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Volumn 106, Issue 51, 2009, Pages 21585-21590

Unique charge distribution in surface loops confers high velocity on the fast motor protein Chara myosin

Author keywords

Actin; ATPase; Cytoplasmic streaming; Molecular engineering; Motility

Indexed keywords

ADENOSINE TRIPHOSPHATASE; MOLECULAR MOTOR; MUTANT PROTEIN; MYOSIN; RECOMBINANT PROTEIN;

EID: 76049122706     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.0910787106     Document Type: Article
Times cited : (31)

References (39)
  • 1
    • 0024007381 scopus 로고
    • The mechanism of cytoplasmic streaming in characean algal cells: Sliding of endoplasmic reticulum along actin filaments
    • Kachar B, Reese TS (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
  • 3
    • 0028892673 scopus 로고
    • The fastest actin-based motor protein from the green algae, Chara, and its distinct mode of interaction with actin
    • Higashi-Fujime S, et al. (1995) The fastest actin-based motor protein from the green algae, Chara, and its distinct mode of interaction with actin FEBS Lett 375:151-154.
    • (1995) FEBS Lett , vol.375 , pp. 151-154
    • Higashi-Fujime, S.1
  • 4
    • 0033935268 scopus 로고    scopus 로고
    • Cloning and characterization of a myosin from characean alga, the fastest motor protein in the world
    • Kashiyama T, Kimura N, Mimura T, Yamamoto K (2000) Cloning and characterization of a myosin from characean alga, the fastest motor protein in the world. J Biochem 127:1065-1070.
    • (2000) J Biochem , vol.127 , pp. 1065-1070
    • Kashiyama, T.1    Kimura, N.2    Mimura, T.3    Yamamoto, K.4
  • 5
    • 0344064204 scopus 로고    scopus 로고
    • Recombinantmotordomainconstructs of Chara corallina myosin display fast velocity and high ATPase activity
    • Ito K, et al. (2003) Recombinantmotordomainconstructs of Chara corallina myosin display fast velocity and high ATPase activity. Biochem Biophys Res Commun 312:958-964.
    • (2003) Biochem Biophys Res Commun , vol.312 , pp. 958-964
    • Ito, K.1
  • 6
    • 34547122257 scopus 로고    scopus 로고
    • Kinetic mechanism of the fastest motor protein, Chara myosin
    • Ito K, et al. (2007) Kinetic mechanism of the fastest motor protein, Chara myosin. J Biol Chem 282:19534-19545.
    • (2007) J Biol Chem , vol.282 , pp. 19534-19545
    • Ito, K.1
  • 8
    • 33646595393 scopus 로고    scopus 로고
    • Toward understanding actin activation of myosin ATPase: The role of myosin surface loops
    • Onishi H, Mikhailenko SV, Morales MF (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
  • 9
    • 0018609595 scopus 로고
    • Interaction of myosin subfragment-1 with actin. I. Effects of actin binding on the susceptibility of subfragment-1 to trypsin
    • Yamamoto K, Sekine T (1979) Interaction of myosin subfragment-1 with actin. I. Effects of actin binding on the susceptibility of subfragment-1 to trypsin. J Biochem 86:1855-1862.
    • (1979) J Biochem , vol.86 , pp. 1855-1862
    • Yamamoto, K.1    Sekine, T.2
  • 10
    • 0018789449 scopus 로고
    • The limited tryptic cleavage of chymotryptic S-1:Anapproach to the characterization of the actin site in myosin heads
    • Mornet D, Pantel P, Audemard E, Kassab R (1979) The limited tryptic cleavage of chymotryptic S-1:Anapproach to the characterization of the actin site in myosin heads. Biochem Biophys Res Commun 89:925-932.
    • (1979) Biochem Biophys Res Commun , vol.89 , pp. 925-932
    • Mornet, D.1    Pantel, P.2    Audemard, E.3    Kassab, R.4
  • 11
    • 0020395203 scopus 로고
    • An actin-binding site on the 20K fragment of myosin subfragment 1
    • Sutoh K (1982) An actin-binding site on the 20K fragment of myosin subfragment 1. Biochemistry 21:4800-4804.
    • (1982) Biochemistry , vol.21 , pp. 4800-4804
    • Sutoh, K.1
  • 12
    • 0020382825 scopus 로고
    • Identification of myosin-binding sites on the actin sequence
    • Sutoh K (1982) Identification of myosin-binding sites on the actin sequence. Biochemistry 21:3654-3661.
    • (1982) Biochemistry , vol.21 , pp. 3654-3661
    • Sutoh, K.1
  • 13
    • 0020563473 scopus 로고
    • Mapping of actin-binding sites on the heavy chain of myosin subfragment 1
    • Sutoh K (1983) Mapping of actin-binding sites on the heavy chain of myosin subfragment 1. Biochemistry 22:1579-1585.
    • (1983) Biochemistry , vol.22 , pp. 1579-1585
    • Sutoh, K.1
  • 14
    • 0022658288 scopus 로고
    • Difference between subfragment-1 and heavy meromyosin in their interaction with F-actin
    • Yamamoto K, Sekine T (1986) Difference between subfragment-1 and heavy meromyosin in their interaction with F-actin. J Biochem 99:199-206.
    • (1986) J Biochem , vol.99 , pp. 199-206
    • Yamamoto, K.1    Sekine, T.2
  • 15
    • 0024461342 scopus 로고
    • Interaction between stretch of residues 633-642 (actin binding site) and nucleotide binding site on skeletal myosin subfragment 1 heavy chain
    • Chaussepied P (1989) Interaction between stretch of residues 633-642 (actin binding site) and nucleotide binding site on skeletal myosin subfragment 1 heavy chain. Biochemistry 28:9123-9128.
    • (1989) Biochemistry , vol.28 , pp. 9123-9128
    • Chaussepied, P.1
  • 16
    • 0022531397 scopus 로고
    • Modification of the actin interface of skeletal myosin subfragment-1 by treatment with dibromobimane
    • Mornet D, Ue K, Chaussepied P, Morales MF (1986) Modification of the actin interface of skeletal myosin subfragment-1 by treatment with dibromobimane. Eur J Biochem 159:555-561.
    • (1986) Eur J Biochem , vol.159 , pp. 555-561
    • Mornet, D.1    Ue, K.2    Chaussepied, P.3    Morales, M.F.4
  • 17
    • 0024352016 scopus 로고
    • Binding manner of actin to the lysine-rich sequence of myosin subfragment 1 in the presence and absence of ATP
    • Yamamoto K (1989) Binding manner of actin to the lysine-rich sequence of myosin subfragment 1 in the presence and absence of ATP. Biochemistry 28:5573-5577.
    • (1989) Biochemistry , vol.28 , pp. 5573-5577
    • Yamamoto, K.1
  • 18
    • 0027053493 scopus 로고
    • Synthetic peptide of the sequence 632-642 on myosin subfragment 1 inhibits actomyosin ATPase activity
    • Cheung P, Reisler E (1992) Synthetic peptide of the sequence 632-642 on myosin subfragment 1 inhibits actomyosin ATPase activity. Biochem Biophys Res Comm 189:1143-1149.
    • (1992) Biochem Biophys Res Comm , vol.189 , pp. 1143-1149
    • Cheung, P.1    Reisler, E.2
  • 19
    • 0028921163 scopus 로고
    • A single myosin head can be cross-linked to the N termini of two adjacent actin monomers
    • Bonafe N, Chaussepied P (1995) A single myosin head can be cross-linked to the N termini of two adjacent actin monomers. Biophys J 68(Suppl 4):35S- 43S.
    • (1995) Biophys J , vol.68 , Issue.SUPPL. 4
    • Bonafe, N.1    Chaussepied, P.2
  • 20
    • 0029118087 scopus 로고
    • Fluorescence polarization study of the rigor complexes formed at different degrees of saturation of actin filaments with myosin subfragment-1
    • Andreev OA, Takashi R, Borejdo J (1995) Fluorescence polarization study of the rigor complexes formed at different degrees of saturation of actin filaments with myosin subfragment-1. J Muscle Res Cell Motil 16:353-367.
    • (1995) J Muscle Res Cell Motil , vol.16 , pp. 353-367
    • Andreev, O.A.1    Takashi, R.2    Borejdo, J.3
  • 21
    • 0030683682 scopus 로고    scopus 로고
    • Interaction of the heavy and light chains of cardiac myosin subfragment-1 with F-actin
    • Andreev OA, Borejdo J (1997) Interaction of the heavy and light chains of cardiac myosin subfragment-1 with F-actin. Circ Res 81:688-693.
    • (1997) Circ Res , vol.81 , pp. 688-693
    • Andreev, O.A.1    Borejdo, J.2
  • 22
    • 0028075752 scopus 로고
    • How molecular motors work
    • Spudich JA (1994) How molecular motors work. Nature 372:515-518.
    • (1994) Nature , vol.372 , pp. 515-518
    • Spudich, J.A.1
  • 23
    • 0033583079 scopus 로고    scopus 로고
    • Specialized conservation of surface loops of myosin: Evidence that loops are involved in determining functional characteristics
    • Goodson HV, Warrick HM, Spudich JA (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
  • 24
    • 0028354078 scopus 로고
    • Enzymatic activities correlate with chimaeric substitutions at the actin-binding face of myosin
    • Uyeda TQP, Ruppel KM, Spudich JA (1994) Enzymatic activities correlate with chimaeric substitutions at the actin-binding face of myosin. Nature 368:567-569.
    • (1994) Nature , vol.368 , pp. 567-569
    • Uyeda, T.Q.P.1    Ruppel, K.M.2    Spudich, J.A.3
  • 25
    • 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
    • TrybusKM
    • Joel PB, Sweeney HL, TrybusKM(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
  • 26
    • 0032485859 scopus 로고    scopus 로고
    • Modulation of actin affinity and actomyosin adenosine triphosphatase by charge changes in the myosin motor domain
    • Furch M, Geeves MA, Manstein DJ (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
  • 27
    • 0033575216 scopus 로고    scopus 로고
    • Disturbed communication between actin-and nucleotide-binding sites in a myosin II with truncated 50/20-kDa junction
    • Knetsch ML, Uyeda TQ, Manstein DJ (1999) Disturbed communication between actin-and nucleotide-binding sites in a myosin II with truncated 50/20-kDa junction. J Biol Chem 274:20133-20138.
    • (1999) J Biol Chem , vol.274 , pp. 20133-20138
    • Knetsch, M.L.1    Uyeda, T.Q.2    Manstein, D.J.3
  • 28
    • 1542267772 scopus 로고    scopus 로고
    • Functional role of loop 2 in myosin V
    • Yengo CM, Sweeney HL (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
  • 29
    • 34848896360 scopus 로고    scopus 로고
    • Engineering the processive run length of Myosin V
    • Hodges AR, Krementsova EB, Trybus KM (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
  • 30
    • 0025900542 scopus 로고
    • Quantized velocities at low myosin densities in an in vitro velocity assay
    • Uyeda TQ, Warrick HM, Kron SJ, Spudich JA (1991) Quantized velocities at low myosin densities in an in vitro velocity assay. Nature 352:307-311.
    • (1991) Nature , vol.352 , pp. 307-311
    • Uyeda, T.Q.1    Warrick, H.M.2    Kron, S.J.3    Spudich, J.A.4
  • 31
    • 0035793563 scopus 로고    scopus 로고
    • Two conserved lysines at the 50/20-kDa junction of myosin are necessary for triggering actin activation
    • Joel PB, Trybus KM, Sweeney HL (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
  • 32
    • 0020501746 scopus 로고
    • The limiting rate of the ATP-mediated dissociation of actin from rabbit skeletal muscle myosin subfragment 1
    • GeevesMA
    • Millar NC, GeevesMA(1983) The limiting rate of the ATP-mediated dissociation of actin from rabbit skeletal muscle myosin subfragment 1. FEBS Letters 160:141-148.
    • (1983) FEBS Letters , vol.160 , pp. 141-148
    • Millar, N.C.1
  • 33
    • 0010083875 scopus 로고
    • ADP dissociation from actomyosin subfragment 1 is sufficiently slow to limit the unloaded shortening velocity in vertebrate muscle
    • Siemankowski RF, Wiseman MO, White HD (1985) ADP dissociation from actomyosin subfragment 1 is sufficiently slow to limit the unloaded shortening velocity in vertebrate muscle. Proc Natl Acad Sci USA 82:658-662.
    • (1985) Proc Natl Acad Sci USA , vol.82 , pp. 658-662
    • Siemankowski, R.F.1    Wiseman, M.O.2    White, H.D.3
  • 34
    • 0032564352 scopus 로고    scopus 로고
    • Filament structure as an essential factor for regulation of Dictyostelium myosin by regulatory light chain phosphorylation
    • Liu X, et al. (1998) Filament structure as an essential factor for regulation of Dictyostelium myosin by regulatory light chain phosphorylation. Proc Natl Acad Sci USA 95:14124-14129.
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 14124-14129
    • Liu, X.1
  • 35
    • 0027226230 scopus 로고
    • Structure of the actin-myosin complex and its implications for muscle contraction
    • Rayment I, et al. (1993) Structure of the actin-myosin complex and its implications for muscle contraction. Science 261:58-65.
    • (1993) Science , vol.261 , pp. 58-65
    • Rayment, I.1
  • 36
    • 0027194702 scopus 로고
    • Three-dimensional structure of myosin subfragment-1: A molecular motor
    • Rayment I, et al. (1993) Three-dimensional structure of myosin subfragment-1: A molecular motor. Science 261:50-58.
    • (1993) Science , vol.261 , pp. 50-58
    • Rayment, I.1
  • 37
    • 0042733142 scopus 로고    scopus 로고
    • Requirement of domain-domain interaction for conformational change and functional ATP hydrolysis in myosin
    • Ito K, Uyeda TQ, Suzuki Y, Sutoh K, Yamamoto K (2003) Requirement of domain-domain interaction for conformational change and functional ATP hydrolysis in myosin. J Biol Chem 278:31049-31057.
    • (2003) J Biol Chem , vol.278 , pp. 31049-31057
    • Ito, K.1    Uyeda, T.Q.2    Suzuki, Y.3    Sutoh, K.4    Yamamoto, K.5
  • 38
    • 0028284391 scopus 로고
    • Role of highly conserved lysine 130 of myosin motor domain. In vivo and in vitro characterization of site specifically mutated myosin
    • Ruppel KM, Uyeda TQ, Spudich JA (1994) Role of highly conserved lysine 130 of myosin motor domain. In vivo and in vitro characterization of site specifically mutated myosin. J Biol Chem 269:18773-18780.
    • (1994) J Biol Chem , vol.269 , pp. 18773-18780
    • Ruppel, K.M.1    Uyeda, T.Q.2    Spudich, J.A.3
  • 39
    • 0029913506 scopus 로고    scopus 로고
    • Myosin light chain kinase (MLCK) gene disruption in Dictyostelium: A role for MLCK-A in cytokinesis and evidence for multiple MLCKs
    • Smith JL, Silveira LA, Spudich JA (1996) Myosin light chain kinase (MLCK) gene disruption in Dictyostelium: A role for MLCK-A in cytokinesis and evidence for multiple MLCKs. Proc Natl Acad Sci USA 93:12321-12326.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 12321-12326
    • Smith, J.L.1    Silveira, L.A.2    Spudich, J.A.3


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