ライフサイエンスコーパス: DNA polymerase IV

1 ludes the nearby dinB+ gene (for error-prone DNA polymerase IV).

2 leted for the SOS gene dinB, which codes for DNA polymerase IV.

3 notype that is suppressed by inactivation of DNA polymerase IV.

4 ed was examined with Solfolobus solfataricus DNA polymerase IV, a member of the RAD30A subfamily of t

5 E. coli dinB encodes DNA polymerase IV and greatly increases spontaneous muta

6 DNA polymerases, including Escherichia coli DNA polymerase IV and human DNA polymerase kappa, effici

7 stress-induced ampD mutations require DinB (DNA polymerase IV) and partially require error-prone DNA

8 repair system and the inducible error-prone DNA polymerase IV, and the mutations are mostly -1 delet

9 Using single-molecule analyses, we show that DNA polymerase IV associates with the replisome in a con

10 ing affinity is an intrinsic property of the DNA polymerase IV-beta clamp interaction and not an indi

11 is association slows the replisome, requires DNA polymerase IV binding to the beta clamp but not its

12 DNA polymerase IV binds dNTP substrates with about 10-fo

13 Bypass by DNA polymerase IV came at the expense of the inherent le

14 e translesion DNA synthesis DNA polymerases, DNA polymerase IV, can either act in concert with the re

15 We show that DinB (DNA polymerase IV) catalyses accurate TLS over one such

16 primitive DNA damage checkpoint and prevents DNA polymerase IV-dependent -1 frameshift mutagenesis, w

17 strate that YqjH has 36% identity to E. coli DNA polymerase IV (DinB protein), and YqjW has 26% ident

18 t for cleavage and interacts physically with DNA polymerase IV (DinB) and the beta clamp.

19 rding the role of SOS-inducible, error-prone DNA polymerase IV (DinB) in spontaneous mutation are res

20 arily conserved Escherichia coli translesion DNA polymerase IV (DinB) is one of three enzymes that ca

21 proteins, the SOS response, and error-prone DNA polymerase IV (DinB), amplification requires neither

22 We show that the increased DNA polymerase IV-dNTP binding affinity is an intrinsic

23 tension studies have shown that the Y-family DNA polymerase IV (Dpo4) from Sulfolobus solfataricus P2

24 Y-Family DNA polymerase IV (Dpo4) from Sulfolobus solfataricus se

25 sfer reaction catalyzed by the lesion-bypass DNA polymerase IV (Dpo4) from Sulfolobus solfataricus, w

26 Sulfolobus solfataricus P2 DNA polymerase IV (Dpo4) has been shown to catalyze bypa

27 imer extension by Sulfolobus solfataricus P2 DNA polymerase IV (Dpo4) indicated preferential incorpor

28 These data indicate that the error-prone DNA polymerase IV (Dpo4) inefficiently extended past the

29 Sulfolobus solfataricus P2 DNA polymerase IV (Dpo4) is a DinB homolog that belongs

30 Sulfolobus solfataricus DNA polymerase IV (Dpo4) is a member of the Y family of

31 Sulfolobus solfataricus P2 DNA polymerase IV (Dpo4) is a thermostable archaeal enzy

32 tion catalyzed by Sulfolobus solfataricus P2 DNA polymerase IV (Dpo4) is resolved by pre-steady-state

33 merase kappa homolog Sulfolobus solfataricus DNA polymerase IV (Dpo4) produces "-1" frameshift deleti

34 cs with the Y-family Sulfolobus solfataricus DNA polymerase IV (Dpo4) showed 90-fold higher incorpora

35 family polymerase Sulfolobus solfataricus P2 DNA polymerase IV (Dpo4) using single-molecule fluoresce

36 lesion catalyzed by Sulfolobus solfataricus DNA polymerase IV (Dpo4), a model Y-family DNA polymeras

37 r pre-steady-state kinetic studies show that DNA polymerase IV (Dpo4), a prototype Y-family enzyme fr

38 , can be bypassed by Sulfolobus solfataricus DNA polymerase IV (Dpo4), although this representative Y

39 d, with the Y-family Sulfolobus solfataricus DNA polymerase IV (Dpo4), at resolutions between 2.4 and

40 mily DNA polymerase, Sulfolobus solfataricus DNA polymerase IV (Dpo4), for the correct insertion of d

41 N(2)-epsilondG by Sulfolobus solfataricus P2 DNA polymerase IV (Dpo4), leading to a one-base deletion

42 inding processes of the multidomain Y-family DNA polymerase IV (DPO4).

43 mily DNA polymerase, Sulfolobus solfataricus DNA polymerase IV (Dpo4).

44 ossesses a DinB homolog that has been termed DNA polymerase IV (Dpo4).

45 Escherichia coli DNA polymerase IV encoded by the dinB gene is involved i

46 Escherichia coli DNA polymerase IV, encoded by the dinB gene, is a member

47 ofolate reductase, chemotaxis protein Y, and DNA polymerase IV) in soluble and ribosome-bound states.

48 eotide deletions is a biological hallmark of DNA polymerase IV infidelity responsible for enhancing c

49 anslesion synthesis polymerases tested, only DNA polymerase IV, not DNA polymerase II, could engage p

50 Our efforts to understand why DinB (DNA polymerase IV) overproduction is cytotoxic to Escher

51 ved Escherichia coli result from error-prone DNA polymerase IV (Pol IV) (DinB) and that the mutagenes

52 response sigma factor, regulates error-prone DNA polymerase IV (Pol IV) (encoded by the dinB gene).

53 e activity of the specialized DNA polymerase DNA polymerase IV (Pol IV) both in stationary-phase and

54 SOS-induced levels of DNA polymerase IV (Pol IV) confer UV sensitivity upon th

55 The actions of Escherichia coli DNA Polymerase IV (Pol IV) in mutagenesis are managed by

56 oli strains with and without the error-prone DNA polymerase IV (Pol IV) were compared.

57 Escherichia coli DNA polymerase IV (pol IV), a member of the error-prone

58 tion in FC40 mostly results from error-prone DNA polymerase IV (Pol IV), encoded by dinB; most of the

59 have been proposed for the Escherichia coli DNA polymerase IV (pol IV).

60 largely but not entirely due to error-prone DNA polymerase IV (Pol IV).

61 pair, Saccharomyces cerevisiae has only one, DNA polymerase IV (pol IV).

62 t strains had 1/10 the amount of error-prone DNA polymerase IV (Pol IV).

63 tly homologous with that of Escherichia coli DNA polymerase IV (pol IV).

64 Escherichia coli DNA polymerase IV (Pol IV, also known as DinB) is a Y-fa

65 Escherichia coli DinB (DNA polymerase IV) possesses an enzyme architecture resu

66 Bypass by DNA polymerase IV required its ability to interact with

67 erty for the beta clamp, which when bound to DNA polymerase IV results in a large increase in dNTP bi

68 irect consequence of an increased binding of DNA polymerase IV to DNA.

69 and thus prevents binding of the translesion DNA polymerase IV to the clamp, providing a novel insigh

70 tion of the SOS response, the association of DNA polymerase IV with the replisome provides both a sur

71 NA damage is not required for association of DNA polymerase IV with the replisome.