ライフサイエンスコーパス: heavy meromyosin

1 dephosphorylated but not thiophosphorylated heavy meromyosin.

2 C) in the regulatory domain of smooth muscle heavy meromyosin.

3 ng of the intact RLC bound to the two-headed heavy meromyosin.

4 position 23 of the regulatory light chain of heavy meromyosin.

5 exed (folded) transition in unphosphorylated heavy meromyosin.

6 on microscopy of two-dimensional crystals of heavy meromyosin.

7 d in unphosphorylated but not phosphorylated heavy meromyosin.

8 ted that a dimer of Myo5c-HMM (double-headed heavy meromyosin 5c) has a 6-fold lower Km for actin fil

9 experiments comparing the subfragment-1 with heavy meromyosin (a two-headed subfragment).

10 Myosin 5 heavy meromyosin, a constitutively active fragment lacki

11 Smooth muscle heavy meromyosin, a double-headed proteolytic fragment o

12 orylated regulatory light chain N termini in heavy meromyosin, a double-headed subfragment with an in

13 The apparent affinity of acto-heavy meromyosin (acto-HMM) for MgATP was reduced by the

14 rates of MgATP-induced dissociation of acto-heavy meromyosin (acto-HMM) were virtually identical for

15 showed that one head of the unphosphorylated heavy meromyosin-ADP complex bound to actin and that the

16 For unphosphorylated and phosphorylated heavy meromyosin and for S1, approximately 50% of the mo

17 aments and the smaller force produced by the heavy meromyosin and I341A actin system.

18 f the maximal MgATPase activity of wild type heavy meromyosin and moves actin filaments at half the w

19 filamentous forms of Acanthamoeba myosin II, heavy meromyosin and myosin subfragment 1, have actin-ac

20 recombinant calponin shows interaction with heavy meromyosin and myosin subfragment 2 but not subfra

21 e first bond to form between actin and rigor heavy meromyosin and the load-dependent durations of tho

22 despite the qualitatively similar effects of heavy meromyosin and tropomyosin on the conformational d

23 died: monomers, the short-tailed subfragment heavy meromyosin, and SMM filaments.

24 Recombinant heavy meromyosin- and subfragment-1 (S1)-like constructs

25 We have shown that unphosphorylated heavy meromyosin appears to adopt a special state in the

26 presence of ADP based upon analysis of actin-heavy meromyosin association rate constants.

27 M2B, and NM2C and monomeric, non-filamentous heavy meromyosin bind to liposomes containing one or mor

28 ither thiophosphorylated or unphosphorylated heavy meromyosin bind very strongly to actin (K(d) < 10

29 olytic cleavage of the head-tail junction of heavy meromyosin by papain and chymotrypsin, suggesting

30 Here, smooth muscle heavy meromyosin C-loop chimeras were constructed with s

31 Nucleotide binding to unphosphorylated heavy meromyosin caused a decrease in exposure and an in

32 he in vitro sliding of thin filaments over a heavy meromyosin-coated surface.

33 ADP-induced dissociation of the pyrene-actin-heavy meromyosin complex, and (iii) amplitudes of the as

34 For the actin-heavy meromyosin complex, cross-links were formed in bot

35 d unphosphorylated recombinant nonmuscle IIA heavy meromyosin constructs.

36 x-ray and neutron scattering measurements of heavy meromyosin containing all three light chains (LC(1

37 s populations of heterodimeric smooth muscle heavy meromyosins containing heads with different proper

38 il junction, we prepared five well regulated heavy meromyosins containing single-cysteine mutants of

39 Expressed chimeric smooth muscle heavy meromyosins containing skeletal muscle myosin heav

40 nhibits the motilities of both actins at low heavy meromyosin densities but potentiates only the moti

41 nly the motility of the mutant actin at high heavy meromyosin densities.

42 pCa(50) decreased by 0.12-0.18 when either heavy meromyosin density was reduced to approximately 60

43 g speed but reduced the isometric force that heavy meromyosin exerted on regulated thin filaments.

44 ng that a greater percentage of NEM-modified heavy meromyosin (external load) was required for arrest

45 this, a fluorescently labeled double-headed heavy meromyosin form showed no processive movements alo

46 A recombinant myosin V heavy meromyosin fragment that is missing the distal por

47 inetic analysis, one-head thiophosphorylated heavy meromyosin had a similar K(m) value for actin but

48 This heavy meromyosin has only 4% of the maximal MgATPase act

49 sity profiles were best fit by models of the heavy meromyosin head-tail junction in which the angular

50 orescence methods that monitor the number of heavy meromyosin heads that bind to pyrene-actin: (i) am

51 ession of noninserted and inserted NMHC II-C heavy meromyosin (HMM II-C/HMM II-C1) resulted in signif

52 Since the junction between the heavy meromyosin (HMM) and light meromyosin (LMM) region

53 The effect of H(2)O(2) on smooth muscle heavy meromyosin (HMM) and subfragment 1 (S1) was examin

54 We have used two myosin fragments, heavy meromyosin (HMM) and Subfragment 1 (S1), to look a

55 for nucleotide complexes of skeletal muscle heavy meromyosin (HMM) and subfragment 1 (S1).

56 We find that wild-type and zippered heavy meromyosin (HMM) are able to bind by both heads to

57 on actin filaments when they were placed on heavy meromyosin (HMM) attached to a glass surface.

58 ted thin filaments) when they were placed on heavy meromyosin (HMM) attached to a glass surface.

59 cle myosin for that of gizzard smooth muscle heavy meromyosin (HMM) causes activation of the dephosph

60 ze the mechanical properties of an expressed heavy meromyosin (HMM) construct with only one of its RL

61 affinity chromatography were used to isolate heavy meromyosin (HMM) containing one phosphorylated and

62 east actin required higher concentrations of heavy meromyosin (HMM) for its sliding than did the rabb

63 ecreased nonlinearly with reduced density of heavy meromyosin (HMM) for regulated (and unregulated) F

64 mutated and wild-type baculovirus-expressed heavy meromyosin (HMM) II-B and II-C.

65 scle myosin IIs, baculovirus-expressed mouse heavy meromyosin (HMM) II-C2 demonstrates no requirement

66 d (i) the motor function of SH1 spin-labeled heavy meromyosin (HMM) in the in vitro motility assays a

67 d possible interactions between the heads of heavy meromyosin (HMM) in the presence and absence of ca

68 nctions as a mechanical lever, smooth muscle heavy meromyosin (HMM) mutants were expressed with short

69 Measurements of actin-activated heavy meromyosin (HMM) NTPase, the rates of NTP binding

70 rylated and thiophosphorylated smooth muscle heavy meromyosin (HMM) on positively charged lipid monol

71 duced into the assay and at low densities of heavy meromyosin (HMM) on the cover slip.

72 Scallop heavy meromyosin (HMM) preparation obtained by a new imp

73 Steady-state hydrolytic activity of cardiac heavy meromyosin (HMM) showed that PTU treatment resulte

74 ac myosin and rabbit skeletal myosin and its heavy meromyosin (HMM) subfragment.

75 terminal domains of MyBP-C on the ability of heavy meromyosin (HMM) to support movement of actin fila

76 er stroke sizes of single- and double-headed heavy meromyosin (HMM) were each ~6 nm.

77 Tryptic digestions of myosin, which produced heavy meromyosin (HMM) with different percentages of mol

78 y between heads, we examined the kinetics of heavy meromyosin (HMM) with one thiophosphorylated head.

79 , we expressed a smooth muscle heterodimeric heavy meromyosin (HMM) with one wild-type head, and the

80 f ATP, MBP bound to dephosphorylated myosin, heavy meromyosin (HMM), and subfragment 1.

81 fragments of human cardiac myosin, including heavy meromyosin (HMM), the S1 subfragment, and two ligh

82 ddress this question, we produced asymmetric heavy meromyosin (HMM), which is composed of a wild-type

83 e engineered and characterized smooth muscle heavy meromyosin (HMM), which is composed of one entire

84 Heavy meromyosin (HMM), which lacks two-thirds of the ta

85 ents were visualized gliding over a skeletal heavy meromyosin (HMM)-coated surface.

86 MgATP] >/= 0.25 mM, the flexural rigidity of heavy meromyosin (HMM)-propelled actin filaments is simi

87 d the density of the adsorbed motor protein (heavy meromyosin, HMM) using quartz crystal microbalance

88 mutagenesis and baculovirus expression of a heavy meromyosin- (HMM-) like fragment of human nonmuscl

89 One of the expressed heavy meromyosins (HMMexp) consists of two 150-kDa myosi

90 ed three recombinant constructs of nonmuscle heavy meromyosin IIB containing 1) two complete heads, 2

91 filament movement over a surface coated with heavy meromyosin in in vitro motility assays.

92 atory domains of double-headed smooth muscle heavy meromyosin, including the N terminus of the regula

93 build a single-species homology model of two heavy meromyosin interacting-heads motifs (IHMs).

94 microscopy was used to determine whether the heavy meromyosin IQ molecules were capable of processive

95 Actin-activated MgATPase of smooth muscle heavy meromyosin is activated by thiophosphorylation of

96 The stabilizing effect of heavy meromyosin is cooperative.

97 When the subfragment 2 domain of heavy meromyosin is oriented as it would be in an actomy

98 low actin velocity generated by minus-insert heavy meromyosin is significantly influenced, but not li

99 observed for the Q15C mutant on a truncated heavy meromyosin lacking both catalytic domains.

100 ly forms in 10 S and not in unphosphorylated heavy meromyosin (lacking the light meromyosin), suggest

101 t this hypothesis we have expressed myosin V heavy meromyosin-like fragments containing 6IQ motifs, a

102 ility assay to characterize the mechanics of heavy meromyosin-like fragments of myosin V (M5(HMM)) ex

103 These two mutations were engineered into a heavy meromyosin-like recombinant fragment of nonmuscle

104 Double-headed (heavy meromyosin-like) and single-headed (subfragment 1-

105 MHC rod, located in the C-terminal third of heavy meromyosin, may form a less stable coiled-coil tha

106 the mechanochemistry of single smooth muscle heavy meromyosin molecules lacking a seven-amino acid in

107 Comparison with studies of single heavy meromyosin molecules suggests that an increased mo

108 for regulation, we engineered smooth muscle heavy meromyosin molecules that contained one complete h

109 m Ile/Leu-25 to Lys-53 bound both myosin and heavy meromyosin more strongly and was capable of displa

110 says reveal that at nanomolar calcium levels heavy meromyosin moves robustly on actin filaments where

111 atory light chain of each head of a skeletal heavy meromyosin, near the head-rod junction (positions

112 This behavior was found for native regulated heavy meromyosin prepared by proteolytic digestion of ch

113 hyperbolic [MgATP]-velocity relationship of heavy-meromyosin-propelled actin filaments in the in vit

114 Proteolytic gizzard heavy meromyosin regulatory light chains were partially

115 , TnT-(1-153) increased the concentration of heavy meromyosin required to support in vitro sliding of

116 n vitro motility assays with rabbit skeletal heavy meromyosin (rsHMM) or porcine cardiac myosin (pcMy

117 For SMM and heavy meromyosin, several sites showed two heterogeneous

118 SH2-labeled heavy meromyosin (SH2-HMM), similar to SH1-labeled HMM (

119 th actin over a surface coated with skeletal heavy meromyosin (sHMM) or full-length beta-cardiac myos

120 e energy transfer measurements revealed that heavy meromyosin, similarly to tropomyosin, restores the

121 Smooth muscle myosin and smooth muscle heavy meromyosin (smHMM) are activated by regulatory lig

122 ATPase activity of smooth muscle myosin and heavy meromyosin (smHMM) is regulated by phosphorylation

123 variable portion of loop 2 of smooth muscle heavy meromyosin (smHMM).

124 Heavy meromyosin stabilizes the formin-nucleated actin f

125 the laser trap, applied load slows myosin V heavy meromyosin stepping and increases the probability

126 The folding pathway of the heavy meromyosin subfragment (HMM) of a skeletal muscle

127 ed in dephosphorylated or thiophosphorylated heavy meromyosin, suggesting positions outside the regio

128 hosphorylated inactive form of smooth muscle heavy meromyosin suitable for structural studies by elec

129 of both filamentous NM2 and non-filamentous heavy meromyosin; the addition of excess unbound RLC, bu

130 alloidin-labeled skeletal actin and skeletal heavy meromyosin to propel the filaments.

131 of loop 2 specifically blocks the ability of heavy meromyosin to undergo a weak to strong binding tra

132 LC, exchanged each mutant onto smooth muscle heavy meromyosin, verified normal regulatory function, a

133 ads, showed that one-head thiophosphorylated heavy meromyosin was 46-120 times more active than unpho

134 ylation upon the actin binding properties of heavy meromyosin was investigated using three fluorescen

135 ctivity towards phosphorylated smooth muscle heavy meromyosin was proportional to the amount of PP1cd

136 the effects of nucleotide on phosphorylated heavy meromyosin were the opposite.

137 , and (iii) amplitudes of the association of heavy meromyosin with pyrene-actin.

138 owing that two-head binding is a property of heavy meromyosin with uncleaved heavy chains.