ライフサイエンスコーパス: RFC

1 RFC 80A and 5-aminoimidazole-4-carboxamide ribonucleotid

2 RFC and PCNA dramatically activate polymerase delta-medi

3 RFC consists of five subunits in a spiral arrangement (R

4 RFC does not appreciably destabilize the closed state of

5 RFC is characterized by 12 transmembrane domains (TMDs),

6 RFC subunits belong to the AAA(+) superfamily, and their

7 RFC was expressed in mouse Muller cells that had been al

8 RFC-C-dependent activation of RFC also enables ptDNA bin

9 inity for the reduced folate carrier type 1 (RFC-1).

10 tive enables assessment of individual RFC-A, RFC-B, RFC-C, RFC-D, and RFC-E subunit functions in the

11 M. acetivorans RFC (RFC(Ma)), which represents an intermediate between

12 own that ptDNA entry inside an ATP-activated RFC-PCNA complex accelerates clamp opening and ATP hydro

13 the PCNA loading mechanism that occur after RFC binds ATP.

14 strand, and CMG protects Pol epsilon against RFC inhibition on the leading strand.

15 LG1 distinct from its role as an alternative RFC complex because knockdowns of any other RFC subunits

16 g depends on the Elg1-containing alternative RFC complex, ubiquitination of PCNA, and the checkpoint

17 any other RFC subunits or other alternative RFCs did not affect PCNA monoubiquitination.

18 Thus, hpr-17 defines an RFC-like complex that facilitates telomerase activity in

19 e plasma membrane expression of FR-alpha and RFC transporter isoforms without affecting global protei

20 an extended interface between the clamp and RFC.

21 ) that most likely include clamp closing and RFC dissociation.

22 f individual RFC-A, RFC-B, RFC-C, RFC-D, and RFC-E subunit functions in the reaction mechanism.

23 n II (CFII) included pol delta, pol eta, and RFC.

24 plication are common features of FAM111A and RFC, IRF2 is a transcriptional regulator.

25 PI-1 protein and the host IRF2, FAM111A, and RFC complex likely form an interaction network that infl

26 This interaction among ZMP, folates, and RFC, a folate/organic phosphate antiporter, is consisten

27 regulating the interaction between hLigI and RFC, which is required for efficient DNA replication and

28 ndent upon the interaction between hLigI and RFC.

29 h high nitrate concentration but that LR and RFC may better describe bulk conditions in the aquifer.

30 PCFT and RFC produced comparable increases in pemetrexed activity

31 and of HepG2 cells expressing both PCFT and RFC.

32 variously transported by FRalpha, PCFT, and RFC and, unlike PMX, inhibited de novo purine nucleotide

33 These could be replaced by purified PCNA and RFC to retain full activity.

34 polymerase alpha in the presence of PCNA and RFC.

35 is that requires polymerase delta, PCNA, and RFC and support a role for aRPA in DNA repair.

36 without Msh2-Msh6 (or Msh2-Msh3), PCNA, and RFC but did not require nicking of the substrate, follow

37 d ATP hydrolysis upon contact with ptDNA and RFC-D Arg-101 serving as a brake that confers specificit

38 an intermediate between the common archaeal RFC and the eukaryotic RFC, comprises two different smal

39 ts of five subunits in a spiral arrangement (RFC-A, -B, -C, -D, and -E, corresponding to subunits RFC

40 subunit response to ATP binding decreases as RFC-C>RFC-D>RFC-B, with RFC-A being unnecessary.

41 ables assessment of individual RFC-A, RFC-B, RFC-C, RFC-D, and RFC-E subunit functions in the reactio

42 eaction, particularly at a checkpoint before RFC commits to ATP hydrolysis.

43 lta), loaded PCNA is captured from DNA-bound RFC which subsequently dissociates, leaving behind the h

44 tion assay showed that the PCNA assembled by RFC is functional.

45 CNA is bound by Rad24-RFC than when bound by RFC.

46 ill unclear how recognition of primed DNA by RFC triggers ATP hydrolysis and how hydrolysis leads to

47 es not interact with and is not inhibited by RFC, demonstrating that inhibition of ligation is depend

48 he addition of PCNA alleviates inhibition by RFC.

49 esenting a general model for PCNA loading by RFC in archaea and eukaryotes.

50 Analysis of PCNA opening by RFC revealed a two-step reaction in which RFC binds PCNA

51 DNA polymerase delta that loading of PCNA by RFC targets DNA polymerase delta to the D loop formed by

52 g may relate to the opening of PCNA rings by RFC during the loading reaction.

53 igen (PCNA) loading by replication factor C (RFC) acts as the initial sensor of telomere damage to es

54 ar antigen (PCNA), and replication factor C (RFC) and a reconstituted Mlh1-Pms1-dependent 3' nick-dir

55 uclear antigen (PCNA), replication factor C (RFC) and DNA polymerase delta.

56 s loaded around DNA by replication factor C (RFC) and functions in DNA replication and repair.

57 actions that contained replication factor C (RFC) and proliferating cell nuclear antigen (PCNA) were

58 The eukaryotic replication factor C (RFC) clamp loader is an AAA+ spiral-shaped heteropentame

59 We find that the replication factor C (RFC) clamp loader specifically inhibits Pol epsilon on t

60 ccharomyces cerevisiae replication factor C (RFC) clamp loader, respectively, and assessed the impact

61 e loaded onto DNA by a replication factor C (RFC) clamp loader.

62 mprises an alternative replication factor C (RFC) complex and plays an important role in preserving g

63 The multi-subunit replication factor C (RFC) complex loads circular proliferating cell nuclear a

64 loaded onto DNA by the replication factor C (RFC) complex, which consists of five distinct subunits (

65 on between subunits in replication factor C (RFC) from Archaeoglobus fulgidus.

66 vorans clamp loader or replication factor C (RFC) homolog.

67 Replication factor C (RFC) is a five-subunit complex that loads proliferating

68 en loading onto DNA by replication factor C (RFC) is a key step in eukaryotic DNA replication and rep

69 Replication factor C (RFC) is an AAA+ heteropentamer that couples the energy o

70 al that ATP binding to replication factor C (RFC) is sufficient for loading the heterotrimeric PCNA12

71 ccharomyces cerevisiae replication factor C (RFC), and present the first kinetic model of a eukaryoti

72 revisiae clamp loader, replication factor C (RFC), and the DNA damage checkpoint clamp loader, Rad24-

73 de extracts identified replication factor C (RFC), proliferating cell nuclear antigen (PCNA), and pol

74 th and is inhibited by replication factor C (RFC), the clamp loader complex that loads PCNA onto DNA.

75 NA sliding clamp, and, replication factor C (RFC), the clamp loader.

76 lear antigen (PCNA) in replication factor C (RFC)-catalyzed loading of the clamp onto primer template

77 e demonstrate that the replication factor C (RFC)-CTF18 clamp loader (RFC(CTF18)) controls the veloci

78 cc1, the subunits of a Replication Factor C (RFC)-like complex, are essential for the perinuclear pos

79 der molecular machine, replication factor C (RFC).

80 ll nuclear antigen and replication factor C (RFC).

81 ity of a clamp-loader [replication factor C (RFC)] complex and the energy derived from ATP hydrolysis

82 igen (PCNA, clamp) and replication factor C (RFC, clamp loader), we have examined the assembly of the

83 ssessment of individual RFC-A, RFC-B, RFC-C, RFC-D, and RFC-E subunit functions in the reaction mecha

84 The reduced folate carrier (RFC) 80A allele and the thymidylate synthase (TS) 3'-unt

85 specificity over the reduced folate carrier (RFC) and inhibition of de novo purine nucleotide biosynt

86 ess PCFT without the reduced folate carrier (RFC) and of HepG2 cells expressing both PCFT and RFC.

87 s transported by the reduced folate carrier (RFC) and proton-coupled folate transporter (PCFT).

88 The reduced folate carrier (RFC) and the proton-coupled folate transporter (PCFT) ar

89 Reduced folate carrier (RFC) is the major membrane transporter for folates and a

90 iquitously expressed reduced folate carrier (RFC) is the major transport system for folate cofactors

91 The reduced folate carrier (RFC) is the major transport system for folates in mammal

92 ssed FRs but not the reduced folate carrier (RFC) or proton-coupled folate transporter (PCFT).

93 rter (PCFT) over the reduced folate carrier (RFC), 3a was not.

94 at express FR alpha, reduced folate carrier (RFC), and PCFT.

95 The reduced folate carrier (RFC), proton-coupled folate transporter (PCFT), and fola

96 t substrates for the reduced folate carrier (RFC), the major facilitative folate transporter, RFC exp

97 nsporter (PCFT), and reduced folate carrier (RFC).

98 s expressing PCFT or reduced folate carrier (RFC).

99 test activity is the reduced folate carrier (RFC).

100 the widely expressed reduced-folate carrier (RFC).

101 lls that express the reduced folate carrier (RFC).

102 action catalyzed by Saccharomyces cerevisiae RFC and present a comprehensive kinetic model based on g

103 transient events in Saccharomyces cerevisiae RFC-catalyzed PCNA loading, including ATP-induced RFC ac

104 long-hypothesized structure of an open clamp-RFC complex as an intermediate in loading has remained e

105 on algorithms: Random Forest Classification (RFC) and Support Vector Classification (SVC) with linear

106 gression (LR), random forest classification (RFC), and random forest regression (RFR).

107 DNA binding commits RFC to ATP hydrolysis, which is followed by PCNA closure

108 activation of replication factor C complex (RFC) subunits.

109 n is complex, involving multiple components (RFC, PCNA, DNA, and ATP) and events (minimally: PCNA ope

110 e (IPCC) identified 5 "reasons for concern" (RFCs).

111 Our results suggest that the Ctf18 RFC-like complex modifies telomeric chromatin to make it

112 Ctf18-RFC was also a weak loader of PCNA onto naked template-p

113 of the RFC-like complexes Elg1-RFC and Ctf18-RFC to the viability of rfc1-44, genes encoding the larg

114 he 'alternative clamp loader' known as Ctf18-RFC acts by an unknown mechanism to activate the checkpo

115 n rfc1-44 background showing that full Ctf18-RFC function is required in the absence of fully functio

116 rily conserved 'Pol binding module' in Ctf18-RFC that is produced by interaction of the carboxyl term

117 Inactivation of Ctf18-RFC by the deletion of ctf18+, dcc1+ or ctf8+ is lethal

118 d DNA binding protein, both binding of Ctf18-RFC to substrate DNA and loading of PCNA were strongly i

119 dings indicate that the association of Ctf18-RFC with Pol at defective replication forks is a key ste

120 The Dcc1 and Ctf8 subunits of Ctf18-RFC, while required for establishing sister chromatid co

121 This seven-subunit Ctf18-RFC complex consists of the four small subunits of RFC,

122 the cohesion establishment factor, the Ctf18-RFC (replication factor C) complex.

123 by separating the functionality of the Ctf18-RFC complex into two distinct paths.

124 Here we show that budding yeast Ctf18-RFC associates with DNA polymerase epsilon, via an evolu

125 for yeast DNA polymerase delta (Pol delta), RFC and PCNA in LLR repair synthesis.

126 In the presence of purified FEN1, Pol delta, RFC and PCNA, repair occurred on heteroduplexes with loo

127 eplication system in which polymerase delta, RFC, and PCNA were replaced with T4 DNA polymerase and g

128 Also, in addition to polymerase delta, RFC, and PCNA, an as yet unidentified factor(s) is requi

129 Thus, polymerase delta, RFC, PCNA, and the MCM complex, along with the virally e

130 ps between various impacts reflected in each RFC and increases in global mean temperature (GMT) were

131 Either RFC or PCFT cDNA was stably transfected into a transport

132 contribution of the RFC-like complexes Elg1-RFC and Ctf18-RFC to the viability of rfc1-44, genes enc

133 1 in rfc1-44 is lethal, suggesting that Elg1-RFC plays a negative role when RFC function is inhibited

134 n the common archaeal RFC and the eukaryotic RFC, comprises two different small subunits (RFCS1 and R

135 tion of R1-11-RFC6 HeLa cells, which express RFC without PCFT.

136 y more than C1 or C2 at pH 7.2, which favors RFC transport over PCFT.

137 Binding of ring-open PCNA to all five RFC subunits transforms the free-energy landscape underl

138 ds 2-5 had negligible substrate activity for RFC but showed variably potent (nanomolar) and selective

139 The high affinity of pralatrexate for RFC-1 significantly improves its internalization into ce

140 lso suggests that, starting with RFC-A, four RFC subunits (A-D) are sequentially activated through a

141 Dissociation of PCNA.ptDNA from RFC leads to catalytic turnover.

142 required in the absence of fully functional RFC.

143 t response to ATP binding decreases as RFC-C>RFC-D>RFC-B, with RFC-A being unnecessary.

144 onse to ATP binding decreases as RFC-C>RFC-D>RFC-B, with RFC-A being unnecessary.

145 e show that hChlR1 interacts with the hCtf18-RFC complex, human proliferating cell nuclear antigen, a

146 rast to the inhibitory effect of RFC, hRad17-RFC stimulates joining by DNA ligase I.

147 eracts with the hRad17 subunit of the hRad17-RFC cell cycle checkpoint clamp loader, and with each of

148 eviously demonstrated the existence of human RFC (hRFC) homo-oligomers and established the importance

149 es in transmembrane domain (TMD) 11 of human RFC.

150 nt study examines the possibility that human RFC (hRFC) exists as higher order homo-oligomers.

151 ccessful after several failed attempts; (ii) RFC does not act catalytically on a primed 45-mer templa

152 are intramolecular conformational changes in RFC and PCNA that control clamp opening and closure, and

153 al or Ala and mutant constructs expressed in RFC-null HeLa cells.

154 In this study, the arginine fingers in RFC were mutated to examine the steps in the PCNA loadin

155 s study, we examined the roles of individual RFC subunits in opening the PCNA clamp.

156 perspective enables assessment of individual RFC-A, RFC-B, RFC-C, RFC-D, and RFC-E subunit functions

157 atalyzed PCNA loading, including ATP-induced RFC activation, PCNA opening, ptDNA binding, ATP hydroly

158 Extracellular ZMP inhibited RFC-mediated folate influx, and the presence of intracel

159 ATP binding to this subunit initiates RFC activation, and the clamp loader adopts a spiral con

160 X, wild-type (wt) RFC was labeled; for K411A RFC, radiolabeling was abolished.

161 > 1 > 4; inhibition was abolished for K411A RFC.

162 For wt and K411A RFCs, inhibitory potencies were in the order 4 > 5 > 1 >

163 RFC-null K562 cells expressing wt and K411A RFCs.

164 Ala, Arg, Gln, Glu, Leu, and Met, only K411E RFC showed substantially decreased transport.

165 b) similarity of inhibitory potency of known RFC substrates; (c) lack of potentiation in a CCRF-CEM s

166 ve enhanced activities toward tumors lacking RFC function, reflecting contraction of THF cofactor poo

167 the sliding clamp PCNA, and the clamp loader RFC slightly increase the processivity of yeast pol eta

168 polymerase delta, the PCNA clamp, its loader RFC, and completed by DNA ligase I.

169 Pol delta, together with PCNA and its loader RFC.

170 plication factor C (RFC)-CTF18 clamp loader (RFC(CTF18)) controls the velocity, spacing and restart a

171 study the clamp (PCNA) and the clamp loader (RFC) from the mesophilic archaeon Methanosarcina acetivo

172 The clamp loader (RFC) loads a sliding clamp (PCNA) onto a primer/template

173 PCNA opening locks RFC into an active state, and the resulting RFC.ATP.PCNA

174 ATP binding to multiple RFC subunits initiates a slow conformational change in t

175 hat is activated in a mismatch-, MutSalpha-, RFC-, PCNA-, and ATP-dependent manner.

176 clamp opening in the presence and absence of RFC allowed us to substantiate the role of RFC in the in

177 n pemetrexed activity even in the absence of RFC, tumor cells are unlikely to become resistant to pem

178 RFC-C-dependent activation of RFC also enables ptDNA binding, leading to the formation

179 udies suggest that the unloading activity of RFC maximizes the utilization of PCNA by inhibiting the

180 s switched off, resulting in low affinity of RFC for DNA and ejection of RFC from the site of PCNA lo

181 The affinity of RFC for PCNA is about an order of magnitude lower in the

182 ivity required the ATP-bound conformation of RFC.

183 Previous considerations of RFC structure and mechanism were based on the notion tha

184 In contrast to the inhibitory effect of RFC, hRad17-RFC stimulates joining by DNA ligase I.

185 low affinity of RFC for DNA and ejection of RFC from the site of PCNA loading.

186 a phenomenon intrinsic to the energetics of RFC-mediated folate transport.

187 The unexpected finding of RFC expression and activity in cultured Muller cells may

188 mplexes and that the nonreplicative forms of RFC are strongly deleterious to cells that have genomewi

189 The importance of RFC subunit response to ATP binding decreases as RFC-C>R

190 e of thiamine pyrophosphate, an inhibitor of RFC.

191 roperties of selective FR targeting, lack of RFC transport, and GARFTase inhibition resulting in pote

192 dissociation was observed in the presence of RFC-loaded PCNA.

193 f RFC allowed us to substantiate the role of RFC in the initial stage of the clamp-loading cycle.

194 This report finds that the ATP sites of RFC function in distinct steps during loading of PCNA on

195 mplex consists of the four small subunits of RFC, together with Ctf18, Dcc1, and Ctf8.

196 about an order magnitude weaker than that of RFC for PCNA, similar to the RFC-PCNA interaction in the

197 cies disassemble through either unloading of RFC.PCNA from DNA or dissociation of PCNA into its compo

198 to progress rapidly without ESCO1, ESCO2, or RFC(CTF18).

199 RFC complex because knockdowns of any other RFC subunits or other alternative RFCs did not affect PC

200 ecarious balance between Rfc1p and the other RFC complexes and that the nonreplicative forms of RFC a

201 antifolate drugs via transport by PCFT over RFC by exploiting the acidic tumor microenvironment.

202 ive chemotherapy drug delivery via PCFT over RFC, a process that takes advantage of a unique biologic

203 to selective transport by FRs and PCFT over RFC.

204 analogs were selective for FR and PCFT over RFC.

205 vely] are selective substrates for PCFT over RFC.

206 mplete selectivity for FRalpha and PCFT over RFC.

207 we show that the ability of PCNA to overcome RFC-mediated inhibition of Cdc9 is dependent upon both t

208 In addition to DNA polymerase delta, PCNA, RFC, and RPA, 5'-directed repair depends on MutSalpha an

209 MutSbeta, MutLalpha, RPA, EXO1, HMGB1, PCNA, RFC, polymerase delta, and ligase I.

210 ted system of yeast Rad51, Rad54, RPA, PCNA, RFC, and DNA polymerase delta that loading of PCNA by RF

211 ed in the presence of the accessory proteins RFC, PCNA and RPA and are consistent with the establishe

212 LigI51A was defective in binding to purified RFC and in associating with RFC in cell extracts.

213 tumor cells including wild-type (WT) and R5 (RFC-null) HeLa cells express high levels of PCFT protein

214 We propose that Rad.RFC may clear PCNA from DNA to facilitate shutdown of re

215 Interestingly, the Rad.RFC DNA damage checkpoint clamp loader unloads PCNA clam

216 The C. elegans Rad17 RFC clamp loader homolog, hpr-17, functions in the same

217 ent of replication protein A, Claspin, Rad17-RFC, and Rad9-Rad1-Hus1 was not detected in these experi

218 s1 (9-1-1) clamp complex together with Rad17-RFC clamp loader.

219 Although Rad24-RFC alone does not bind to naked partial double-stranded

220 lexes are formed when PCNA is bound by Rad24-RFC than when bound by RFC.

221 Ddc2 and loading of the 9-1-1 clamp by Rad24-RFC, but not Rad9 or Mrc1.

222 9-1-1 complex in human) and its loader Rad24-RFC are also essential components of this signal transdu

223 he DNA damage checkpoint clamp loader, Rad24-RFC, using two separate fluorescence intensity-based ass

224 The affinity of Rad24-RFC for PCNA in the presence of ATP is about an order ma

225 plication protein A) causes binding of Rad24-RFC via interactions with RPA.

226 ponse factor is loaded onto DNA by the Rad24-RFC (replication factor C-like complex with Rad24) clamp

227 activity, but also at neutral pH, reflecting RFC function.

228 r is the first small molecule that regulates RFC activity.

229 RFC into an active state, and the resulting RFC.ATP.PCNA((open)) intermediate is ready for the entry

230 M. acetivorans RFC (RFC(Ma)), which represents an intermediate between the c

231 lease 1 (Exo1), replication protein A (RPA), RFC, PCNA, and DNA polymerase delta.

232 ture of Msh2-Msh6 (or Msh2-Msh3), Exo1, RPA, RFC-Delta1N, PCNA, and Pol epsilon was found to catalyze

233 ture of Msh2-Msh6 (or Msh2-Msh3), Exo1, RPA, RFC-Delta1N, PCNA, and Pol epsilon was found to catalyze

234 te the SDSA pathway using Rad51, Rad54, RPA, RFC, DNA Polymerase delta with different forms of PCNA.

235 CC authors did not assess whether any single RFC was more important than any other; nor did they conc

236 pecific interactions between S. solfataricus RFC clamp loader and PCNA permit us to superimpose our d

237 The central subunit RFC-C serves as a critical swivel point in the clamp loa

238 , and that ATP binding and hydrolysis switch RFC between conformations with high and low affinities,

239 d, recombinant proteins, we demonstrate that RFC directly binds Asf1 and can recruit Asf1 to DNA mole

240 Unexpectedly, we discovered that RFC can assemble a PCNA ring from monomers in solution.

241 There is little evidence that RFC-mediated influx is posttranscriptionally regulated.

242 er mechanisms--suggesting, for example, that RFC-A possesses a triggering component for DNA-dependent

243 and mechanism were based on the notion that RFC monomers were sufficient to mediate transport of fol

244 The RFC subunits are AAA+ family proteins and the complex co

245 The RFC-mediated thymidylate synthase inhibitor plevitrexed

246 The RFC-related checkpoint protein Rad17, a phosphorylation

247 ctural details regarding PCNA loading by the RFC complex are still developing.

248 lls that lacked FRs but contained either the RFC or PCFT.

249 a CCRF-CEM subline that does not express the RFC; and (d) similarity of time and temperature dependen

250 on a primed 45-mer templated fork; (iii) the RFC.PCNA.DNA complex formed in the presence of ATP is de

251 rent for the large and small subunits in the RFC complex.

252 ngthening the biological significance of the RFC complex as a host restriction factor for poxviruses.

253 these constraints, within the context of the RFC structure, provides clues regarding clamp-loader mec

254 The pivotal role of the RFC-B/C/D subunit ATPase core in clamp loading is consis

255 To assess the contribution of the RFC-like complexes Elg1-RFC and Ctf18-RFC to the viabili

256 d binding of ptDNA leads to formation of the RFC.ATP.PCNA(open).ptDNA complex, which catalyzes a burs

257 DNA binding, leading to the formation of the RFC.ATP.PCNA(open).ptDNA complex.

258 oader), we have examined the assembly of the RFC.PCNA.DNA complex and its progression to holoenzyme u

259 ct with DNA thread through the center of the RFC/clamp complex.

260 nflux by AICAr is mediated by effects on the RFC is supported by analyses +/-AICAr showing (a) simila

261 We show that upon clamp opening the RFC/PCNA complex undergoes a large conformational rearra

262 elicase, the Pol epsilon DNA polymerase, the RFC clamp loader, the PCNA sliding clamp, and the RPA si

263 reak-induced telomere synthesis requires the RFC-PCNA-Pol delta axis, but is independent of other can

264 er than that of RFC for PCNA, similar to the RFC-PCNA interaction in the absence of ATP.

265 of poldelta only one species converts to the RFC.PCNA.DNA.poldelta holoenzyme.

266 as selected from a HeLa subline in which the RFC gene was deleted and PCFT was highly overexpressed.

267 functions of individual subunits within the RFC(Ma) complex.

268 scribe revisions of the sensitivities of the RFCs to increases in GMT and a more thorough understandi

269 Functions have been ascribed to RFC subunits previously based on a steady-state analysis

270 e reaction mechanism are that ATP binding to RFC initiates slow activation of the clamp loader, enabl

271 ATP binding to RFC powers recruitment and opening of PCNA and activates

272 uired for high-affinity substrate binding to RFC, whereas the gamma-carboxyl is not essential.

273 PCNA closure severs contact to RFC subunits D and E (RFC2 and RFC5), and the gamma-phos

274 es of this and other antifolates relative to RFC at physiological pH.

275 Activity toward RFC-expressing cells was negligible.

276 , the major facilitative folate transporter, RFC expression may alter drug efficacies by affecting ce

277 Unlike RFC, PCFT is active at acidic pH levels characterizing t

278 d compare the constraints imposed on various RFC clamp-loader subunits, each of which performs a rela

279 e transported into tumor cells primarily via RFC.

280 ing that Elg1-RFC plays a negative role when RFC function is inhibited.

281 by RFC revealed a two-step reaction in which RFC binds PCNA before opening PCNA rather than capturing

282 is in vitro by yeast pol zeta alone and with RFC, PCNA and RPA.

283 ding to purified RFC and in associating with RFC in cell extracts.

284 binding decreases as RFC-C>RFC-D>RFC-B, with RFC-A being unnecessary.

285 aloyl-l-ornithine (PT523) in comparison with RFC irrespective of the folate growth source.

286 e an open yeast PCNA clamp in a complex with RFC through fluorescence energy transfer experiments.

287 drolysis leads to complex dissociation, with RFC-D activity contributing the most to rapid ptDNA rele

288 Unable to slide away, PCNA re-engages with RFC and is unloaded.

289 g cell nuclear antigen, the interaction with RFC is regulated by hLigI phosphorylation.

290 on negatively regulates the interaction with RFC.

291 ver, their actions are subunit-specific with RFC-C Arg-88 serving as an accelerator that enables rapi

292 It also suggests that, starting with RFC-A, four RFC subunits (A-D) are sequentially activate

293 y than WT cells or R5 cells transfected with RFC.

294 ere used to inhibit [(3)H]MTX transport with RFC-null K562 cells expressing wt and K411A RFCs.

295 , 2, and 4 were used to covalently modify wt RFC, inhibitory potencies were in the order 2 > 1 > 4; i

296 labeling with NHS-[(3)H]MTX, wild-type (wt) RFC was labeled; for K411A RFC, radiolabeling was abolis

297 (CTD) of the large subunit of fission yeast RFC is shown to be essential for its function in vivo.

298 Neither yeast RFC itself nor two other related clamp loaders, containi

299 rimpose our data upon the structure of yeast RFC-PCNA complex, thereby presenting a general model for

300 unctionally homologous human proteins, yeast RFC interacts with and inhibits Cdc9 DNA ligase whereas