ライフサイエンスコーパス: dRP lyase

1 ructures, and as a 5'-deoxyribose phosphate (dRP) lyase.

2 the 40-kDa core domain, indicating that the dRP lyase active site is in this region.

3 ng with a BER intermediate revealed that the dRP lyase active site resides in a 24-kDa domain of Pol

4 trometry and deletion analysis localized the dRP lyase active site to the C-terminal segment of Rev1'

5 ulate the deoxynucleotidyltransferase and 5'-dRP lyase activities of pol beta.

6 rimidinic (AP) and 5'-deoxyribose phosphate (dRP) lyase activities.

7 her DNA polymerases and a repair factor with dRP lyase activity (pol lambda, pol iota, pol theta and

8 a possesses both DNA polymerase activity and dRP lyase activity and is sufficient to carry out base e

9 Purified HMGB1 was found to have weak dRP lyase activity and to stimulate AP endonuclease and

10 is cancer-associated variant has very little dRP lyase activity but retains its polymerase activity.

11 The dRP lyase activity does not require divalent metal ions,

12 in their ability to support BER in vitro The dRP lyase activity in both of these proteins was confirm

13 tory effect of pyridoxal 5'-phosphate on the dRP lyase activity is consistent with involvement of a p

14 The 5'-dRP lyase activity is independent of the polymerase acti

15 hese results imply that Pol beta-dependent 5'dRP lyase activity is the rate-limiting step in BER in t

16 nthesis by pol beta demonstrated that the 5'-dRP lyase activity lags behind the polymerase activity d

17 Importantly, we also found that the dRP lyase activity of AtPol lambda allows efficient comp

18 Here we show that only the dRP lyase activity of beta-pol is required to reverse me

19 n of cytotoxic 5'dRP lesions, and that the 5'dRP lyase activity of Pol beta is required to restore re

20 On the other hand, the 5'-dRP lyase activity of the exon alpha Pol beta variant is

21 Finally, the dRP lyase activity of these mutants was evaluated using

22 as a nucleotidyl transferase but also has a dRP lyase activity that cleaves 5'-deoxyribose phosphate

23 how that AtPol lambda possesses an intrinsic dRP lyase activity that is reduced by mutations at two l

24 ting in a 5' 2-deoxyribose 5-phosphate (i.e. dRP lyase activity).

25 Lys35 and Lys60 are significantly reduced in dRP lyase activity, consistent with the lower ssDNA bind

26 lanine mutant, K35A/K68A/K72A, was devoid of dRP lyase activity, suggesting that the effects of the a

27 dentify BER cofactors, especially those with dRP lyase activity, we used a Pol beta null cell extract

28 s important for DNA binding and contains the dRP lyase activity, which is the rate-limiting step in t

29 Lys72 resulted in a greater than 90% loss of dRP lyase activity, without affecting DNA binding.

30 omain of DNA polymerase beta, which exhibits dRP lyase activity.

31 8 kDa domain of pol lambda also contains the dRP lyase activity.

32 de chains may be involved in DNA binding and dRP lyase activity.

33 ind that the mitochondrial pol beta also has dRP lyase activity.

34 ine mutants of Lys68 and Lys84 had wild-type dRP lyase activity.

35 polymerase inactive mutant retained full 5'-dRP lyase activity.

36 at human pol iota has deoxyribose phosphate (dRP) lyase activity and unusual specificity for activity

37 ncovered a weak 5'-deoxyribose phosphate (5'-dRP) lyase activity in mouse Rev1 and demonstrated the e

38 xcised by the 5'-deoxyribose-5-phosphate (5'-dRP) lyase activity of DNA polymerase beta (pol beta): h

39 a has intrinsic 5'-deoxyribose phosphate (5'-dRP) lyase activity that is involved in single-nucleotid

40 t functional for 5'-deoxyribose-phosphate (5'dRP) lyase activity.

41 a has an intrinsic 5'-deoxyribose phosphate (dRP) lyase activity.

42 evaluate the BER capacity of the enzyme, the dRP lyase and DNA polymerase activities were characteriz

43 lease and DNA ligase I, pol iota can use its dRP lyase and polymerase activities to repair G*U and A*

44 We confirm that DNA pol gamma is an active dRP lyase and show that other members of the family A of

45 e predominant Schiff base nucleophile in the dRP lyase beta-elimination catalytic reaction.

46 inding pocket that is required for efficient dRP lyase catalysis.

47 the pH profiles of beta-pol and 8-kDa domain dRP lyase catalytic efficiency exhibit a broad alkaline

48 system was found to be removal of dRP (i.e. dRP lyase), catalyzed by the amino-terminal domain of be

49 endonuclease, deoxyribonucleotide phosphate (dRP) lyase, DNA synthesis, and DNA ligase activities com

50 ormer indicates interactions of the 8 kDa 5'-dRP lyase domain of the second Pol beta molecule with th

51 As ASFV Pol X has no 5'-dRP lyase domain, it is reasonable not to form a 2 : 1 c

52 at sensitivity of this activity suggests the dRP lyase function requires a three-dimensional protein

53 l beta catalyzes two key enzymatic steps: 5'-dRP lyase gap trimming and template-directed DNA synthes

54 unlike pol beta, may only be able to act as dRP lyases in repair of AP sites when they occur at low

55 fractory to the beta-elimination step of the dRP lyase mechanism, thus blocking single-nucleotide BER

56 s not in an optimal configuration for the 5'-dRP lyase reaction in the crystal structures of the clos

57 The dRP lyase reaction proceeds by formation of a covalent e

58 , representing a trapped intermediate in the dRP lyase reaction, was subjected to controlled proteoly

59 ay interact with ssDNA or play a role in the dRP lyase reaction.

60 his limits the overall catalytic rate of the dRP lyase, so that family A DNA polymerases, unlike pol

61 We show that, unlike the canonical dRP lyases that act on a single substrate, hEXOG functio