ライフサイエンスコーパス: dGMP

1 nt of DNA polymerase, dAMP (22%), TMP (16%), dGMP (5.3%) and dCMP (1.2%) were all incorporated opposi

2 red with the MutT-Mg(2+) and the MutT-Mg(2+)-dGMP complexes, suggesting a more compact structure when

3 5'dCMP > 5'-dAMP > 5'dTMP >> 5'-dGMP and 3'-dGMP > 3'-dAMP approximately equal to 3'-dCMP approximat

4 e(-) transfer to produce cyclic (5'-O-C8)-3'-dGMP and [Pt(II)Cl(2)(dach)].

5 s not 8-oxo-3'-dGMP, but cyclic (5'-O-C8)-3'-dGMP.

6 2'-Deoxyguanosine, 3'-dGMP, 5'-dGMP, d-GpG, or double-stranded DNA were expose

7 ation of guanine radical cations in 2'dG, 3'-dGMP and 5'-dGMP in aqueous LiCl glasses at 143 K is fou

8 The product spectra from dG, 3'-dGMP, and 5'-dGMP differ from one another, and the spect

9 by NADH follows the sequence dG < d-GpG < 3'-dGMP < 5'-dGMP < DNA; the reverse sequence is observed f

10 dizes 2'-deoxyguanosine 3'-monophosphate (3'-dGMP) stoichiometrically.

11 echanism involves Pt(IV) binding to N7 of 3'-dGMP followed by nucleophilic attack of a 5'-hydroxyl ox

12 The final oxidation product is not 8-oxo-3'-dGMP, but cyclic (5'-O-C8)-3'-dGMP.

13 primarily deoxyguanosine 5'-monophosphate, 5'dGMP, and pyrophosphate-linked dideoxyguanylate, dG5'ppd

14 The product spectra from dG, 3'-dGMP, and 5'-dGMP differ from one another, and the spectrum of the 5'

15 nine radical cations in 2'dG, 3'-dGMP and 5'-dGMP in aqueous LiCl glasses at 143 K is found to result

16 2'-Deoxyguanosine, 3'-dGMP, 5'-dGMP, d-GpG, or double-stranded DNA were exposed to H2O2

17 ng the trend 5'dCMP > 5'-dAMP > 5'dTMP >> 5'-dGMP and 3'-dGMP > 3'-dAMP approximately equal to 3'-dCM

18 llows the sequence dG < d-GpG < 3'-dGMP < 5'-dGMP < DNA; the reverse sequence is observed for ethanol

19 dizes 2'-deoxyguanosine 5'-monophosphate (5'-dGMP) to 7,8-dihydro-8-oxo-2'-deoxyguanosine 5'-monophos

20 2'-deoxyguanosine 5'-monophosphate (8-oxo-5'-dGMP) stoichiometrically.

21 With R283A, a dGMP was incorporated opposite a template thymidine as o

22 wild-type-like selectivity for T.dGMP and A.dGMP mispairs but reduced selectivity for T.dCMP and A.d

23 were readily coupled to morpholine-activated dGMP.

24 P concentration and to be enhanced by adding dGMP to a replication reaction.

25 owever, a significant increase in dCMP.A and dGMP.A mispairs was also observed at the "upstream" 3'-t

26 almost exclusively the insertion of dAMP and dGMP (encoding G --> T and G --> C transversions, respec

27 n, accompanied by lesser amounts of dAMP and dGMP incorporation.

28 ation of 8-oxoG was found to induce dAMP and dGMP insertion opposite the lesion by Kf exo- with trans

29 hesis, preferentially incorporating dAMP and dGMP opposite gamma-OH-PdG.

30 nit alone primarily misincorporated dAMP and dGMP opposite the BaP DE-dG adducts, and incorporated th

31 ide incorporation; the insertion of dAMP and dGMP was favored over that of the correct nucleotide, dC

32 dAMP and dGMP were found to be inserted opposite these OG oxidati

33 acteriophage RB69 (RB69pol) inserts dAMP and dGMP with low efficiency when situated opposite Gh.

34 h small amounts of incorporation of dAMP and dGMP, was detected.

35 ation of dTMP and lesser amounts of dAMP and dGMP.

36 nvolving stable misincorporation of dAMP and dGMP.

37 mounts of misincorporation of dTMP, dAMP and dGMP.

38 d by much smaller amounts of dCMP, dAMP, and dGMP and some one- and two-base deletions.

39 t, promoted small amounts of dTMP, dAMP, and dGMP misincorporation opposite the lesion (total 2.7% of

40 h fidelity, misincorporating dTMP, dAMP, and dGMP opposite a template G target with efficiencies finc

41 C, accompanied by lesser amounts of dCMP and dGMP and some two-base deletions.

42 m aerobic reactions of Fe2+/H2O2 with dG and dGMP, 16 of which were identified.

43 scheme, product inhibition by 8-oxo-dGMP and dGMP and direct binding of these nucleotides to MutT wer

44 Both the dTMP and dGMP kinase reactions are reversible.

45 The enzyme phosphorylates dTMP and dGMP to dTDP and dGDP, respectively, in the presence of

46 both sequence contexts, followed by dTMP and dGMP.

47 The stabilization of dUMP, FdUMP, and dGMP binding to Escherichia coli thymidylate synthase (T

48 tion of guanosine 5'-monophosphate (GMP) and dGMP to guanosine 5'-diphosphate (GDP) and dGDP, respect

49 dducts, the following were identified: 1 BPQ-dGMP adduct, 2 BPQ-dAMP adducts, and 3 BPQ-dCMP adducts.

50 , the structural identities of the novel BPQ-dGMP, BPQ-dAMP, and BPQ-dCMP adducts were confirmed by a

51 The BPQ-dGMP, BPQ-dAMP, and BPQ-dCMP adduct standards were used

52 Noncompetitive inhibition by dGMP and 8-oxo-dGMP indicates an "iso" mechanism in whic

53 e kinase-deficient cells can be prevented by dGMP and dAMP supplementation, providing conclusive evid

54 with small amounts of incorporation of dAMP, dGMP, and dCMP opposite the lesion.

55 orms of the four mononucleotides dAMP, dCMP, dGMP, and dTMP was studied experimentally by equilibrium

56 tive values (< or =-12 kcal mol-1) for dCMP, dGMP, and dTMP and the least negative value for dAMP.

57 binds to the charge-carrying group for dCMP, dGMP, and dTMP.

58 1)) were measured for the insertion of dCMP, dGMP, and dTMP opposite the abasic site using single-tur

59 tate time courses for the insertion of dCMP, dGMP, or dTMP opposite an abasic site were linear.

60 ive relationship between dGDP and both dGTP, dGMP, whereas dTDP appears to have a mixed type of inhib

61 ctively oxidizes the guanine moiety of dGuo, dGMP, and dGTP to 2-Ih, and both peracetic and m-chlorop

62 by oxidation of the monomeric species dGuo, dGMP, and dGTP.

63 Elevated dGMP.G and dTMP.G misincorporation efficiencies of 3.2 x

64 fold higher than that obtained with dGTP for dGMP kinase (1.3 x 10(-4) M), indicating that a higher c

65 ciency equal to 27 and 85% that observed for dGMP-terminated control template-primers.

66 nd 13-fold higher misincorporation rates for dGMP.G, dTMP.G, and dAMP.G mispairs.

67 Never or less-frequently, dGMP, the correct base, was inserted opposite the lesion

68 pes of abasic sites follows the order dAMP > dGMP > dCMP > dTMP.

69 entary dNMP decreases in the order of dAMP > dGMP > dTMP > dCMP, from a high of 5.8 when dAMP is to b

70 ide incorporation followed the order: dAMP > dGMP > dTMP > dCMP, which did not correlate with the mut

71 site dG-AAF followed the order dCMP > dAMP > dGMP > dTMP; the frequency of dNTP insertion opposite th

72 atalytic core of pol eta was found to insert dGMP opposite the mC of the CPD with about a 120:1 selec

73 man DNA polymerase kappa (Pol kappa) inserts dGMP and dCMP within the [T](11) mononucleotide repeat,

74 rrect nucleotide (dTMP) opposite the lesion, dGMP and dAMP were inserted with a comparable frequency.

75 nucleotide, deoxyguanosine 5'-monophosphate (dGMP) by trans-d,l-1,2-diaminocyclohexanetetrachloroplat

76 xGMP incorporation approaches that of native dGMP.

77 ntially incorporated the correct nucleotide, dGMP.

78 lymerase incorporated incorrect nucleotides, dGMP and dAMP, opposite the lesion more preferentially t

79 refore, in the current study, BPQ adducts of dGMP(3'), dAMP(3'), and dCMP(3') were prepared.

80 were observed, along with lesser amounts of dGMP and dTMP incorporations and deletions.

81 -tamoxifen, accompanied by lesser amounts of dGMP.

82 The 10(4.6)-fold weaker binding of dGMP to MutT-Mg(2+) (K(D) = 1.8 mM) slowed the backbone

83 philic attack of a phosphate oxygen at C8 of dGMP.

84 se lesions directed very high frequencies of dGMP misincorporation in E. coli cells.

85 dG-AAF also promoted some incorporation of dGMP and a two-base deletion.

86 cts showed the preferential incorporation of dGMP and dCMP opposite the N(2)-Et-dG lesion, accompanie

87 The incorporation of dGMP increases linearly, while the incorporation of dCMP

88 The incorporation of dGMP is 2.7 +/- 0.5 times greater than the incorporation

89 duct; the Vmax/Kmvalues for incorporation of dGMP were similar in both sequence contexts, whereas the

90 No direct incorporation of dGMP, the correct base, was observed with Y-family enzym

91 f nucleotide incorporation; the insertion of dGMP or dAMP was slightly favored over the insertion of

92 d mechanism involves Pt(IV) binding to N7 of dGMP followed by cyclization via nucleophilic attack of

93 had little effect on the K(I)(sl)(o)(pe) of dGMP or of 8-oxo-dGMP, consistent with the second-sphere

94 0(4.6)-fold lower than the K(I)(sl)(o)(pe)of dGMP (1.7 mM).

95 that gp1.7 catalyses the phosphorylation of dGMP and dTMP to dGDP and dTDP, respectively, by using e

96 proportionately, than the representation of dGMP in vaccinia virus DNA.

97 50-fold, while increasing the K(I)(slope) of dGMP and dAMP less than 2-fold.

98 -oxo-dGMP is 10(4.0)-fold lower than that of dGMP.

99 bypass polymerases to insert dTMP, dAMP, or dGMP opposite 1,N(6)-gamma-HMHP-dA and detected large am

100 addition to the nucleotides (dUMP, FdUMP, or dGMP), a Td of 72 degrees C is achieved and the enthalpy

101 the phosphorylation of either GMP to GDP or dGMP to dGDP and is an essential enzyme in nucleotide me

102 de metabolism, phosphorylating GMP to GDP or dGMP to dGDP.

103 kinetic scheme, product inhibition by 8-oxo-dGMP and dGMP and direct binding of these nucleotides to

104 enzyme to minimize the formation of dA:8-oxo-dGMP at the expense of decreasing the insertion rate of

105 19D mutation also selectively weakened 8-oxo-dGMP binding but only by 37-fold, suggesting that Asn119

106 double mutant weakened the binding of 8-oxo-dGMP by a factor (63,000 +/- 22,000) which overlaps with

107 lectively increased the K(I)(slope) of 8-oxo-dGMP by factors of 17 and 6.6, respectively, indicating

108 This intermediate slowly converts to 8-oxo-dGMP by reacting with solvent H(2)O.

109 hydrogen bonding of the purine ring of 8-oxo-dGMP by the side chains of Asn-119 and Arg-78 may also c

110 phobic nucleotide-binding cleft in the 8-oxo-dGMP complex resulting from a 2.5-4.5 A movement of heli

111 ture of the ternary MutT enzyme-Mg(2+)-8-oxo-dGMP complex showed the proximity of Asn119 and Arg78 an

112 formation of the wild-type MutT-Mg(2+)-8-oxo-dGMP complex slowed the backbone NH exchange rates of 45

113 Formation of the MutT-Mg(2+)-8-oxo-dGMP complex slowed the backbone NH exchange rates of 45

114 ith their locations in the MutT-Mg(2+)-8-oxo-dGMP complex, on opposite sides of the active site cleft

115 ine resulted in a dramatic increase in 8-oxo-dGMP incorporation opposite dA.

116 Noncompetitive inhibition by dGMP and 8-oxo-dGMP indicates an "iso" mechanism in which the nucleotid

117 Similarly, the K(I)(intercept) of 8-oxo-dGMP is 10(4.0)-fold lower than that of dGMP.

118 With Mg(2+)-activated dGTP hydrolysis, 8-oxo-dGMP is a noncompetitive inhibitor with K(I)(sl)(o)(pe)

119 ggesting a more compact structure when 8-oxo-dGMP is bound.

120 , the high affinity of MutT-Mg(2+) for 8-oxo-dGMP likely results from widespread ligand-induced confo

121 the slow steps are the release of the 8-oxo-dGMP product (k4 = 3.9 s(-1)) and the iso step (k5 = 12.

122 solution structure of the MutT-Mg(2+)-8-oxo-dGMP product complex (K(D) = 52 nM) was determined by st

123 The tight binding of 8-oxo-dGMP to MutT (DeltaG degrees = -9.8 kcal/mol) is driven

124 The binding of 8-oxo-dGMP to MutT induces changes in backbone (15)N and NH ch

125 The binding of 8-oxo-dGMP to MutT-Mg(2+) buries 71-78% of the surface area of

126 Direct binding of 8-oxo-dGMP to N119A, monitored by continuous changes in the (1

127 /mol) to the selectivity of binding of 8-oxo-dGMP versus dGMP indicates a 2 order of magnitude smalle

128 ein, and Rv1700 converts 8-oxo-dGDP to 8-oxo-dGMP with a Km of approximately 9.5 muM and Vmax of appr

129 al calorimetric titration of MutT with 8-oxo-dGMP yields a K(D) of 52 nM, in agreement with its K(I)(

130 xo-2'-deoxyguanosine 5'-monophosphate (8-oxo-dGMP) stoichiometrically.

131 , and a K(D) of 237 +/- 130 microM for 8-oxo-dGMP, comparable to its K(I)(slope) of 81 +/- 22 microM.

132 t on the K(I)(sl)(o)(pe) of dGMP or of 8-oxo-dGMP, consistent with the second-sphere enzyme-M(2+)-H(2

133 ly weakened the active site binding of 8-oxo-dGMP, increasing the K(I)(slope) of this product inhibit

134 rg78 than for Asn119 in the binding of 8-oxo-dGMP, likely donating a hydrogen bond to its C6=O group.

135 Arg78 and the modified purine ring of 8-oxo-dGMP, suggesting specific roles for these residues in th

136 type enzyme inefficiently incorporates 8-oxo-dGMP, the substitution of Ser(266) to asparagine resulte

137 With 8-oxo-dGMP, tight binding and slow exchange (n = 1.0 +/- 0.1,

138 a hydrogen bond from the N7H group of 8-oxo-dGMP, while Asp119 functioned as only an acceptor.

139 s (8-oxo-dGTP-ases) that convert it to 8-oxo-dGMP.

140 with the ability of TthPolX to insert 8-oxo-dGMP.

141 of Asn119 and Arg78 in the binding of 8-oxo-dGMP.

142 hydrolyzes specifically 8-oxo-dGTP to 8-oxo-dGMP.

143 ions and -1 frameshift mutations within poly(dGMP) and poly(dAMP) runs.

144 MP does not alter the Td of the enzyme since dGMP alone does not bind to TS.

145 around 0.5 muM in the presence of substrate dGMP.

146 particular base substitution in vivo (e.g. T-dGMP or A-dCMP for T to C transitions), L612M pol delta

147 groove, has wild-type-like selectivity for T.dGMP and A.dGMP mispairs but reduced selectivity for T.d

148 This substrate was designed so that dGMP and dCMP were exclusively incorporated into the lea

149 ultistep conversion of hypoxanthine (Hyp) to dGMP for DNA synthesis.

150 selectivity of binding of 8-oxo-dGMP versus dGMP indicates a 2 order of magnitude smaller contributi

151 (T4G4)2 reveals modest retardation vis-a-vis dGMP, which rules out quadruplex formation by the telome

152 FdUMP shows a similar profile, while dGMP does not alter the Td of the enzyme since dGMP alon

153 ly distributed throughout the protein, while dGMP binding induces smaller changes in only 22 residues

154 heme, (1)H-(15)N HSQC titration of MutT with dGMP reveals weak binding and fast exchange from one sit