ライフサイエンスコーパス: primosome

1 e-primase complex and in the three component primosome.

2 of PriB during assembly of the phiX174-type primosome.

3 riate DNA templates to reconstitute a stable primosome.

4 rimosome and DnaG generates the five-protein primosome.

5 in the replisome: the DNA polymerase and the primosome.

6 a-primase (pol-prim), constituting the viral primosome.

7 y pol-prim, constituting a relatively simple primosome.

8 The human primosome, a 340-kilodalton complex of primase and DNA p

9 tion is believed to require the phiX174-type primosome, a mobile priming apparatus assembled without

10 ation model, the p68 subunit is required for primosome activity and binds directly to the hexameric v

11 ution in Tag disrupted both p68N-binding and primosome activity but did not affect docking with other

12 ndicating that Tag ATPase is dispensable for primosome activity in vitro.

13 SV40 primosome activity of corresponding pol-prim mutants dec

14 To assess this possibility, we examined the primosome activity of Tag with a single residue substitu

15 it did not reduce pol-prim docking on Tag or primosome activity on single-stranded DNA, indicating th

16 nted for how this interaction regulates SV40 primosome activity, and the implications of our findings

17 dynamic multiprotein assembly that displays primosome activity.

18 l link between T antigen-p68 interaction and primosome activity.

19 The leading strand polymerase and the primosome also associate, such that gp59 mediates the co

20 n assembled on intact phiX174 phage DNA, the primosome also contains PriC.

21 and duplex DNA unwinding activity of the T4 primosome and are consistent with more indirect equilibr

22 The results demonstrate a role for the primosome and Rep helicase in overcoming replication for

23 number of gp61 contact positions within the primosome and reveal interactions that may be important

24 ta have been reported: the former within the primosome and separately with CTD and the latter with th

25 investigate the subunit stoichiometry of the primosome and the assembly pathway required to form func

26 l structures of two key complexes, the human primosome and the C-terminal domain of the primase large

27 or replication fork formation by the restart primosome and the DNA polymerase III holoenzyme.

28 The primosome and the lagging strand polymerase remain activ

29 ated actions of two catalytic domains in the primosome and ultimately could impact the design of anti

30 ting the primase (gp61) to form a functional primosome and, subsequently, a fully active replisome.

31 al repair system and the replication restart primosome are also prominent, as are mutations in genes

32 oading and the composition of the eukaryotic primosome are poorly understood.

33 Primosomes are multienzyme replication machines that con

34 that both pol II and the origin-independent primosome-assembling function of PriA are essential for

35 D and RecA proteins, which requires only the primosome assembly activity of PriA to load DnaB at D lo

36 ull mutations, has led to proposals that the primosome assembly activity of PriA was required to load

37 the DnaB helicase onto DNA as a prelude for primosome assembly and DNA replication.

38 work for the elucidation of further steps in primosome assembly and for quantitative analyses of othe

39 f the formation of intermediate complexes in primosome assembly and the effect of PriB on PriA bindin

40 lysis to isolate and identify the pathway of primosome assembly at a primosome assembly site (PAS) on

41 synthesis and is essential for helicase and primosome assembly during T4 recombination-dependent DNA

42 Concerted helicase and primosome assembly functions would allow PriA to act as

43 These results suggest that PriA-dependent primosome assembly is crucial for both homologous recomb

44 ites for PriA and DnaT, suggesting a dynamic primosome assembly process in which single-stranded DNA

45 Primosome assembly protein PriA functions in the assembl

46 Escherichia coli PriA is a primosome assembly protein with 3' to 5' helicase activi

47 PriA and other primosome assembly proteins of Escherichia coli recruit

48 ion of DNA synthesis only in the presence of primosome assembly proteins PriA, DnaT, DnaB and DnaC.

49 Primosome assembly proteins PriA, PriB, DnaT, and the Dn

50 In Escherichia coli, the primosome assembly proteins, PriA, PriB, PriC, DnaT, Dna

51 lving PriA and PriB proteins and the minimal primosome assembly site (PAS) of phage varphiX174, has b

52 ntify the pathway of primosome assembly at a primosome assembly site (PAS) on a 300-nucleotide-long s

53 otide-long single strand of DNA containing a primosome assembly site.

54 t form a PriA-PriB complex on DNA carrying a primosome assembly site.

55 lts for the enzyme activities in recognizing primosome assembly sites or the ssDNA gaps is discussed.

56 Although no pre-existing primosome assembly sites that bind PriA were found withi

57 the invading strand, effectively preventing primosome assembly there.

58 Instead, gp59 directs primosome assembly to the displaced strand of the D loop

59 onsible for loading DnaB onto the DNA during primosome assembly, in the PriA- and DnaA-mediated casca

60 uantitative analysis of the initial steps in primosome assembly, involving PriA and PriB proteins and

61 Thus, during primosome assembly, PriB facilitates complex formation b

62 helicase and primase activities as part of a primosome assembly.

63 blocking leading-strand synthesis during the primosome assembly.

64 PriA has ATPase, helicase, translocase, and primosome-assembly activities.

65 We conclude that priA's primosome-assembly activity is essential for DNA repair

66 (K230R), a mutant allele retaining only the primosome-assembly activity of priA+, restores both UVR

67 interact to form the bacteriophage T4-coded primosome at the DNA replication fork.

68 This protein is a major component of the primosome, being essential for coordinated leading and l

69 nce quenching results, are consistent with a primosome-binding model in which the lagging DNA strand

70 able of catalyzing the assembly of an active primosome but which is missing the n'-pas-dependent ATPa

71 e molecular mass or helicase activity of the primosome, but significantly inhibits its primase activi

72 lts suggest that both the holoenzyme and the primosome can be simultaneously assembled onto the minic

73 nit of gp61 primase stabilized the resulting primosome complex at the fork and resulted in fully acti

74 Identification of this archaeal primosome complex broadly impacts evolutionary relations

75 Binding of gp43 to the primosome complex causes displacement of gp32 from the g

76 ormation of a unique but homologous archaeal primosome complex is possible but may require other comp

77 t stoichiometry, and assembly pathway of the primosome complex of the bacteriophage T4 DNA replicatio

78 nce of primase, but forms a much more stable primosome complex that expresses full and functional hel

79 teracts with the helicase (gp41) to form the primosome complex, an interaction that greatly stimulate

80 ase is assembled within the complete ternary primosome complex.

81 interaction with other proteins forming the primosome complex.

82 displacement of gp32 from the gp59.gp61.gp41 primosome complex.

83 ty of the bacteriophage T4 helicase-primase (primosome) complex.

84 ding activities are coupled within bacterial primosome complexes to initiate synthesis on the lagging

85 rminal tier of SsoMCM analogous to bacterial primosome complexes.

86 h is important for the reconstitution of the primosome component of the T4 DNA replication fork, appe

87 function of the processive helicase-primase (primosome) component of the bacteriophage T4-coded DNA r

88 bly of the replisome through addition of the primosome components and elements of the lagging-strand

89 can be broken down into four basic units: a primosome composed of gp41, gp61, and gp59; a leading st

90 The bacterial primosome comprises the replicative homo-hexameric ring

91 ggest that the functional T4 DNA replication primosome consists of an integrated 6:1 helicase-primase

92 isotropy methods show that the functional T4 primosome consists of six gp41 helicase subunits that as

93 The Herpes simplex virus type 1 primosome consists of three subunits that are the produc

94 g protein, polymerase accessory factors, and primosome (DNA helicase and DNA primase activities).

95 required to form functional and fully active primosome-DNA complexes.

96 en activities proposed to participate in its primosome function include DNA helicase and protein-prot

97 acts Tag, and demonstrated its vital role in primosome function.

98 that p68-T antigen interaction is vital for primosome function.

99 other two mutants, is required for T-antigen primosome function.

100 ted for the polA (DNA polymerase I) or priA (primosome) genes are as sensitive to MMS and MNNG as alk

101 The primosome helicase of bacteriophage T4 was assembled fro

102 e assembly of the bacterial loader-dependent primosome, helicase loader proteins bind to the hexameri

103 and resulted in fully active and processive primosome helicases with gp41:gp61 subunit ratios of 6:1

104 functional importance in activating the SV40 primosome in cell-free reactions with purified Pol-prim,

105 Our spectroscopic probes show that the primosome in this stable helicase initiation complex bin

106 ed PriA, PriB, PriC, DnaT, and DnaB, whereas primosomes included DnaG.

107 usible mechanism for all transactions of the primosome including initiation, elongation, accurate cou

108 ichiometry of primase binding as part of the primosome is helicase hexamer:primase in a ratio of 1:6,

109 nd whose mechanism of association within the primosome is not yet understood.

110 on stalls and forks disassemble, the restart primosome is required to reload the replicative helicase

111 Within replisomes for DNA replication, the primosome is responsible for unwinding double-stranded D

112 template of forked structures such that the primosome is specifically assembled on that DNA strand.

113 e primase subunit; and (v) the reconstituted primosome is stable for at least 10 to 20 min after NTP

114 NA primase mutants and provide insights into primosome loading on RPA-coated ssDNA and regulation of

115 ication fork occurs normally in both rep and primosome mutants.

116 he fundamental activities of the replicative primosomes of Escherichia coli are provided by DnaB, the

117 Like the well characterized primosomes of phages T7 and T4, this trio of proteins co

118 The ability to load a complete primosome on D loop DNA is a step necessary for replicat

119 so directs the assembly of a varphiX174-type primosome on D loop DNA.

120 equired for the assembly of the phiX174-type primosome on DNA, in cellular DNA replication has been u

121 Assembly of the bacteriophage T4 primosome on individual molecules of ssDNA or forked DNA

122 ' --> 5' DNA helicase, directs assembly of a primosome on some bacteriophage and plasmid DNAs.

123 scription of the pathway for assembly of the primosome on the lagging strand of DNA at a replication

124 We hypothesize that maintenance of the primosome on the replicated DNA may provide a mechanism

125 Assembling the components of the primosome onto a model DNA replication fork is a multist

126 f gp41, the DNA helicase component of the T4 primosome, onto lagging strand ssDNA at nascent replicat

127 f gp41, the DNA helicase component of the T4 primosome, onto lagging strand ssDNA.

128 We show that this primosome plays an essential role in bacteriophage Mu DN

129 Here, we demonstrate that assembly of primosome protein complexes represents a key regulatory

130 h single-stranded DNA is handed off from one primosome protein to another as a repaired replication f

131 o the corresponding domains of the bacterial primosome protein, DnaD.

132 r replication restart mechanism and requires primosome proteins PriA, PriB, and DnaT for replisome re

133 ied Escherichia coli DNA replication restart primosome proteins, suggesting that there might be disti

134 d protein binding by DNA replication restart primosome proteins, we determined the crystal structure

135 the assembly and function of the replication primosome subassemblies of higher organisms as well.

136 We have examined the formation of the primosome subassembly of the bacteriophage T4-coded DNA

137 del for the structure and function of the T4 primosome that are likely to be relevant to the assembly

138 SV40 large T antigen, constituting a simple primosome that is active in vitro.

139 licated DNA may provide a mechanism to allow primosomes to participate in the resolution of recombina

140 wer subunit ratios substantially reduced the primosome unwinding activity.

141 ate of approximately 1 primer per second per primosome was achieved.

142 rate of unwinding of duplex DNA by the HSV-1 primosome was also determined indirectly by measuring th

143 The phiX-type primosome was discovered during the resolution and recon

144 rus type 1 (HSV-1)-encoded helicase-primase (primosome) was determined by measuring the rate of appea

145 riA protein, a component of the phiX174-type primosome, was previously shown to be essential for dama

146 ailed interactions of the primase within the primosome, we have constructed and characterized variant

147 imase, ATPase and helicase activities of the primosome, we have used site-directed mutagenesis and in

148 strand DNA-binding protein, a heterotrimeric primosome with 5'-3' DNA helicase and primase activities