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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
