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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 g helicase-nuclease of Escherichia coli, the RecBCD enzyme.
6 nsible for the nucleolytic activities of the RecBCD enzyme.
7 is a recombination hotspot recognized by the RecBCD enzyme.
8 ocessivity of DNA unwinding catalyzed by the RecBCD enzyme.
9 ks as the major RecA-independent role of the RecBCD enzyme.
10 ction with chi also affects translocation by RecBCD enzyme.
11  that regulate the recombination function of RecBCD enzyme.
12 he same manner as the chi-modified wild-type RecBCD enzyme.
13 protein but functions outside the context of RecBCD enzyme.
14 ia coli are initiated by the multifunctional RecBCD enzyme.
15 NA break repair in Escherichia coli requires RecBCD enzyme, a complex nuclease and DNA helicase regul
16 ia coli pathway of DNA break repair requires RecBCD enzyme, a complex protein machine with multiple a
17 d at double-stranded DNA breaks requires the RecBCD enzyme, a multifunctional heterotrimeric complex
18    In Escherichia coli, Chi hotspots control RecBCD enzyme, a protein machine essential for the major
19 nit, it has a biological role in stimulating RecBCD enzyme activity.
20                                              RecBCD enzyme acts in the major pathway of homologous re
21 on: the disassembly of all three subunits of RecBCD enzyme after its interaction with a Chi recombina
22                      In Escherichia coli the RecBCD enzyme also loads the DNA strand-exchange protein
23 nuclease activity, recognition of chi by the RecBCD enzyme also up-regulates a nuclease activity of t
24 ngly, the organism does not appear to have a RecBCD enzyme, an enzyme that is critical for double-str
25  of approximately 24 nt was tightly bound to RecBCD enzyme and co-purified with it.
26 tion in Escherichia coli is initiated by the RecBCD enzyme and is stimulated by an 8-nucleotide eleme
27  element that modifies the activities of the RecBCD enzyme and leads to loading of the DNA strand exc
28  of helicase and nuclease domains within the RecBCD enzyme, and also suggest a new level at which the
29 cement), stemming from studies with purified RecBCD enzyme, and argue against models in which Chi con
30 er stimulate ATP hydrolysis by the RecBC and RecBCD enzymes, and they are substrates for the ATP-stim
31 y sequence, chi, the enzymatic properties of RecBCD enzyme are altered.
32  hotspot activity and that nicking of DNA by RecBCD enzyme at Chi is sufficient.
33 The rates of ATP hydrolysis observed for the RecBCD enzyme at low concentrations of pd(T)12 are best
34 ion makes E. coli cells dependent on RecA or RecBCD enzymes at high temperature, suggesting dependenc
35 hey also imply conformational differences of RecBCD enzyme bound to different types of ends; these co
36                                 Although the RecBCD enzyme briefly pauses at chi, no specific binding
37  regulates not only the nuclease activity of RecBCD enzyme, but also the ability of RecBCD to promote
38         Inactivation of the Escherichia coli RecBCD enzyme by the lambda Gam protein is an essential
39 ted inactivation and disassembly of purified RecBCD enzyme can account for the previously reported Ch
40       We also show that the Escherichia coli RecBCD enzyme can mediate the degradation of broken DNA
41                             Furthermore, the RecBCD enzyme can translocate through DNA heteroduplex b
42 ns lead us to hypothesize that, in wild-type RecBCD enzyme, Chi is recognized by RecC, which then sig
43 red in the structure of the Escherichia coli RecBCD enzyme complex reported previously.
44          The heterotrimeric Escherichia coli RecBCD enzyme comprises two helicase motors with differe
45 led biochemical characterization of a mutant RecBCD enzyme, designated RecBC1004D, that displays a re
46  A crucial feature of this regulation is the RecBCD enzyme-directed loading of RecA protein specifica
47 tein reduces the level of DNA degradation by RecBCD enzyme during unwinding, by binding to these ssDN
48                                         When RecBCD enzyme encounters chi, the intensity and polarity
49                                              RecBCD enzyme facilitates loading of RecA protein onto s
50                                  The E. coli RecBCD enzyme facilitates the loading of RecA onto singl
51            Both the binding stoichiometry of RecBCD enzyme for the ends of duplex DNA and the apparen
52    We have expressed the RecD subunit of the RecBCD enzyme from Escherichia coli as a fusion protein
53                                          The RecBCD enzyme from Escherichia coli is an ATP-dependent
54                                          The RecBCD enzyme from Escherichia coli is an ATP-dependent
55  Bacteriophage P22 Abc2 protein binds to the RecBCD enzyme from Escherichia coli to promote phage gro
56     The RecB subunit of the Escherichia coli RecBCD enzyme has been shown in previous work to have tw
57 raction with the recombination hot spot chi, RecBCD enzyme has both 3'-->5' exonuclease and a weaker
58     The RecB subunit of the Escherichia coli RecBCD enzyme has both helicase and nuclease activities.
59 ts unwinding of DNA containing Chi, purified RecBCD enzyme has two alternative nucleolytic reactions,
60 3.6 A) electron density maps for the E. coli RecBCD enzyme in complex with a long DNA substrate that
61 among possible RecA-independent roles of the RecBCD enzyme in replication, repair, and DNA degradatio
62 haracterized homologues are RecD subunits of RecBCD enzymes in other bacteria.
63 ivity, we test this idea by analyzing mutant RecBCD enzymes in which either of the two helicase motor
64  converts the antirecombinogenic form of the RecBCD enzyme into a recombinogenic form by causing two
65            We recently demonstrated that the RecBCD enzyme is a bipolar DNA helicase that employs two
66                                              RecBCD enzyme is a complex helicase and nuclease, essent
67                                          The RecBCD enzyme is a complex heterotrimeric helicase/nucle
68                                              RecBCD enzyme is a heterotrimeric helicase/nuclease that
69                                              RecBCD enzyme is a processive DNA helicase and nuclease
70                The structure and function of RecBCD enzyme is altered on its interaction with the rec
71                                          The RecBCD enzyme is an ATP-dependent nuclease on both singl
72 nation hotspot, chi (5'-GCTGGTGG-3'), by the RecBCD enzyme is central to homologous recombination.
73  new level at which the nuclease activity of RecBCD enzyme is controlled.
74 loading of RecA protein by the chi-activated RecBCD enzyme is essential for RecBCD-mediated homologou
75                                          The RecBCD enzyme is important for both restriction of forei
76 t after reaction with DNA bearing Chi sites, RecBCD enzyme is inactivated and the three subunits migr
77 how that, in the absence of SSB protein, the RecBCD enzyme is inhibited by the ssDNA products of unwi
78                                          The RecBCD enzyme is required for homologous recombination a
79 cal results demonstrate that RecA loading by RecBCD enzyme is required for recombination in E. coli c
80                         In Escherichia coli, RecBCD enzyme is required for the major pathway of these
81 functional counterpart, the Escherichia coli RecBCD enzyme, it also recognizes and responds to a spec
82 ical functions associated with the wild-type RecBCD enzyme, it is completely defective for genetic re
83  the nuclease and helicase activities of the RecBCD enzyme, leading to generation of an early DNA int
84  of recombination in which Chi regulates one RecBCD enzyme molecule to make a single recombinational
85 ,300 base pairs of dsDNA unwound by a single RecBCD enzyme molecule.
86         The mean behaviour of the individual RecBCD enzyme molecules corresponds to that observed in
87 arations the molar ratio of RNA molecules to RecBCD enzyme molecules ranged from 0.2 to <0.008.
88  DNA ends, but there is no evidence that the RecBCD enzyme moves along these DNA molecules in an ATP-
89 D; therefore, to observe full fragmentation, RecBCD enzyme needs to be inactivated.
90                                          The RecBCD enzyme of Escherichia coli functions in the seemi
91                                          The RecBCD enzyme of Escherichia coli initiates homologous r
92                                          The RecBCD enzyme of Escherichia coli is an ATP-dependent DN
93                           The heterotrimeric RecBCD enzyme of Escherichia coli is required for the ma
94 is is placed on contrasting views of how the RecBCD enzyme of Escherichia coli promotes recombination
95 ught to be the functional counterpart of the RecBCD enzyme of Escherichia coli.
96 sualized directly the movement of individual RecBCD enzymes on single molecules of double-stranded DN
97 ase complex: either an Escherichia coli-type RecBCD enzyme or a Bacillus-type AddAB enzyme.
98  along single molecules of DNA, we could see RecBCD enzyme pause precisely at chi.
99 at the enzymatic activities of the AddAB and RecBCD enzymes promote their horizontal transfer is disc
100 ks requires LexA repressor, and the RecA and RecBCD enzymes--proteins best known for their role as in
101  results show that an actively translocating RecBCD enzyme requires only the sequence information in
102  following DNA cleavage by the translocating RecBCD enzyme, resulting in the restoration of catalytic
103                             We conclude that RecBCD enzyme's nucleolytic degradation of DNA is not ne
104      The nuclease reactions catalyzed by the RecBCD enzyme should therefore follow the same mechanism
105 e we demonstrate that purified RecA protein, RecBCD enzyme, single-stranded DNA-binding (SSB) protein
106 e chi* sequence also regulates the wild-type RecBCD enzyme, supporting the notion that variants of th
107             These data define a locus of the RecBCD enzyme that is essential not only for nuclease fu
108              We report a new class of mutant RecBCD enzymes that cut DNA at novel positions that depe
109                           Like the wild-type RecBCD enzyme, the two mutant proteins maintain the abil
110 d argue against models in which Chi converts RecBCD enzyme to a state capable of promoting multiple e
111  taken together present a unique response of RecBCD enzyme to bulky DNA adducts.
112 he polarity of DNA degradation and activates RecBCD enzyme to coordinate the loading of the DNA stran
113 in a manner analogous to the response of the RecBCD enzyme to interaction with chi sequences.
114  eliminated the ability of the translocating RecBCD enzyme to recognize and respond to the recombinat
115 ntage of the ability of the Escherichia coli RecBCD enzyme to unwind restricted dsDNA.
116  RecA loading is not observed with wild-type RecBCD enzyme until it acts at a Chi site, our observati
117 er binding to a double-stranded DNA end, the RecBCD enzyme unwinds and degrades the DNA processively.
118                         The Escherichia coli RecBCD enzyme unwinds DNA from a free double-stranded DN
119  thus appears critical for the regulation of RecBCD enzyme via the assembly and, we propose, disassem
120 ssays, we demonstrate that the translocating RecBCD enzyme, which has been activated by chi, coordina
121     Stimulation requires the multifunctional RecBCD enzyme, which is both a helicase and a 3' --> 5'
122 izing radiation, in spite of the lack of the RecBCD enzyme, which is essential for double-strand DNA
123 ecombination in E. coli are initiated by the RecBCD enzyme, which unwinds and simultaneously degrades
124 ase enzymes, related to the Escherichia coli RecBCD enzyme, which, with RecA, is required for repair

 
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