclear magnetic resonance. Arch. Biochem. Biophys. 240, 712-722
    • (1985) Arch. Biochem. Biophys. , vol.240 , pp. 712-722
    • Roberts, J.K.1    Lane, A.N.2    Clark, R.A.3    Nieman, R.H.4
  • 76
    • 0014298705 scopus 로고
    • The intracellular distribution of free nucleotides in the tobacco leaf. Formation of adenosine 5′-phosphate from adenosine 5′-triphosphate in the chloroplasts
    • Keys, A. J. (1968) The intracellular distribution of free nucleotides in the tobacco leaf. Formation of adenosine 5′-phosphate from adenosine 5′-triphosphate in the chloroplasts. Biochem. J. 108, 1-8
    • (1968) Biochem. J. , vol.108 , pp. 1-8
    • Keys, A.J.1
  • 77
    • 0000437024 scopus 로고
    • Role of metabolites in the reversible light activation of pyruvate, orthophosphate dikinase in Zea mays mesophyll cells in vivo
    • Roeske, C. A., and Chollet, R. (1989) Role of metabolites in the reversible light activation of pyruvate, orthophosphate dikinase in Zea mays mesophyll cells in vivo. Plant Physiol. 90, 330-337
    • (1989) Plant Physiol. , vol.90 , pp. 330-337
    • Roeske, C.A.1    Chollet, R.2
  • 78
    • 0001060481 scopus 로고
    • Adenylate levels, energy charge, and phosphorylation potential during dark-light and light-dark transition in chloroplasts, mitochondria, and cytosol of mesophyll protoplasts from Avena sativa L
    • Hampp, R., Goller, M., and Ziegler, H. (1982) Adenylate levels, energy charge, and phosphorylation potential during dark-light and light-dark transition in chloroplasts, mitochondria, and cytosol of mesophyll protoplasts from Avena sativa L. Plant Physiol. 69, 448-455
    • (1982) Plant Physiol. , vol.69 , pp. 448-455
    • Hampp, R.1    Goller, M.2    Ziegler, H.3
  • 79
    • 0001674051 scopus 로고
    • Estimation of cytoplasmic free Mg2+ levels and phosphorylation potentials in mung bean root tips by in vivo 31PNMR spectroscopy
    • Yazaki, Y., Asukagawa, N., Ishikawa, Y., Ohta, E., and Sakata, M. (1988) Estimation of cytoplasmic free Mg2+ levels and phosphorylation potentials in mung bean root tips by in vivo 31PNMR spectroscopy. Plant Cell Physiol. 29, 919-924
    • (1988) Plant Cell Physiol. , vol.29 , pp. 919-924
    • Yazaki, Y.1    Asukagawa, N.2    Ishikawa, Y.3    Ohta, E.4    Sakata, M.5
  • 80
    • 34047276448 scopus 로고    scopus 로고
    • ORYZA SATIVA MYOSIN XI B controls pollen development by photoperiod-sensitive protein localizations
    • Jiang, S. Y., Cai, M., and Ramachandran, S. (2007) ORYZA SATIVA MYOSIN XI B controls pollen development by photoperiod-sensitive protein localizations. Dev. Biol. 304, 579-592
    • (2007) Dev. Biol. , vol.304 , pp. 579-592
    • Jiang, S.Y.1    Cai, M.2    Ramachandran, S.3
  • 81
    • 77949542561 scopus 로고    scopus 로고
    • Cytoplasmic streaming enables the distribution of molecules and vesicles in large plant cells
    • Verchot-Lubicz, J., and Goldstein, R. E. (2010) Cytoplasmic streaming enables the distribution of molecules and vesicles in large plant cells. Protoplasma 240, 99-107
    • (2010) Protoplasma , vol.240 , pp. 99-107
    • Verchot-Lubicz, J.1    Goldstein, R.E.2
  • 84
    • 0027327250 scopus 로고
    • Partial characterization of the Nicotiana tabacum actin gene family: Evidence for pollen-specific expression of one of the gene family members
    • Thangavelu, M., Belostotsky, D., Bevan, M. W., Flavell, R. B., Rogers, H. J., and Lonsdale, D. M. (1993) Partial characterization of the Nicotiana tabacum actin gene family: evidence for pollen-specific expression of one of the gene family members. Mol. Gen. Genet. 240, 290-295
    • (1993) Mol. Gen. Genet. , vol.240 , pp. 290-295
    • Thangavelu, M.1    Belostotsky, D.2    Bevan, M.W.3    Flavell, R.B.4    Rogers, H.J.5    Lonsdale, D.M.6
  • 86
    • 10344262074 scopus 로고    scopus 로고
    • Phylogeny and substitution rates of angiosperm actin genes
    • Moniz de Sá, M., and Drouin, G. (1996) Phylogeny and substitution rates of angiosperm actin genes. Mol. Biol. Evol. 13, 1198-1212
    • (1996) Mol. Biol. Evol. , vol.13 , pp. 1198-1212
    • Moniz De Sá, M.1    Drouin, G.2
  • 88
    • 0033149815 scopus 로고    scopus 로고
    • Isovariant dynamics expand and buffer the responses of complex systems: The diverse plant actin gene family
    • Meagher, R. B., McKinney, E. C., and Kandasamy, M. K. (1999) Isovariant dynamics expand and buffer the responses of complex systems: the diverse plant actin gene family. Plant Cell 11, 995-1006
    • (1999) Plant Cell , vol.11 , pp. 995-1006
    • Meagher, R.B.1    McKinney, E.C.2    Kandasamy, M.K.3
  • 89
    • 80053504267 scopus 로고    scopus 로고
    • Recent advances in understanding plant myosin function: Life in the fast lane
    • Sparkes, I. (2011) Recent advances in understanding plant myosin function: life in the fast lane. Mol. Plant 4, 805-812
    • (2011) Mol. Plant , vol.4 , pp. 805-812
    • Sparkes, I.1


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