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Volumn 45, Issue 38, 2006, Pages 11589-11597

Temperature dependence of nucleotide association and kinetic characterization of Myo1b

Author keywords

[No Author keywords available]

Indexed keywords

ACTIVATION ENERGY; ADENOSINETRIPHOSPHATE; BIOCHEMICAL ENGINEERING; ENZYMES; MEMBRANES; PHOSPHATES; RATE CONSTANTS; THERMAL EFFECTS;

EID: 33749008779     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi0611917     Document Type: Article
Times cited : (27)

References (40)
  • 1
    • 33644771150 scopus 로고    scopus 로고
    • Myo1c binds tightly and specifically to phosphatidylinositol 4, 5-bisphosphate and inositol 1, 4, 5-trisphosphate
    • Hokanson, D. E., and Ostap, E. M. (2006) Myo1c binds tightly and specifically to phosphatidylinositol 4, 5-bisphosphate and inositol 1, 4, 5-trisphosphate, Proc. Natl. Acad. Sci. U.S.A. 103, 3118-23.
    • (2006) Proc. Natl. Acad. Sci. U.S.A. , vol.103 , pp. 3118-3123
    • Hokanson, D.E.1    Ostap, E.M.2
  • 2
    • 0027499951 scopus 로고
    • Identification, characterization and cloning of myr 1, a mammalian myosin-I
    • Ruppert, C., Kroschewski, R., and Bahler, M. (1993) Identification, characterization and cloning of myr 1, a mammalian myosin-I, J. Cell Biol. 120, 1393-403.
    • (1993) J. Cell Biol. , vol.120 , pp. 1393-1403
    • Ruppert, C.1    Kroschewski, R.2    Bahler, M.3
  • 3
    • 0035943018 scopus 로고    scopus 로고
    • Motor domain-dependent localization of myo1b (myr-1)
    • Tang, N., and Ostap, E. M. (2001) Motor domain-dependent localization of myo1b (myr-1), Curr. Biol. 11, 1131-5.
    • (2001) Curr. Biol. , vol.11 , pp. 1131-1135
    • Tang, N.1    Ostap, E.M.2
  • 7
    • 33645749163 scopus 로고    scopus 로고
    • Type ID unconventional myosin controls left-right asymmetry in Drosophila
    • Speder, P., Adam, G., and Noselli, S. (2006) Type ID unconventional myosin controls left-right asymmetry in Drosophila, Nature 440, 803-7.
    • (2006) Nature , vol.440 , pp. 803-807
    • Speder, P.1    Adam, G.2    Noselli, S.3
  • 9
    • 0029915892 scopus 로고    scopus 로고
    • Biochemical kinetic characterization of the Acanthamoeba myosin-I ATPase
    • Ostap, E. M., and Pollard, T. D. (1996) Biochemical kinetic characterization of the Acanthamoeba myosin-I ATPase, J. Cell Biol. 132, 1053-60.
    • (1996) J. Cell Biol. , vol.132 , pp. 1053-1060
    • Ostap, E.M.1    Pollard, T.D.2
  • 13
    • 0033618274 scopus 로고    scopus 로고
    • Transient kinetic analysis of the 130-kDa myosin I (MYR-1 gene product) from rat liver. A myosin I designed for maintenance of tension?
    • Coluccio, L. M., and Geeves, M. A. (1999) Transient kinetic analysis of the 130-kDa myosin I (MYR-1 gene product) from rat liver. A myosin I designed for maintenance of tension? J. Biol. Chem. 274, 21575-80.
    • (1999) J. Biol. Chem. , vol.274 , pp. 21575-21580
    • Coluccio, L.M.1    Geeves, M.A.2
  • 14
    • 0034647735 scopus 로고    scopus 로고
    • Kinetic analyses of a truncated mammalian myosin I suggest a novel isomerization event preceding nucleotide binding
    • Geeves, M. A., Perreault-Micale, C., and Coluccio, L. M. (2000) Kinetic analyses of a truncated mammalian myosin I suggest a novel isomerization event preceding nucleotide binding, J. Biol. Chem. 275, 21624-30.
    • (2000) J. Biol. Chem. , vol.275 , pp. 21624-21630
    • Geeves, M.A.1    Perreault-Micale, C.2    Coluccio, L.M.3
  • 15
    • 24744460288 scopus 로고    scopus 로고
    • Loop 1 of transducer region in mammalian class I myosin, Myo1b, modulates actin affinity, ATPase activity, and nucleotide access
    • Clark, R., Ansari, M. A., Dash, S., Geeves, M. A., and Coluccio, L. M. (2005) Loop 1 of transducer region in mammalian class I myosin, Myo1b, modulates actin affinity, ATPase activity, and nucleotide access, J. Biol. Chem. 280, 30935-42.
    • (2005) J. Biol. Chem. , vol.280 , pp. 30935-30942
    • Clark, R.1    Ansari, M.A.2    Dash, S.3    Geeves, M.A.4    Coluccio, L.M.5
  • 16
    • 1642333310 scopus 로고    scopus 로고
    • Relating biochemistry and function in the myosin superfamily
    • De La Cruz, E. M., and Ostap, E. M. (2004) Relating biochemistry and function in the myosin superfamily, Curr. Opin. Cell Biol. 16, 61-7.
    • (2004) Curr. Opin. Cell Biol. , vol.16 , pp. 61-67
    • De La Cruz, E.M.1    Ostap, E.M.2
  • 17
    • 0020674810 scopus 로고
    • New ribose-modified fluorescent analogs of adenine and guanine nucleotides available as substrates for various enzymes
    • Hiratsuka, T. (1983) New ribose-modified fluorescent analogs of adenine and guanine nucleotides available as substrates for various enzymes, Biochim. Biophys. Acta 742, 496-508.
    • (1983) Biochim. Biophys. Acta , vol.742 , pp. 496-508
    • Hiratsuka, T.1
  • 18
    • 0015218407 scopus 로고
    • The regulation of rabbit skeletal muscle contraction. I. Biochemical studies of the interaction of the tropomyosin-troponin complex with actin and the proteolytic fragments of myosin
    • Spudich, J. A., and Watt, S. (1971) The regulation of rabbit skeletal muscle contraction. I. Biochemical studies of the interaction of the tropomyosin-troponin complex with actin and the proteolytic fragments of myosin, J. Biol. Chem. 246, 4866-71.
    • (1971) J. Biol. Chem. , vol.246 , pp. 4866-4871
    • Spudich, J.A.1    Watt, S.2
  • 19
    • 0021705094 scopus 로고
    • Purification of a high molecular weight actin filament gelation protein from Acanthamoeba that shares antigenic determinants with vertebrate spectrins
    • Pollard, T. D. (1984) Purification of a high molecular weight actin filament gelation protein from Acanthamoeba that shares antigenic determinants with vertebrate spectrins, J. Cell Biol. 99, 1970-80.
    • (1984) J. Cell Biol. , vol.99 , pp. 1970-1980
    • Pollard, T.D.1
  • 20
    • 0021886339 scopus 로고
    • Bacterial expression and characterization of proteins derived from the chicken calmodulin cDNA and a calmodulin processed gene
    • Putkey, J. A., Slaughter, G. R., and Means, A. R. (1985) Bacterial expression and characterization of proteins derived from the chicken calmodulin cDNA and a calmodulin processed gene, J. Biol. Chem. 260, 4704-12.
    • (1985) J. Biol. Chem. , vol.260 , pp. 4704-4712
    • Putkey, J.A.1    Slaughter, G.R.2    Means, A.R.3
  • 21
    • 29244458650 scopus 로고    scopus 로고
    • Biochemical and motile properties of Myo1b splice isoforms
    • Lin, T., Tang, N., and Ostap, E. M. (2005) Biochemical and motile properties of Myo1b splice isoforms, J. Biol. Chem. 280, 41562-7.
    • (2005) J. Biol. Chem. , vol.280 , pp. 41562-41567
    • Lin, T.1    Tang, N.2    Ostap, E.M.3
  • 23
    • 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, 32373-81.
    • (2001) J. Biol. Chem. , vol.276 , pp. 32373-32381
    • De La Cruz, E.M.1    Ostap, E.M.2    Sweeney, H.L.3
  • 24
    • 0030823636 scopus 로고    scopus 로고
    • Kinetics of nucleoside triphosphate cleavage and phosphate release steps by associated rabbit skeletal actomyosin, measured using a novel fluorescent probe for phosphate
    • White, H. D., Belknap, B., and Webb, M. R. (1997) Kinetics of nucleoside triphosphate cleavage and phosphate release steps by associated rabbit skeletal actomyosin, measured using a novel fluorescent probe for phosphate, Biochemistry 36, 11828-36.
    • (1997) Biochemistry , vol.36 , pp. 11828-11836
    • White, H.D.1    Belknap, B.2    Webb, M.R.3
  • 25
    • 0028098798 scopus 로고
    • Direct, real-time measurement of rapid inorganic phosphate release using a novel fluorescent probe and its application to actomyosin subfragment 1 ATPase
    • Brune, M., Hunter, J. L., Corrie, J. E., and Webb, M. R. (1994) Direct, real-time measurement of rapid inorganic phosphate release using a novel fluorescent probe and its application to actomyosin subfragment 1 ATPase, Biochemistry 33, 8262-71.
    • (1994) Biochemistry , vol.33 , pp. 8262-8271
    • Brune, M.1    Hunter, J.L.2    Corrie, J.E.3    Webb, M.R.4
  • 26
    • 0037108276 scopus 로고    scopus 로고
    • Mechanism of regulation of Acanthamoeba myosin-IC by heavy-chain phosphorylation
    • Ostap, E. M., Lin, T., Rosenfeld, S. S., and Tang, N. (2002) Mechanism of regulation of Acanthamoeba myosin-IC by heavy-chain phosphorylation, Biochemistry 41, 12450-6.
    • (2002) Biochemistry , vol.41 , pp. 12450-12456
    • Ostap, E.M.1    Lin, T.2    Rosenfeld, S.S.3    Tang, N.4
  • 27
    • 0034700284 scopus 로고    scopus 로고
    • Actin and light chain isoform dependence of myosin V kinetics
    • De La Cruz, E. M., Wells, A. L., Sweeney, H. L., and Ostap, E. M. (2000) Actin and light chain isoform dependence of myosin V kinetics, Biochemistry 39, 14196-202.
    • (2000) Biochemistry , vol.39 , pp. 14196-14202
    • De La Cruz, E.M.1    Wells, A.L.2    Sweeney, H.L.3    Ostap, E.M.4
  • 28
    • 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, 141-8.
    • (1983) FEBS Lett. , vol.160 , pp. 141-148
    • Millar, N.C.1    Geeves, M.A.2
  • 29
    • 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., Durrwang, 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, 6064-71.
    • (2005) J. Biol. Chem. , vol.280 , pp. 6064-6071
    • Fujita-Becker, S.1    Durrwang, U.2    Erent, M.3    Clark, R.J.4    Geeves, M.A.5    Manstein, D.J.6
  • 30
    • 20544449370 scopus 로고    scopus 로고
    • Thermodynamics of nucleotide binding to actomyosin V and VI: A positive heat capacity change accompanies strong ADP binding
    • Robblee, J. P., Cao, W., Kenn, A., Hannemann, D. E., and De La Cruz, E. M. (2005) Thermodynamics of nucleotide binding to actomyosin V and VI: a positive heat capacity change accompanies strong ADP binding, Biochemistry 44, 10238-49.
    • (2005) Biochemistry , vol.44 , pp. 10238-10249
    • Robblee, J.P.1    Cao, W.2    Kenn, A.3    Hannemann, D.E.4    De La Cruz, E.M.5
  • 31
    • 0034682824 scopus 로고    scopus 로고
    • Tryptophan 512 is sensitive to conformational changes in the rigid relay loop of smooth muscle myosin during the MgATPase cycle
    • Yengo, C. M., Chrin, L. R., Rovner, A. S., and Berger, C. L. (2000) Tryptophan 512 is sensitive to conformational changes in the rigid relay loop of smooth muscle myosin during the MgATPase cycle, J. Biol. Chem. 275, 25481-7.
    • (2000) J. Biol. Chem. , vol.275 , pp. 25481-25487
    • Yengo, C.M.1    Chrin, L.R.2    Rovner, A.S.3    Berger, C.L.4
  • 32
    • 0034719112 scopus 로고    scopus 로고
    • Resolution of conformational states of Dictyostelium myosin II motor domain using tryptophan (W501) mutants: Implications for the open-closed transition identified by crystallography
    • Malnasi-Csizmadia, A., Woolley, R. J., and Bagshaw, C. R. (2000) Resolution of conformational states of Dictyostelium myosin II motor domain using tryptophan (W501) mutants: implications for the open-closed transition identified by crystallography, Biochemistry 39, 16135-46.
    • (2000) Biochemistry , vol.39 , pp. 16135-16146
    • Malnasi-Csizmadia, A.1    Woolley, R.J.2    Bagshaw, C.R.3
  • 33
    • 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, 2605-12.
    • (2004) Biochemistry , vol.43 , pp. 2605-2612
    • Yengo, C.M.1    Sweeney, H.L.2
  • 34
    • 0026329490 scopus 로고
    • Determination of cytosolic ADP and AMP concentrations and the free energy of ATP hydrolysis in human muscle and brain tissues with 31P NMR spectroscopy
    • Roth, K., and Weiner, M. W. (1991) Determination of cytosolic ADP and AMP concentrations and the free energy of ATP hydrolysis in human muscle and brain tissues with 31P NMR spectroscopy, Magn. Reson. Med. 22, 505-11.
    • (1991) Magn. Reson. Med. , vol.22 , pp. 505-511
    • Roth, K.1    Weiner, M.W.2
  • 36
    • 26944449015 scopus 로고    scopus 로고
    • Load-dependent kinetics of myosin-V can explain its high processivity
    • Veigel, C., Schmitz, S., Wang, F., and Sellers, J. R. (2005) Load-dependent kinetics of myosin-V can explain its high processivity, Nat. Cell Biol. 7, 861-9.
    • (2005) Nat. Cell Biol. , vol.7 , pp. 861-869
    • Veigel, C.1    Schmitz, S.2    Wang, F.3    Sellers, J.R.4
  • 37
    • 0242609969 scopus 로고    scopus 로고
    • Load-dependent kinetics of force production by smooth muscle myosin measured with optical tweezers
    • Veigel, C., Molloy, J. E., Schmitz, S., and Kendrick-Jones, J. (2003) Load-dependent kinetics of force production by smooth muscle myosin measured with optical tweezers, Nat. Cell Biol. 5, 980-6.
    • (2003) Nat. Cell Biol. , vol.5 , pp. 980-986
    • Veigel, C.1    Molloy, J.E.2    Schmitz, S.3    Kendrick-Jones, J.4
  • 38
    • 33645758327 scopus 로고    scopus 로고
    • Force generation in single conventional actomyosin complexes under high dynamic load
    • Takagi, Y., Homsher, E. E., Goldman, Y. E., and Shuman, H. (2006) Force generation in single conventional actomyosin complexes under high dynamic load, Biophys. J. 90, 1295-307.
    • (2006) Biophys. J. , vol.90 , pp. 1295-1307
    • Takagi, Y.1    Homsher, E.E.2    Goldman, Y.E.3    Shuman, H.4
  • 40
    • 0032539594 scopus 로고    scopus 로고
    • Interaction of actin and ADP with the head domain of smooth muscle myosin: Implications for strain-dependent ADP release in smooth muscle
    • Cremo, C. R., and Geeves, M. A. (1998) Interaction of actin and ADP with the head domain of smooth muscle myosin: implications for strain-dependent ADP release in smooth muscle, Biochemistry 37, 1969-78.
    • (1998) Biochemistry , vol.37 , pp. 1969-1978
    • Cremo, C.R.1    Geeves, M.A.2


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