ライフサイエンスコーパス: DnaB helicase

1 be on the correct side of the helix to load DnaB helicase.

2 nable to block T7 RNA polymerase and E. coli DnaB helicase.

3 mobilized when each forms a complex with the DnaB helicase.

4 winding the DNA and promoting the binding of DnaB helicase.

5 the possible domain that interacts with the DnaB helicase.

6 d DNA (ssDNA) by the DnaB x DnaC complex and DnaB helicase.

7 gomeric structure, which is required to load DnaB helicase.

8 is similar to the intrinsic affinity of the DnaB helicase.

9 structure is insufficient by itself to load DnaB helicase.

10 is located on the large 33 kDa domain of the DnaB helicase.

11 y suppressing unproductive ATP hydrolysis by DnaB helicase.

12 atly stimulated through its interaction with DnaB helicase.

13 DnaB helicase accelerated the rate of primer syntheisis,

14 lts for a mechanistic model of the hexameric DnaB helicase action is discussed.

15 nd opening appeared normal but the levels of DnaB helicase activity were substantially reduced.

16 y further evaluation in a specific assay for DnaB helicase activity.

17 In the presence of DnaB helicase, all trinucleotides could serve as the pri

18 how that the analogous Escherichia coli (Ec) DnaB helicase also interacts specifically with the exclu

19 Besides stimulating primase activity, DnaB helicase also prevented primase from synthesizing R

20 f crossing over were increased by defects in DnaB helicase and by oxidative damage, showing that dama

21 l protein system, composed solely of E. coli DnaB helicase and DNA polymerase III holoenzyme.

22 following inactivation of a thermosensitive DnaB helicase and found that they are distinct from thos

23 II) and polymerase IV (Pol IV) function with DnaB helicase and regulate its rate of unwinding, slowin

24 rrested Escherichia coli DNA replication and DnaB helicase and T7 RNA polymerase in vitro in both ori

25 in Escherichia coli requires the replicative DnaB helicase and the DNA primase, the DnaG gene product

26 The complex between the DnaB helicase and the DnaG primase unwinds duplex DNA at

27 ommon to known replicative helicases such as DnaB helicase and the SV40 T-antigen.

28 gruencies between the CMG and both bacterial DnaB helicases and the AAA+ motor of the eukaryotic prot

29 interaction between wild type pi with DnaA, DnaB helicase, and DnaG primase on one hand and between

30 priming reaction by employing DnaG primase, DnaB helicase, and ribonucleotidetriphosphates (incorpor

31 plasmid DNA replication, as measured by the DnaB helicase- and gyrase-dependent formation of FI*, a

32 tion with initiator proteins, interestingly, DnaB helicase appears to have at least a limited number

33 the DnaC molecules, in the complex with the DnaB helicase, are induced by the binding to the helicas

34 In contrast, the DnaB helicase associates stably with the replication for

35 A step that follows is the binding of DnaB helicase at oriC so that it is properly positioned

36 complex then forms, involving the binding of DnaB helicase at oriC so that it is properly positioned

37 for self-oligomerization and the loading of DnaB helicase at oriC, we asked if these functions are s

38 An AAA+ ATPase, DnaC, delivers DnaB helicase at the E. coli chromosomal origin by a poo

39 that utilizes ATP hydrolysis to assemble the DnaB helicase at the origin.

40 uiting and positioning an active form of the DnaB helicase at the RK2 replication origin by a DnaA-in

41 aining 14, or less, nucleotide residues, the DnaB helicase becomes a completely distributive enzyme.

42 the ATP nonhydrolyzable analog AMP-PNP, the DnaB helicase binds polymer DNA with a site-size of 20 +

43 experiments provide direct evidence that the DnaB helicase binds the 5' arm of the fork in a single o

44 Moreover, unlike the E.coli DnaB helicase, both Pseudomonas helicases could be deliv

45 DnaB helicase bound ssDNA with a high affinity [Kd = (5.

46 P is necessary to engage the 3' arm with the DnaB helicase, but it does not change the initial distri

47 of enzymatic activities of Escherichia coli DnaB helicase by homologous and heterologous single-stra

48 The acceleration of the DnaB helicase can be observed in the absence of primase,

49 Although DnaB helicase can unwind a variety of DNA substrates pos

50 h protein components of the Escherichia coli DnaB helicase complex with the replication factor, the D

51 Site-specific Trp --> Cys mutants of DnaB helicase demonstrated that conformational change up

52 The conformational transition of the DnaB helicase-DNA complex, preceding the unwinding, is a

53 Anthrax DnaB helicase (DnaB(BA)) is a 453-amino-acid, 50-kDa pol

54 By contrast, Escherichia coli DnaB helicase (DnaB(EC)) did not stimulate DnaG(BA) and

55 nce of the results in the functioning of the DnaB helicase-DnaC protein complex is discussed.

56 nd NTP-binding sites of the Escherichia coli DnaB helicase engaged in the DnaB-DnaC complex and the m

57 quence motifs that are characteristic of the DnaB helicase family.

58 the ATP nonhydrolyzable analog, AMP-PNP, the DnaB helicase fully preserves its hexameric structure.

59 )uridine-5'-diphosphate) have shown that the DnaB helicase has a preference for purine nucleotides.

60 coli replication factor DnaC protein and the DnaB helicase have been performed using sedimentation ve

61 ggest that primarily a single subunit of the DnaB helicase hexamer is in contact with the DNA.

62 coefficient s20,w = 10.5 +/- 0.2 of the free DnaB helicase hexamer.

63 The kinetic step-size of the DnaB helicase, i.e. the number of the base-pairs unwound

64 In vitro, the sequence arrested DnaB helicase in both orientations, albeit more weakly t

65 mechanistic model of the functioning of the DnaB helicase in DNA replication is discussed.

66 Upon addition of DnaC and the DnaB helicase in the presence of ATPgammaS, helicase is

67 f Escherichia coli physically interacts with DnaB helicase in vivo.

68 vitro by SV40 T antigen and Escherichia coli dnaB helicases in an orientation-independent manner.

69 required for recruitment of the Pseudomonas DnaB helicases in the initiation of RK2 replication.

70 e mechanism of the nucleotide binding to the DnaB helicase indicates the lack of the existence of a k

71 The analysis of the DnaB helicase interactions with nonfluorescent, unmodifi

72 ese data suggest that the oligomerization of DnaB helicase involves at least two distinct protein-pro

73 DnaB helicase is a ring-shaped hexamer of 300 kDa that i

74 DnaB helicase is a ring-shaped hexamer that unwinds DNA

75 of the DNA polymerase III holoenzyme and the DnaB helicase is critical for coupling the replicase and

76 anism of the free energy transduction of the DnaB helicase is discussed.

77 of these results for the functioning of the DnaB helicase is discussed.

78 anism of the free energy transduction by the DnaB helicase is discussed.

79 onstrated that ssDNA binding activity of the DnaB helicase is necessary for directing the primase to

80 in the DNA polymerase III holoenzyme and the DnaB helicase is required for replication fork propagati

81 DnaB helicase is responsible for unwinding duplex DNA du

82 well as in loading DnaB onto the ssDNA than DnaB helicase itself.

83 he stimulation of open complex formation and DnaB helicase loading on oriV, even in the absence of th

84 other conserved residues leads to decreased DnaB helicase loading onto SSB-bound DNA.

85 vitro, for localized strand opening and for DnaB helicase mediated unwinding.

86 that the major conformational change of the DnaB helicase-nucleotide complex occurs in the formation

87 fication and is an intrinsic property of the DnaB helicase-nucleotide system.

88 f helicase A appears to have homology to the DnaB helicase of E. coli (approximately 25%).

89 DnaB helicase of E. coli unwinds duplex DNA in the repli

90 es of two other hexameric DNA helicases: the DnaB helicase of Escherichia coli and the T-antigen heli

91 diated by the C-terminal domain gamma of the DnaB helicase of Escherichia coli.

92 of three distinct structural domains of the DnaB helicase of Escherichia coli: domain alpha, amino a

93 at had lost the ability to bind and load the DnaB helicase of P. aeruginosa or Pseudomonas putida ont

94 s predominantly unaffected in the absence of DnaB helicase on short ssDNA templates, whereas in conju

95 The effect of DnaB helicase on the initiation specificity of primase w

96 cation restart, reloading of the replicative DnaB helicase onto an abandoned replication fork.

97 DnaC loads the DnaB helicase onto DNA as a prelude for primosome assemb

98 itment and correct spatial deposition of the DnaB helicase onto origins.

99 s capacity to mediate efficient reloading of DnaB helicase onto rolling circle replication products,

100 ate the transfer of one or more molecules of DnaB helicase onto the chromosome; the transferred DnaB,

101 In this report, we determined that one DnaB helicase or one DnaB-DnaC complex is bound to a sin

102 The specificity of DnaB helicase places it on the lagging strand template w

103 nonhydrolyzable analog, AMP-PNP, the E. coli DnaB helicase preferentially binds to the 5' arm of the

104 In the absence of DnaB helicase, primase preferentially primed the d(CTG)

105 m excludes conformational transitions of the DnaB helicase prior to ATP binding.

106 a helicase substrate, the ATPase activity of DnaB helicase remained uninhibited.

107 Secondary structural predictions of 4A' and DnaB helicases resemble the known structures of RecA and

108 acteriophage T7 gene 4 protein and bacterial DnaB helicase, respectively.

109 Binding of oligonucleotides to DnaB helicase resulted in a significant attenuation of t

110 e lagging strand, such as primase binding to DnaB helicase, RNA synthesis, and SS B antigen (SSB) dis

111 It was shown that DnaB helicase stabilized the open or single-stranded con

112 DnaB helicase stimulated the second-order RNA primer syn

113 In vitro, DnaB helicase stimulates primase to synthesize primers o

114 tifiable structural/conformational states of DnaB helicase that are likely important in the helicase

115 In the presence of DnaB helicase, the initiation preference was not only al

116 In the absence of DnaB helicase, the majority of primers synthesized by pr

117 ssDNA templates, whereas in conjunction with DnaB helicase, the specificity was altered and this alte

118 the replication terminator protein (RTP) and DnaB helicase, there has been continuing debate in the l

119 This template length is the same as the DnaB helicase thermodynamic binding site size.

120 necessary to determine the optimal amount of DnaB helicase to achieve this stimulation because helica

121 eplicase on the beta-clamp and function with DnaB helicase to form alternative replisomes, even befor

122 erial DNA replication, DnaA protein recruits DnaB helicase to the chromosomal origin, oriC, leading t

123 ng it to the binding of the Escherichia coli DnaB helicase to unmodified, nonfluorescent single-stran

124 epsilonA)19, s20,w = 12.4, suggests that the DnaB helicase undergoes further conformational changes u

125 The ring-shaped hexameric DnaB helicase unwinds duplex DNA at the replication fork

126 Thus, the DnaB helicase unzips the dsDNA in a reverse process to t

127 gging strand polymerases are tethered to the DnaB helicase via dimeric tau.

128 Binding of ssDNA to DnaB helicase was significantly modulated by nucleotide

129 of long-range allosteric interactions in the DnaB helicase which encompass the entire DnaB hexamer.

130 been performed with the fluorescein-modified DnaB helicase, which allows an exclusive monitoring of t

131 Association of the DnaB helicase with nucleotide cofactors is characterized

132 Association of the DnaB helicase with the 20-mer is characterized by three

133 ted by TrfA result in a repositioning of the DnaB helicase within the open origin region and an activ