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 e bound at each the 5'- and 3'-end of the 5'-dGMP-fill-in PDGFR-B vG4.

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

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

24 were readily coupled to morpholine-activated dGMP.

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

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

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

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

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

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

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

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

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

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

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

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

37 nvolving stable misincorporation of dAMP and dGMP.

38 mounts of misincorporation of dTMP, dAMP and dGMP.

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

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

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

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

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

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

45 Both the dTMP and dGMP kinase reactions are reversible.

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

47 both sequence contexts, followed by dTMP and dGMP.

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

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

50 ent in the PDGFR-beta promoter sequence, and dGMP favors the 5'-end fill-in.

51 ically relevant guanine metabolites, such as dGMP, GMP, and cGMP, as well as guanine-derivative drugs

52 d stabilized by guanine metabolites, such as dGMP.

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

72 and ZmPTPN release Pi by hydrolyzing GDP/GMP/dGMP/IMP/dIMP, and that AtPTPN positively regulated AsA

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

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

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

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

77 electrostatic interactions, and the fill-in dGMP is covered and well-protected by berberine.

78 berberine covers and stabilizes the fill-in dGMP.

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

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

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

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

83 xGMP incorporation approaches that of native dGMP.

84 ntially incorporated the correct nucleotide, dGMP.

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

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

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

88 -tamoxifen, accompanied by lesser amounts of dGMP.

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

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

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

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

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

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

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

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

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

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

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

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

101 0(4.6)-fold lower than the K(I)(sl)(o)(pe)of dGMP (1.7 mM).

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

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

104 50-fold, while increasing the K(I)(slope) of dGMP and dAMP less than 2-fold.

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

106 nd hPol eta preferentially inserts a dAMP or dGMP nucleotide into primer-templates across from the 6-

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

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

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

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

111 ine analogues that target the PDGFR-B vG4 or dGMP-fill-in vG4.

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

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

114 19D mutation also selectively weakened 8-oxo-dGMP binding but only by 37-fold, suggesting that Asn119

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

141 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

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

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

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

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

146 MTH1 hydrolyzes 8-oxo-dGTP to 8-oxo-dGMP, thereby avoiding 8-oxo-dG incorporation into DNA.

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

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

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

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

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

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

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

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

155 d the 3' hydroxyl group of the primer strand dGMP across from 6-oxo-M(1)dG is not positioned correctl

156 around 0.5 muM in the presence of substrate dGMP.

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

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

159 lso show primer-templates with a 3'-terminal dGMP or dAMP across from 6-oxo-M(1)dG were extended to a

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

161 We determined the NMR structure of the dGMP-fill-in PDGFR-beta vG4 in K(+) solution.

162 a ternary complex of berberine bound to the dGMP-fill-in PDGFR-B vG4 in potassium solution.

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

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

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

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

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

168 es across from the 6-oxo-M(1)dG adduct, with dGMP being slightly preferred.

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