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Myosins / by James R. Sellers. — 2nd ed. — Oxford ;New York : Oxford University Press, 1999.—(58.174211/S467/2nd ed.)

Contents

    Contents
    
    Acknowledgements xii
    Abbreviations xiii
    Introduction 1
     Definition of myosin 1
     Classification of myosins 1
     Domain structure of myosins 9
     Myosin II 14
     Subclassification of myosin II 14
     Proteolytic fragmentation of myosin II 20
     Myosin I 20
     Myosin III 23
     Myosin V 23
     Myosin VI 27
     Myosin VII 28
     Myosin IX 29
     Myosin XV 29
     Other myosin classes 29
     Myosin sequence analysis 31
     Gene localization 31
     Alternative splicing of myosin heavy chain genes 32
     Purification of myosins 35
    Myosin structure 37
     The crystal structure of subfragment 1 37
     Structure of the neck region of chicken skeletal muscle S-1 40
     Scallop regulatory domain 41
     Comparisons to other MgATPases 42
     Structure of Dictyostelium motor domains with bound nucleotides 42
     Low resolution structure of brush border myosin I from two-dimensional crystals 48
     Model for the binding of myosin to actin 48
     Model for the powerstroke 52
     Sequence analysis of the myosin rod 52
     Myosin II filament structure 54
    Functional properties of myosin 57
     MgATPase activity 57
     Actin-activated MgATPase activity 58
     Mechanical experiments on muscle fibres 60
     Structural model of contraction 61
     The nonphysiological high salt ATPase activity of myosin 61
     Hydrolysis of other nucleotide triphosphates 62
     Actin binding properties 63
     Effect of nucleotide on actin binding 63
     In vitro motility assays 63
     In vitro mechanical studies 63
     Functional studies of myosin in cells 67
     Divalent cation binding 68
    Covalent derivatization of myosin 70
     Modification of Cys-707 and Cys-697 70
     Cross-linking experiments 70
     Photoaffinity nucleotide analogs 73
     Modification of light chains 74
    Regulation 75
     Phosphorylation of vertebrate smooth and nonmuscle myosins 75
     Structural basis for phosphorylation-dependent regulation 75
     Phosphorylation-dependent regulation in some invertebrate Myosins 82
     Phosphorylation does not regulate vertebrate skeletal muscle Myosin 82
     Phosphorylation-dependent regulation in lower eukaryotic myosin II 83
     Regulation of lower eukaryotic myosin I 84
     Regulation of brush border myosin I 84
     Regulation of myosin V 85
     Regulation of molluscan myosin II by calcium binding 85
    Myosin binding proteins 87
    Mutations in myosin 91
     Mutations in human/3-cardiac myosin heavy chain 91
    Mutations in the human myosin VA heavy chain gene are linked to Griscelli disease 97
    Mutations in the human myosin heavy chains are linked to congenital deafness 99
    Mouse mutant models 99
    Mutations in the myosins of Dictyostelium discoideum 100
    Mutations in yeast 105
    Mutations in Drosophila 105
    Mutations in C. elegans 105
    Expression of myosins 112
     Expression of mutant light chains in bacteria and exchange into myosin 112
     Expression of active recombinant myosins in heterologous systems 112
    Concluding remarks 113
    Bibliography 115
    Books on myosin 115
    Reviews (references 1-136) 115
    Structure of myosin (references 137-476) 119
    Sequence analysis of myosin (references 47%603) 132
    Interaction with actin (references 60zI~765) 137
    ATPase activity of myosin (references 766-908) 143
    Kinetics of actomyosin interaction (references 909-1045) 148
    Nucleotide binding (references 1046-1137) 153
    Mechanical studies of myosin in muscles and cells (references 1138--1287) 157
    In vitro motility of myosin (references 1288-1403) 163
    Myosin filament assembly and structure (references 1404-1547) 167
    Phosphorylation of myosin (references 1548-1706) 172
    Cation binding to myosin (references 1707-1736) 178
    Myosin light chains (references 173%1931) 179
    Regulation of myosin (references 1932-2018) 187
    Myosin expression, localization, and isoform diversity (references 2019-2193) 190
    Covalent derivatization of myosin (references 2194--2284) 197
    Proteolysis of myosin (references 2285-2358) 200
    Myosin binding proteins (references 235%2494) 203
    Myosin mutations (references 2495-2646) 208
    Unconventional myosins (references 2647 2836) 215
    Methods for analysis of myosin (references 2837-2931) 222
    Other references (references 293~2942) 225
    References added in proof (references 2942~2959) 226
    Sequence alignment 228
     Alignment of myosin motor domains 228
    List of figures
    Figure 1 Phylogenetic tree obtained from neighbour joining analysis of myosin motor domain protein sequences as performed by ClustalW. 2
    Figure 2 Schematic representation of the domain structure of various members of the myosin superfamily. 8
    Figure 3 Domain structure of myosin.9
    Figure 4 Crystal structure of chicken skeletal muscle S-1 depicted as a ribbon diagram.10
    Figure 5 The core of the backbone structure of the motor domain of chicken skeletal muscle myosin is well conserved. 11
    Figure 6 Phylogenetic analysis of regulatory light chains, essential lights, calmodulin, and the light chain for A canthamoeba myosin IC. 13
    Figure 7 Proteolytic cleavage of myosin. 19
    Figure 8 Three-dimensional structure of the scallop regulatory domain. 20
    Figure 9 Electron micrographs of rotary shadowed images of chicken myosin V and A canthamoeba myosin II. 25
    Figure10 Localization of myosin I and myosin 1I in dividing Dictyostelium cells. 31
    Figure 11 Alternative splicing in the head of smooth and nonmuscle myosin II. 33
    Figure 12 Sequence alignment of the motor domains from chicken fast skeletal muscle, chicken smooth muscle, scallop striated muscle, and Dictyostelium. 38
    Figure 13 Structural motifs around the phosphate moieties of myosin. 39
    Figure 14 Structure around the nucleotide-binding pocket of chicken fast skeletal muscle myosin. 41
    Figure 15 Structure around the reactive cysteines of chicken fast skeletal muscle myosin. 42
    Figure 16 Overlap of active site structural elements of myosin and kinesin 44
    Figure 17 Structure of Dictyostelium motor domain with bound MgADP'BeFx. 45
    Figure 18 Structures of Dictyostelium motor domains with bound MgADP-BeFx and MgADP'VO4 showing the movement of the carboxyl-terminal domain. 46
    Figure 19 Schematic showing the coordination of MgADP'VO4 by the Dictyostelium motor
     domain crystal. 47
    Figure 20 Three-dimensional reconstruction of a decorated actin filament 49
    Figure 21 Model of acto-S-1 interaction 50
    Figure 22 Proposed actin binding regions on myosin 51
    Figure 23 ADP induced movement of the neck of chicken smooth musc]e myosin S-1 bound to actin. 53
    Figure 24 Heptad wheels showing the sequence motif of a coiled-coil c~-helix 54
    Figure 25 Two types of thick filaments. 54
    Figure 26 Effect of activation on the thick filament structure of scallop thick filaments. 55
    Figure 27 Three-dimensional structure of the scallop specific Ca2 + -binding site 69
    Figure 28 Alignment of the amino-terminal amino acid sequence of a number of regulatory light chains. 78
    Figure 29 Smooth muscle and nonmuscle myosin can exist in two conformations 79
    Figure 30 Human/3-cardiac myosin heavy chain mutations found near the actin-binding regions that cause hypertrophic cardiomyopathy. 94
    Figure 31 Human/3-cardiac myosin heavy chain mutations found near the ATP-binding pocket that cause hypertrophic cardiomyopathy. 95
    Figure 32 Human/3-cardiac myosin heavy chain mutations found near the SH1/SH2 helix that cause hypertrophic cardiomyopathy. 96
    Figure 33 Human fl-cardiac myosin heavy chain mutations found near the converter domain that cause hypertrophic cardiomyopathy. 97
    Figure 34 Human light chain mutations that cause hypertrophic cardiomyopathy 98
    List of tables
     Table 1 Myosin sequence data 3
     Table 2 Past and present light chain names 14
     Table 3 Summary of myosin biochemical data 15
     Table 4 Phylogenetic distributions of myosins 21
     Table 5 Location of some myosin heavy chain genes 24
     Table 6 In vitro motility rates of various myosins 26
     Table 7 Steady2state kinetic parameters of myosin sub fragments 27
    Table 8 Methodologies 36
    Table 9 Photoaffinity labelling of myosin with nucleotide Analogs 40
    Table 10 Cross-linking studies on myosin 43
    Table 11 Areas of contact between actin and myosin 50
    Table 12 Kinetic rate constants of the MgATPase activity of various myosms 59
    Table 13 Kinetic rate constants of acto-subfragment 1 59
    Table 14 Covalent derivation of myosin 71
    Table 15 Phosphorylation of myosin 76
    Table 16 Myosin-binding proteins 87
    Table 17 Human myosin mutations associated with diseases 92
    Table 18 Dictyostelium myosin lI heavy chain mutations 101
    Table 19 Other myosin mutations 106