ライフサイエンスコーパス: topo IV

1 two type IIA topoisomerases, DNA gyrase and topo IV, that together help manage chromosome integrity

2 two type IIA DNA topoisomerases, gyrase and topo IV, which maintain chromosome topology by variously

3 ysiologic distinction between DNA gyrase and topo IV.

4 drug-resistance mutations in both gyrase and topo IV.

5 and suggesting a framework by which MukB and topo IV may collaborate during daughter chromosome disen

6 ineates strong mechanistic parallels between topo IV and gyrase, while explaining how structural diff

7 se residues, and tested their effect on both topo IV enzymatic activity and DNA binding by the isolat

8 se data show that DNA binding and bending by topo IV can be uncoupled, and indicate that the stabiliz

9 d conformation reflects efficient binding by topo IV of the two DNA segments that participate in the

10 how that the rate of supercoil relaxation by topo IV is several orders of magnitude faster than hithe

11 rinsic recognition' of DNA cleavage sites by topo IV from drug-induced preferences.

12 tes the relaxation of negative supercoils by topo IV; to understand the mechanism of their action and

13 The enzymes tested were Escherichia coli topo IV and yeast topo II (type IIA enzymes that exhibit

14 into DNA, which makes better substrates for topo IV.

15 Although closely related to gyrase, topo IV preferentially decatenates DNA and relaxes posit

16 Our results explain how topo IV can rapidly remove (+) supercoils to support DNA

17 reconciling different models to explain how topo IV discriminates between distinct DNAs topologies.

18 Escherichia coli topoisomerase IV (topo IV) is an essential enzyme that unlinks the daughte

19 We showed recently that topoisomerase IV (topo IV) is the only important decatenase of DNA replica

20 d that both DNA gyrase and topoisomerase IV (topo IV) promote replication fork progression.

21 uency for Escherichia coli topoisomerase IV (topo IV) that displays efficient non-equilibrium topolog

22 somerase, Escherichia coli topoisomerase IV (topo IV), using a combination of site-directed mutagenes

23 previously shown that DNA topoisomerase IV (topo IV), which is encoded by the parE and parC genes, i

24 eins reconstituted to form topoisomerase IV (topo IV), which was highly proficient for ATP-dependent

25 trate for Escherichia coli topoisomerase IV (topo IV).

26 We measured topo IV relaxation of (-) and (+) supercoils in real tim

27 ontrary to the predictions of the KPR model, topo IV and topo III unlinking rates were linearly relat

28 ined the crystal structure of a minimal MukB-topo IV complex to 2.3 A resolution.

29 Interestingly, the configuration of the MukB.topo IV complex sterically disfavours intradimeric inter

30 t selectively with the quinolone norfloxacin topo IV, gyrase, both enzymes, or neither enzyme in vivo

31 The ability of topo IV to discriminate between positively and negativel

32 tly, nor contribute equally to the action of topo IV on different types of DNA substrates.

33 decatenates DNA, two hallmark activities of topo IV.

34 did not affect the basal ATPase activity of topo IV or its affinity for DNA.

35 Here, we used chemical cross-linking of topo IV to demonstrate that enzyme bound to positively s

36 The subcellular localization of topo IV provides physical evidence that it may be part o

37 s, we observed novel cross-linked species of topo IV when positively supercoiled DNA was in the react

38 rC CTD controls the substrate specificity of topo IV, likely by capturing DNA segments of certain cro

39 ecatenation activity comparable with that of topo IV, supporting proposed roles for topo III in DNA s

40 ith a C-terminal DNA binding domain (CTD) on topo IV's ParC subunit.

41 ction reveal that the cellular dependency on topo IV derives from a joint need for both strand passag

42 ictingly categorized as either DNA gyrase or topo IV.

43 Otherwise, topo IV relaxed (+) supercoils at a 20-fold faster rate

44 ted DNA breakage by Streptococcus pneumoniae topo IV and gyrase.

45 mical studies show that the hinge stimulates topo IV by competing for a site on the CTD that normally

46 We also discovered that topo IV has an unexpectedly strong DNA relaxation activi

47 We propose that topo IV discriminates between (-) and (+) supercoiled DN

48 We showed that topo IV is the primary decatenase in vivo and that this

49 These results suggest that topo IV activity may be regulated primarily through parE

50 rC required functional ParE, suggesting that topo IV activity is required for the localization.

51 oils in plasmid DNA in vivo, suggesting that topo IV can promote replication by removing (+) supercoi

52 The presumptive promoters of the topo IV genes display striking similarities to, as well

53 parC promoter architecture suggest that the topo IV genes belong to a specialized subset of cell cyc

54 and report here that transcription of these topo IV genes is induced during the swarmer-to-stalked-c

55 Escherichia coli, the type IIA topoisomerase topo IV rapidly removes positive supercoils and catenane

56 leavage complex of gyrase and topoisomerase (topo) IV inducing site-specific DNA breakage within a be

57 by two interacting proteins, topoisomerase (topo) IV and MukB.

58 In vitro, topo IV readily distinguishes between the two possible c

59 When topo IV alone was inhibited, decatenation was almost com

60 The elongation rate with topo IV alone was 1/3 of normal.