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 the bacteriophage T4 DNA polymerase and the Klenow fragment.

5 teraction with the exonuclease domain of the Klenow fragment.

6 nucleotides by reverse transcriptase or the Klenow fragment.

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

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

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

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

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

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

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

14 similarly by the polymerization unit of the Klenow fragment.

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

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

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

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

19 photoaffinity label of the DNA polymerase I Klenow fragment.

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

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

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

23 Interestingly, the replacement of lKF with Klenow Fragment (3'-5' exo-) (KFexo-) prevented the gene

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

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

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

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

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

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

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

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

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

33 Klenow fragment and DNA polymerase beta showed no discon

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

57 Klenow fragment could not bypass any of the photoproduct

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

59 Analysis of mutant Klenow fragment derivatives indicates that discriminatio

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

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

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

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

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

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

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

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

68 18-A long H-bonding track contributed by the Klenow fragment equivalent of Asn(845), Gln(849), Arg(66

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

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

71 Whereas pol alpha and Klenow fragment exhibited minimal discrimination against

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

128 ated that if ICSDPR was catalyzed with Large Klenow Fragment (lKF), the canonical duplex and some byp

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

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

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

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

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

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

135 e-encoded DNA polymerases, homologous to the Klenow fragment of bacterial DNA polymerase I that inclu

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

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

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

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

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

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

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

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

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

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

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

147 On the other hand, the highly homologous Klenow fragment of DNA polymerase I containing an engine

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

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

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

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

152 The Klenow fragment of DNA polymerase I from Escherichia col

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

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

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

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

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

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

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

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

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

162 exhibit reasonably good efficiency with the Klenow fragment of DNA polymerase I, and we identify the

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

186 The Klenow fragment of Escherichia coli DNA polymerase I cat

187 The Klenow fragment of Escherichia coli DNA polymerase I hou

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

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

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

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

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

193 The Klenow fragment of Escherichia coli DNA polymerase I the

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

216 and their evolved variants, focusing on the Klenow fragment of Taq DNA polymerase (Klentaq).

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

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

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

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

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

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

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

224 e structure and dynamics of DNA polymerase I Klenow Fragment (Pol) substrates both alone and in DNA-P

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

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

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

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

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

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

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

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

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

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

235 In Klenow fragment the templating base is more rigidly held

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

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

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

239 ing Escherichia coli DNA polymerase I or the Klenow fragment to Cas9 greatly increases the frequencie

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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