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 sslinkers such as alpha-actinin, fascin, and heavy meromyosin alter the mechanical response independe

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

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

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

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

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

22 cleotide release by an equal factor for both heavy meromyosin and subfragment 1, thus only indirectly

23 Using recombinant beta-cardiac heavy meromyosin and subfragment 1, which cannot form th

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

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

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

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

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

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

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

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

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

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

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

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

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

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

38 d unphosphorylated recombinant nonmuscle IIA heavy meromyosin constructs.

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

56 not seen using shorter myosin subfragments, heavy meromyosin (HMM) and myosin subfragment 1 (S1).

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

72 filaments are propelled by surface-adsorbed heavy meromyosin (HMM) motor fragments.

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

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

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

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

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

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

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

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

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

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

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

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

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

86 ting head motif (IHM) where the two heads of heavy meromyosin (HMM), or myosin, fold back onto each o

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

102 The stabilizing effect of heavy meromyosin is cooperative.

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

120 Proteolytic gizzard heavy meromyosin regulatory light chains were partially

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

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

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

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

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

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

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

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

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

130 Heavy meromyosin stabilizes the formin-nucleated actin f

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

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

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

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

135 nduce novel conformations in human B-cardiac heavy meromyosin that diverge significantly from the hyp

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

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

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

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

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

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

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

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

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

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