ライフサイエンスコーパス: Klenow fragment

1 the exonuclease-deficient DNA polymerase I (Klenow fragment).

2 rand by either E.coli RNA or DNA polymerase (Klenow fragment).

3 agment of Escherichia coli DNA polymerase I (Klenow fragment).

4 teraction with the exonuclease domain of the Klenow fragment.

5 nucleotides by reverse transcriptase or the Klenow fragment.

6 during DNA synthesis catalyzed by the exo(-) Klenow fragment.

7 rase domain of a 3'-5'-exonuclease-deficient Klenow fragment.

8 trand were used as substrates for binding to Klenow fragment.

9 merase and 3'-5' exonuclease active sites of Klenow fragment.

10 tail in the presence of excess dATP and the Klenow fragment.

11 illing recessed 3'-ends using DNA polymerase Klenow fragment.

12 similarly by the polymerization unit of the Klenow fragment.

13 includes helix O in the finger motif of the Klenow fragment.

14 P) or dCMP by the 3'-->5' exonuclease of the Klenow fragment.

15 base occupies in the p(dT)3 complex with the Klenow fragment.

16 polymerase, a property not observed with the Klenow fragment.

17 photoaffinity label of the DNA polymerase I Klenow fragment.

18 of the template-primer binding sites on the Klenow fragment.

19 f POLN was higher than exonuclease-deficient Klenow fragment.

20 DNA polymerases nu, zeta, and kappa and the Klenow fragment.

21 rporation of dNTPs into DNA by pol alpha and Klenow fragment.

22 the bacteriophage T4 DNA polymerase and the Klenow fragment.

23 ied using Escherichia coli DNA polymerase I (Klenow fragment, 3'-exonuclease deficient) and natural d

24 stigated: mesophilic DNA polymerase I large (Klenow) fragment, 3'-->5' exo(-) Klenow DNA polymerase,

25 The R668A mutation of Klenow fragment abolished this requirement, identifying

26 nuclease-deficient E. coli DNA polymerase I (Klenow fragment) across from either the (+)-trans- or th

27 In Klenow fragment, an A-family DNA polymerase, the steric

28 -purine, Tg is more likely to be bypassed by Klenow fragment, an A-family DNA polymerase.

29 disrupted favorable interactions between the Klenow fragment and a duplex containing a matched termin

30 However, DNA polymerase I Klenow fragment and avian myeloblastosis virus reverse t

31 Here, we show that both Klenow fragment and DNA polymerase alpha can utilize 8-o

32 Klenow fragment and DNA polymerase beta showed no discon

33 TPs and ddNTPs were determined for wild-type Klenow fragment and for mutant derivatives that showed c

34 eversible inhibitors of the DNA polymerase I Klenow fragment and HIV I reverse transcriptase.

35 suggests that the hydrogen bond between the Klenow fragment and O6mG is more important in the incorp

36 plished by a random synthesis reaction using Klenow fragment and random hexamers tagged with a T7 pri

37 n contrast, pol A family polymerases such as Klenow fragment and T7 DNA polymerase only insert dPMP e

38 structures of the exonuclease domains of the Klenow fragment and the T4 DNA polymerase and the recent

39 s (K(i)) for a weak competitive inhibitor of Klenow fragment and two strong noncompetitive inhibitors

40 enesis of Escherichia coli DNA polymerase I (Klenow fragment) and atomic substitution of the DNA.

41 cillus fragment polymerase (homologue of the Klenow fragment) and LdG-DNA duplex elucidate the struct

42 with high-fidelity DNA polymerases, such as Klenow fragment, and include a step that may be related

43 bypassed by an exonuclease-deficient (exo-) Klenow fragment, and termination occurred primarily oppo

44 ction of nucleotides by both pol eta and the Klenow fragment, and the lesser role of shape selection

45 The kinetic data obtained with the Klenow fragment are compared to that of the high-fidelit

46 deficient Escherichia coli DNA polymerase I (Klenow fragment) bound to primer-templates containing ei

47 ased misinsertion rate relative to wild-type Klenow fragment, but a decreased rate of extension from

48 Photoaffinity labeling of the Klenow fragment by 1 yielded a single radiolabeled trypt

49 ve for photoincorporation of [3H]-1 into the Klenow fragment by a factor of 2, indicating a competiti

50 dy show that in addition to base mismatches, Klenow fragment can also recognize irregularities in the

51 lower fidelity of Pol nu compared to that of Klenow fragment can be attributed primarily to a much lo

52 tion binding assay, we have established that Klenow fragment contacts at least the first four unpaire

53 omplex of Escherichia coli DNA polymerase I (Klenow fragment), containing the template-primer and dNT

54 steric rejection was greater than DNA pol I Klenow fragment, correlating with the higher fidelity of

55 E. coli DNA polymerase I Klenow fragment could employ 1-me-dATP as a precursor fo

56 Klenow fragment could not bypass any of the photoproduct

57 In this study, nine Klenow fragment derivatives containing mutations within

58 Analysis of mutant Klenow fragment derivatives indicates that discriminatio

59 ly resembles the corresponding region in the Klenow fragment despite minimal sequence identity.

60 gnificantly less than that of mutants in the Klenow fragment, despite the nearly identical geometric

61 A mutant derivative of Klenow fragment DNA polymerase containing serine substit

62 nt at C-3' of the ribose moiety, and yet the Klenow fragment DNA polymerase prefers the natural (dNTP

63 We previously identified five derivatives of Klenow fragment DNA polymerase that have lower fidelity

64 In Klenow fragment DNA polymerase, a flexible 50-amino acid

65 We demonstrated that the Klenow fragment (DNA polymerase I) performs translesion

66 of a single ribonucleotide to a DNA primer, Klenow fragment does not efficiently synthesize pure RNA

67 18-A long H-bonding track contributed by the Klenow fragment equivalent of Asn(845), Gln(849), Arg(66

68 structures of template-primer-bound KlenTaq (Klenow fragment equivalent of Thermus aquaticus polymera

69 Both pol alpha and Klenow fragment exhibit a remarkable inability to discri

70 Whereas pol alpha and Klenow fragment exhibited minimal discrimination against

71 onstructs, Escherichia coli DNA polymerase I Klenow Fragment exo(-) is much less effective in expandi

72 primer extension studies were conducted with Klenow fragment exo(-).

73 n subjected to primer extension catalyzed by Klenow fragment exo- (Kf exo-), calf thymus DNA polymera

74 dG-C8-(acetylamino)fluorene, indicating that Klenow fragment exo- activity is not greatly affected by

75 The kinetics of primer extension by Klenow fragment exo- at template positions 3' to the les

76 tions were performed using DNA polymerase I, Klenow fragment exo-.

77 iphosphate is accepted as a substrate by the Klenow fragment (exo(-)) of DNA polymerase I from E. col

78 Primer extension studies using the Klenow fragment (exo(-)) of Escherichia coli DNA polymer

79 tes for DNA polymerase alpha (pol alpha) and Klenow fragment (exo-) of DNA polymerase I (Escherichia

80 el enzyme, Escherichia coli DNA polymerase I Klenow fragment (exo-).

81 Kinetics studies with DNA Pol I (Klenow fragment, exonuclease-deficient) in vitro showed

82 ost other high-fidelity DNA polymerases, the Klenow fragment follows the "A-rule" of translesion DNA

83 concentrations of poly(dA).(T)10 protect the Klenow fragment from [3H]-1 photoincorporation, and TTP

84 nsequence-specific DNA-binding proteins, the Klenow fragment from DNA polymerase I and Klenow exonucl

85 e basis of their sequence alignment with the Klenow fragment from Escherichia coli DNA polymerase I.

86 enase 2.0, and 3'-->5' exonuclease-deficient Klenow fragment greatly decreased the production of fram

87 y, the photoincorporation of [3H]-1 into the Klenow fragment has an absolute requirement for magnesiu

88 amination of the kinetic data suggested that Klenow fragment has an extremely low tolerance of even m

89 onstrates that photoprobe 1 does bind to the Klenow fragment in the absence of template-primer and th

90 Asp(705) and Asp(882), of DNA polymerase I (Klenow fragment) in the early prechemistry steps that pr

91 ss by the Escherichia coli DNA polymerase I (Klenow fragment) in the presence of these templates.

92 obes, only nucleotide 1 photoinactivates the Klenow fragment; in the presence of a 200-fold excess of

93 th that of Escherichia coli DNA polymerase I Klenow fragment indicated a high degree of amino acid se

94 itro studies using E. coli DNA polymerase I (Klenow fragment)indicated that both adducts were effecti

95 modeling of the template strand overhang in Klenow fragment, indicated its binding in the region spa

96 The principle is based on DNA polymerase I (Klenow fragment)-induced coupling of the nucleotide-modi

97 Klenow fragment inserts dGTP with a 4-9-fold higher prob

98 is approach was also used to examine how the Klenow fragment interacts with the 3-position of the mut

99 e two proteins: (I) the OH of Tyr-497 in the Klenow fragment interacts with the scissile phosphate in

100 this preference in order to investigate how Klenow fragment interacts with the sugar portion of an i

101 this study suggests a mechanism whereby the Klenow fragment is able to recognize polymerase errors f

102 that the exonucleolytic cleavage activity of Klenow fragment is correlated with the increased level o

103 AG)4 is extended with proofreading-defective Klenow fragment (KF exo-) from Escherichia coli DNA poly

104 , using the proofreading-deficient mutant of Klenow fragment (KF(-)) DNA polymerase.

105 single-stranded DNA by the Escherichia coli Klenow fragment (KF) 3'-5' exonuclease and snake venom p

106 chimeric DNA-RNA oligonucleotides using the Klenow fragment (KF) and two other DNA polymerases, from

107 B family replicative DNA polymerases and the Klenow fragment (KF) as an example of a repair DNA polym

108 se of the template in P/T DNA complexes with Klenow fragment (KF) DNAP as the polymerase moves throug

109 Here, individual DNA polymerase I Klenow fragment (KF) molecules were tethered to a single

110 the 3'-5' exonucleolytic active site of the Klenow fragment (KF) of DNA polymerase I from Escherichi

111 size as recently found for the high-fidelity Klenow fragment (Kf) of Escherichia coli DNA Pol I.

112 ymerase domains of Taq polymerase and of the Klenow fragment (KF) of Pol I are almost identical, wher

113 751) located in the fingers subdomain of the Klenow fragment (KF) polymerase.

114 etic analyses to a high-fidelity polymerase, Klenow fragment (KF), and a low-fidelity polymerase, Afr

115 bonding network in the catalytic function of Klenow fragment (KF), we generated N845A, N845Q, Q849A,

116 DNA adducts positioned in the active site of Klenow fragment (KF).

117 en the pol and exo sites of DNA polymerase I Klenow fragment (KF).

118 inserted into replicating DNA strands by the Klenow fragment (KF, exo- mutant) of Escherichia coli DN

119 ese substrates with yeast polymerase eta and Klenow fragment (KF-).

120 nstants for the binding of DNA polymerase I (Klenow fragment) (KF) to the primer-templates containing

121 nuclease-deficient E. coli DNA polymerase I (Klenow fragment) (KF) when (+)-trans- or (+)-cis-B[a]P-N

122 aelis complex between the large fragment (or Klenow fragment, KF) and a single-stranded DNA substrate

123 template strands on the formation of Pol I (Klenow fragment, KF)/template-primer complexes has been

124 alyzed by polymerase alpha and polymerase I (Klenow fragment, lack of exonuclease activity) but not w

125 strate for the model enzyme DNA polymerase I Klenow fragment lacking proofreading activity, Kf (exo-)

126 Bypass of the nonadjacent dimer by exo(-) Klenow fragment led primarily to a single-nucleotide del

127 Arg668 of Escherichia coli DNA polymerase I (Klenow fragment) makes a critical contact with the N-3-p

128 ed that N(4)-CMdC was a stronger blockade to Klenow fragment-mediated primer extension than N(6)-CMdA

129 ndividual Escherichia coli DNA polymerase I (Klenow fragment) molecules performing substrate selectio

130 l those for the Klenow fragment, whereas the Klenow fragment more strongly discriminates against mism

131 e analogue pairings were better tolerated by Klenow fragment mutants having more spacious active site

132 Relative to wild type, several Klenow fragment mutants showed substantially more discri

133 The Klenow fragment of DNA polymerase I (an A-family polymer

134 zine (tCo) by human DNA polymerase alpha and Klenow fragment of DNA polymerase I (Escherichia coli).

135 ophage T7 DNA polymerase (T7DNAP) and by the Klenow fragment of DNA polymerase I (KF).

136 )(4) repeat sequence and replicated with the Klenow fragment of DNA polymerase I (Kf).

137 A structure upon the interaction between the Klenow fragment of DNA polymerase I and a series of defi

138 rent than that previously determined for the Klenow fragment of DNA polymerase I and is consistent wi

139 owever, the RNA aptamers did not inhibit the Klenow fragment of DNA polymerase I and only had a minor

140 used to examine the interaction between the Klenow fragment of DNA polymerase I and synthetic DNA pr

141 ucleotide repeats were also studied with the Klenow fragment of DNA polymerase I and with T4 DNA poly

142 n vitro elongation of these complexes by the Klenow fragment of DNA polymerase I at 37 degrees C.

143 The Klenow fragment of DNA polymerase I can then cleanly and

144 NA and their reactions with the 3'-5' exo(-) Klenow fragment of DNA polymerase I demonstrate the usef

145 veloped based on intensive studies using the Klenow fragment of DNA polymerase I from E. coli (Kf) an

146 Steady-state kinetic experiments using the Klenow fragment of DNA polymerase I from E. coli suggest

147 in the polymerase reaction catalyzed by the Klenow fragment of DNA polymerase I from Escherichia col

148 The Klenow fragment of DNA polymerase I from Escherichia col

149 ism of the 3'-5' exonuclease activity of the Klenow fragment of DNA polymerase I has been investigate

150 s 5'-triphosphate (dPTP) by exonuclease-free Klenow fragment of DNA polymerase I have been determined

151 rporated into DNA using the exonuclease-free Klenow fragment of DNA polymerase I in a primer extensio

152 Bioconjugating single molecules of the Klenow fragment of DNA polymerase I into electronic nano

153 A mechanism by which the Klenow fragment of DNA polymerase I monitors the geometr

154 se I digested DNA with T4 DNA ligase and the Klenow fragment of DNA polymerase I suggest that single-

155 ause it involves on-slide application of the Klenow fragment of DNA polymerase I to extend unmodified

156 When the 3'-->5' exonuclease free (exo-) Klenow fragment of DNA polymerase I was used, dG-N2-3MeE

157 to determine the polymerization rate of the Klenow fragment of DNA polymerase I, and we demonstrate

158 various DNA polymerases: Taq DNA polymerase, Klenow fragment of DNA polymerase I, DNA Sequence, DNA p

159 Compared to the Klenow fragment of DNA polymerase I, Sequenase could rea

160 ave been measured with four polymerases, the Klenow fragment of DNA polymerase I, the Klenow fragment

161 tivity with that of exo-nuclease III and the Klenow fragment of DNA polymerase I.

162 (C-PdG-C and T-PdG-T) were replicated by the Klenow fragment of DNA polymerase I.

163 Taking advantage of the ability of the Klenow fragment of DNA polymerase to accept templates wi

164 sion; however, when encountered by the exo(-)Klenow fragment of DNA polymerase, dAMP (22%), TMP (16%)

165 The Klenow fragment of E. coli DNA polymerase I selects its

166 We determined the ability of the Klenow fragment of E. coli DNA polymerase I to synthesiz

167 rning the rate of 3'-end proofreading by the Klenow fragment of E. coli DNA polymerase I.

168 by 2 reverse transcriptases and also by the Klenow fragment of E. coli DNA polymerase I.

169 otides) similar to the exonuclease-deficient Klenow fragment of E. coli pol I, is inhibited by dideox

170 ely, but not those of DNA polymerase beta or Klenow fragment of E.coli DNA polymerase I.

171 studies of 1 and 2 were carried out with the Klenow fragment of Escherichia coli DNA Pol I (exo-) in

172 olymerases such as the exonuclease-deficient Klenow fragment of Escherichia coli DNA polymerase I (ex

173 ne) has been investigated in the presence of Klenow fragment of Escherichia coli DNA polymerase I (Kf

174 man DNA polymerase alpha (pol alpha) and the Klenow fragment of Escherichia coli DNA polymerase I (KF

175 The Klenow fragment of Escherichia coli DNA polymerase I (KF

176 the dwell time for complexes of DNA with the Klenow fragment of Escherichia coli DNA polymerase I (KF

177 We use the Klenow fragment of Escherichia coli DNA polymerase I (KF

178 solved fluorescence experiments and uses the Klenow fragment of Escherichia coli DNA polymerase I (KF

179 a 3'-->5' exonuclease-deficient form of the Klenow fragment of Escherichia coli DNA polymerase I as

180 d that an exonuclease-free derivative of the Klenow fragment of Escherichia coli DNA polymerase I can

181 The Klenow fragment of Escherichia coli DNA polymerase I cat

182 The Klenow fragment of Escherichia coli DNA polymerase I hou

183 In contrast, neither the Klenow fragment of Escherichia coli DNA polymerase I nor

184 primer extension reactions catalyzed by the Klenow fragment of Escherichia coli DNA polymerase I or

185 ed G[8-5m]T, and our results showed that the Klenow fragment of Escherichia coli DNA polymerase I sto

186 Similarly, the Klenow fragment of Escherichia coli DNA polymerase I ten

187 To identify the sites in the Klenow fragment of Escherichia coli DNA polymerase I tha

188 The Klenow fragment of Escherichia coli DNA polymerase I the

189 be efficiently incorporated into DNA by the Klenow fragment of Escherichia coli DNA polymerase I whe

190 his unnatural base pair is replicated by the Klenow fragment of Escherichia coli DNA polymerase I wit

191 extended was examined with the high-fidelity Klenow fragment of Escherichia coli DNA polymerase I wit

192 he hydrogen bonding interactions between the Klenow fragment of Escherichia coli DNA polymerase I wit

193 conducted with either Taq polymerase or the Klenow fragment of Escherichia coli DNA polymerase I, bo

194 With the Klenow fragment of Escherichia coli DNA polymerase I, sy

195 tensions in vitro using DNA polymerases (the Klenow fragment of Escherichia coli DNA polymerase I, th

196 /(CA)(7)C, T(9)/A(30), T(20)/A(30)] with the Klenow fragment of Escherichia coli DNA polymerase I, we

197 and a set of Cy3-labeled nucleotides by the Klenow fragment of Escherichia coli DNA polymerase I.

198 than for the A family, exonuclease-deficient Klenow fragment of Escherichia coli DNA polymerase I.

199 d by the 3' --> 5' exonuclease-free (exo(-)) Klenow fragment of Escherichia coli DNA polymerase I.

200 l nu's more accurate A-family homologue, the Klenow fragment of Escherichia coli DNA polymerase I.

201 n synthesis mediated by the exonuclease-free Klenow fragment of Escherichia coli DNA polymerase I.

202 Moloney murine leukemia virus RT but not the Klenow fragment of Escherichia coli DNA polymerase I.

203 ns catalyzed by the 3'-->5' exonuclease-free Klenow fragment of Escherichia coli DNA polymerase I.

204 Sequenase (modified T4 DNA polymerase), the Klenow fragment of Escherichia coli DNA polymerase, and

205 lesional synthesis in vitro catalyzed by the Klenow fragment of Escherichia coli Pol I (exo(-)) was i

206 talyzed by the 3'-->5' exonuclease-deficient Klenow fragment of Escherichia coli pol I, revealed limi

207 NA polymerase was studied in vitro using the Klenow fragment of Escherichia coli polymerase I (Kf exo

208 in vitro using human polymerase beta and the Klenow fragment of Escherichia coli polymerase I.

209 For both DNA pol gamma and the Klenow fragment of pol I, the enzyme-dRP intermediate is

210 imer extension experiments revealed that the Klenow fragment of polymerase I catalyzes error-prone sy

211 Two polymerases were used in this work: the Klenow fragment of the Escherichia coli DNA polymerase I

212 RET measurements, we show that Klentaq1 (the Klenow fragment of Thermus aquaticus DNA polymerase 1) i

213 ease site of the large proteolytic fragment (Klenow fragment) of DNA polymerase I.

214 or the movement of E. coli DNA polymerase I (Klenow fragment) on a DNA template during DNA synthesis

215 extension with 3'-->5'exonuclease-deficient Klenow fragment or T4 polymerase and dNTPs or by enzymat

216 bitor of DNA synthesis by pol eta but not by Klenow fragment or T7 DNA polymerase.

217 m and dynamics by which the Escherichia coli Klenow fragment performs translesion DNA synthesis durin

218 howed mixed noncompetitive inhibition of the Klenow fragment polymerase activity versus poly(dA).(T)1

219 avenger, photoprobe 1 inactivates 92% of the Klenow fragment polymerase activity with saturation obse

220 vestigated conformational transitions in the Klenow fragment polymerase reaction by stopped-flow fluo

221 The Klenow fragment promotes blunt end addition of dAMP; thi

222 oned in the active site of DNA polymerase I (Klenow fragment), serve as donor fluorophores to an acce

223 DNA polymerase I large (Klenow) fragment showed no detectable polymerization pro

224 We screened mutant derivatives of Klenow fragment so as to identify those amino acid resid

225 However, unlike the Klenow fragment, T7 gene 5 protein binds tightly to E. c

226 Like the Klenow fragment, T7 gene 5 protein has both DNA polymera

227 ired dNTP in the Dbh active site, whereas in Klenow fragment the mispaired dNTP sits higher in the ac

228 In Klenow fragment the templating base is more rigidly held

229 isons are made to recent data for DNA pol I (Klenow fragment), the archaeal polymerase Dpo4, and huma

230 ranslesion synthesis catalyzed by the exo(-) Klenow fragment, the expected three-base deletion was fo

231 with RB69 DNA polymerase, in contrast to the Klenow fragment, there is no inhibition of the primer-ex

232 t account for the inability of pol alpha and Klenow fragment to discriminate against unnatural bases.

233 -primer challenge and (b) the ability of the Klenow fragment to form ternary complexes in the presenc

234 R455A mutations disrupted the ability of the Klenow fragment to melt duplex DNA and bind the frayed t

235 ell as oxanine itself can be incorporated by Klenow Fragment to pair with oxanine in a DNA template w

236 inding of Escherichia coli DNA polymerase I (Klenow fragment) to a primer-template is stabilized by t

237 deficient Escherichia coli DNA polymerase I (Klenow fragment) to DNA primer-templates modified with a

238 and kinetics of binding of DNA Polymerase I (Klenow fragment) to DNA.

239 duplex DNA was induced by DNA polymerase I (Klenow fragment) to preserve Watson-Crick base-pairing r

240 erichia coli UvrD helicase, DNA polymerase I Klenow fragment, two accessory proteins, MutL and single

241 utants of Escherichia coli DNA polymerase I (Klenow fragment) were used to study DNA synthesis on DNA

242 tson-Crick base pairs parallel those for the Klenow fragment, whereas the Klenow fragment more strong

243 rporated, in contrast to the behavior of the Klenow fragment which cannot use dCDP as a substrate.

244 Photolabel [3H]-1 covalently labeled the Klenow fragment with photolysis at 300 nm, reaching satu

245 so reveals two interesting properties of the Klenow fragment with regard to enzyme-template-primer bi

246 the Klenow fragment of DNA polymerase I, the Klenow fragment with the proof-reading exonuclease inact

247 a defined site in a template was examined on Klenow fragments with and without 3' --> 5' exonuclease

248 s when a binary complex of DNA polymerase I (Klenow fragment) with a primer-template binds a compleme