ライフサイエンスコーパス: RecBCD enzyme

1 20-fold lower chi recognition than wild-type RecBCD enzyme.

2 double-strand exonuclease activities of the RecBCD enzyme.

3 o turn off the degradative activities of the RecBCD enzyme.

4 or the helicase activity of Escherichia coli RecBCD enzyme.

5 nsible for the nucleolytic activities of the RecBCD enzyme.

6 is a recombination hotspot recognized by the RecBCD enzyme.

7 ocessivity of DNA unwinding catalyzed by the RecBCD enzyme.

8 ks as the major RecA-independent role of the RecBCD enzyme.

9 ction with chi also affects translocation by RecBCD enzyme.

10 that regulate the recombination function of RecBCD enzyme.

11 protein but functions outside the context of RecBCD enzyme.

12 he same manner as the chi-modified wild-type RecBCD enzyme.

13 ia coli are initiated by the multifunctional RecBCD enzyme.

14 NA break repair in Escherichia coli requires RecBCD enzyme, a complex nuclease and DNA helicase regul

15 ia coli pathway of DNA break repair requires RecBCD enzyme, a complex protein machine with multiple a

16 d at double-stranded DNA breaks requires the RecBCD enzyme, a multifunctional heterotrimeric complex

17 In Escherichia coli, Chi hotspots control RecBCD enzyme, a protein machine essential for the major

18 nit, it has a biological role in stimulating RecBCD enzyme activity.

19 RecBCD enzyme acts in the major pathway of homologous re

20 on: the disassembly of all three subunits of RecBCD enzyme after its interaction with a Chi recombina

21 nuclease activity, recognition of chi by the RecBCD enzyme also up-regulates a nuclease activity of t

22 ngly, the organism does not appear to have a RecBCD enzyme, an enzyme that is critical for double-str

23 of approximately 24 nt was tightly bound to RecBCD enzyme and co-purified with it.

24 tion in Escherichia coli is initiated by the RecBCD enzyme and is stimulated by an 8-nucleotide eleme

25 element that modifies the activities of the RecBCD enzyme and leads to loading of the DNA strand exc

26 of helicase and nuclease domains within the RecBCD enzyme, and also suggest a new level at which the

27 cement), stemming from studies with purified RecBCD enzyme, and argue against models in which Chi con

28 er stimulate ATP hydrolysis by the RecBC and RecBCD enzymes, and they are substrates for the ATP-stim

29 y sequence, chi, the enzymatic properties of RecBCD enzyme are altered.

30 hotspot activity and that nicking of DNA by RecBCD enzyme at Chi is sufficient.

31 The rates of ATP hydrolysis observed for the RecBCD enzyme at low concentrations of pd(T)12 are best

32 ion makes E. coli cells dependent on RecA or RecBCD enzymes at high temperature, suggesting dependenc

33 hey also imply conformational differences of RecBCD enzyme bound to different types of ends; these co

34 Although the RecBCD enzyme briefly pauses at chi, no specific binding

35 regulates not only the nuclease activity of RecBCD enzyme, but also the ability of RecBCD to promote

36 Inactivation of the Escherichia coli RecBCD enzyme by the lambda Gam protein is an essential

37 ted inactivation and disassembly of purified RecBCD enzyme can account for the previously reported Ch

38 We also show that the Escherichia coli RecBCD enzyme can mediate the degradation of broken DNA

39 Furthermore, the RecBCD enzyme can translocate through DNA heteroduplex b

40 ns lead us to hypothesize that, in wild-type RecBCD enzyme, Chi is recognized by RecC, which then sig

41 red in the structure of the Escherichia coli RecBCD enzyme complex reported previously.

42 The heterotrimeric Escherichia coli RecBCD enzyme comprises two helicase motors with differe

43 led biochemical characterization of a mutant RecBCD enzyme, designated RecBC1004D, that displays a re

44 A crucial feature of this regulation is the RecBCD enzyme-directed loading of RecA protein specifica

45 tein reduces the level of DNA degradation by RecBCD enzyme during unwinding, by binding to these ssDN

46 When RecBCD enzyme encounters chi, the intensity and polarity

47 RecBCD enzyme facilitates loading of RecA protein onto s

48 The E. coli RecBCD enzyme facilitates the loading of RecA onto singl

49 Both the binding stoichiometry of RecBCD enzyme for the ends of duplex DNA and the apparen

50 We have expressed the RecD subunit of the RecBCD enzyme from Escherichia coli as a fusion protein

51 The RecBCD enzyme from Escherichia coli is an ATP-dependent

52 The RecBCD enzyme from Escherichia coli is an ATP-dependent

53 Bacteriophage P22 Abc2 protein binds to the RecBCD enzyme from Escherichia coli to promote phage gro

54 The RecB subunit of the Escherichia coli RecBCD enzyme has been shown in previous work to have tw

55 raction with the recombination hot spot chi, RecBCD enzyme has both 3'-->5' exonuclease and a weaker

56 The RecB subunit of the Escherichia coli RecBCD enzyme has both helicase and nuclease activities.

57 ts unwinding of DNA containing Chi, purified RecBCD enzyme has two alternative nucleolytic reactions,

58 3.6 A) electron density maps for the E. coli RecBCD enzyme in complex with a long DNA substrate that

59 among possible RecA-independent roles of the RecBCD enzyme in replication, repair, and DNA degradatio

60 haracterized homologues are RecD subunits of RecBCD enzymes in other bacteria.

61 ivity, we test this idea by analyzing mutant RecBCD enzymes in which either of the two helicase motor

62 converts the antirecombinogenic form of the RecBCD enzyme into a recombinogenic form by causing two

63 We recently demonstrated that the RecBCD enzyme is a bipolar DNA helicase that employs two

64 RecBCD enzyme is a complex helicase and nuclease, essent

65 The RecBCD enzyme is a complex heterotrimeric helicase/nucle

66 RecBCD enzyme is a heterotrimeric helicase/nuclease that

67 RecBCD enzyme is a heterotrimeric helicase/nuclease that

68 RecBCD enzyme is a processive DNA helicase and nuclease

69 The structure and function of RecBCD enzyme is altered on its interaction with the rec

70 The RecBCD enzyme is an ATP-dependent nuclease on both singl

71 nation hotspot, chi (5'-GCTGGTGG-3'), by the RecBCD enzyme is central to homologous recombination.

72 new level at which the nuclease activity of RecBCD enzyme is controlled.

73 loading of RecA protein by the chi-activated RecBCD enzyme is essential for RecBCD-mediated homologou

74 The RecBCD enzyme is important for both restriction of forei

75 t after reaction with DNA bearing Chi sites, RecBCD enzyme is inactivated and the three subunits migr

76 how that, in the absence of SSB protein, the RecBCD enzyme is inhibited by the ssDNA products of unwi

77 The RecBCD enzyme is required for homologous recombination a

78 cal results demonstrate that RecA loading by RecBCD enzyme is required for recombination in E. coli c

79 functional counterpart, the Escherichia coli RecBCD enzyme, it also recognizes and responds to a spec

80 ical functions associated with the wild-type RecBCD enzyme, it is completely defective for genetic re

81 the nuclease and helicase activities of the RecBCD enzyme, leading to generation of an early DNA int

82 of recombination in which Chi regulates one RecBCD enzyme molecule to make a single recombinational

83 ,300 base pairs of dsDNA unwound by a single RecBCD enzyme molecule.

84 The mean behaviour of the individual RecBCD enzyme molecules corresponds to that observed in

85 arations the molar ratio of RNA molecules to RecBCD enzyme molecules ranged from 0.2 to <0.008.

86 DNA ends, but there is no evidence that the RecBCD enzyme moves along these DNA molecules in an ATP-

87 D; therefore, to observe full fragmentation, RecBCD enzyme needs to be inactivated.

88 The RecBCD enzyme of Escherichia coli functions in the seemi

89 The RecBCD enzyme of Escherichia coli initiates homologous r

90 The RecBCD enzyme of Escherichia coli is an ATP-dependent DN

91 The heterotrimeric RecBCD enzyme of Escherichia coli is required for the ma

92 is is placed on contrasting views of how the RecBCD enzyme of Escherichia coli promotes recombination

93 ught to be the functional counterpart of the RecBCD enzyme of Escherichia coli.

94 sualized directly the movement of individual RecBCD enzymes on single molecules of double-stranded DN

95 ase complex: either an Escherichia coli-type RecBCD enzyme or a Bacillus-type AddAB enzyme.

96 along single molecules of DNA, we could see RecBCD enzyme pause precisely at chi.

97 at the enzymatic activities of the AddAB and RecBCD enzymes promote their horizontal transfer is disc

98 ks requires LexA repressor, and the RecA and RecBCD enzymes--proteins best known for their role as in

99 results show that an actively translocating RecBCD enzyme requires only the sequence information in

100 following DNA cleavage by the translocating RecBCD enzyme, resulting in the restoration of catalytic

101 We conclude that RecBCD enzyme's nucleolytic degradation of DNA is not ne

102 The nuclease reactions catalyzed by the RecBCD enzyme should therefore follow the same mechanism

103 e we demonstrate that purified RecA protein, RecBCD enzyme, single-stranded DNA-binding (SSB) protein

104 e chi* sequence also regulates the wild-type RecBCD enzyme, supporting the notion that variants of th

105 These data define a locus of the RecBCD enzyme that is essential not only for nuclease fu

106 We report a new class of mutant RecBCD enzymes that cut DNA at novel positions that depe

107 Like the wild-type RecBCD enzyme, the two mutant proteins maintain the abil

108 d argue against models in which Chi converts RecBCD enzyme to a state capable of promoting multiple e

109 taken together present a unique response of RecBCD enzyme to bulky DNA adducts.

110 he polarity of DNA degradation and activates RecBCD enzyme to coordinate the loading of the DNA stran

111 in a manner analogous to the response of the RecBCD enzyme to interaction with chi sequences.

112 eliminated the ability of the translocating RecBCD enzyme to recognize and respond to the recombinat

113 ntage of the ability of the Escherichia coli RecBCD enzyme to unwind restricted dsDNA.

114 RecA loading is not observed with wild-type RecBCD enzyme until it acts at a Chi site, our observati

115 er binding to a double-stranded DNA end, the RecBCD enzyme unwinds and degrades the DNA processively.

116 The Escherichia coli RecBCD enzyme unwinds DNA from a free double-stranded DN

117 thus appears critical for the regulation of RecBCD enzyme via the assembly and, we propose, disassem

118 ssays, we demonstrate that the translocating RecBCD enzyme, which has been activated by chi, coordina

119 Stimulation requires the multifunctional RecBCD enzyme, which is both a helicase and a 3' --> 5'

120 izing radiation, in spite of the lack of the RecBCD enzyme, which is essential for double-strand DNA

121 ecombination in E. coli are initiated by the RecBCD enzyme, which unwinds and simultaneously degrades

122 ase enzymes, related to the Escherichia coli RecBCD enzyme, which, with RecA, is required for repair