ライフサイエンスコーパス: clamp loader

1 ght-handed spiral to match the spiral of the clamp loader.

2 nded DNA-binding protein (SSB), binds to the clamp loader.

3 9-1-1) clamp complex together with Rad17-RFC clamp loader.

4 ded onto DNA by a replication factor C (RFC) clamp loader.

5 clamp, and, replication factor C (RFC), the clamp loader.

6 ubunit to the function of the M. acetivorans clamp loader.

7 physically or genetically with a replication clamp loader.

8 clamp loading activity of the M. acetivorans clamp loader.

9 previously crystallized extended form of the clamp loader.

10 a highly asymmetric and extended form of the clamp loader.

11 conformation seen earlier for the bacterial clamp loader.

12 n conformation to be assembled onto DNA by a clamp loader.

13 t PCNA loading or unloading activity of each clamp loader.

14 Pase active subunits of the Escherichia coli clamp loader.

15 C-C serves as a critical swivel point in the clamp loader.

16 aces of the delta and delta' subunits of the clamp-loader.

17 the mechanism of eukaryotic and prokaryotic clamp loaders.

18 a) and the five-subunit replication factor C clamp loader (250 kDa).

19 ral arrangement of the ATPase domains of the clamp loader above the PCNA ring.

20 loenzyme, chi and Psi are tightly associated clamp loader accessory subunits.

21 lize a fundamentally different mechanism for clamp loader activation than do these other organisms.

22 results support a model in which the E. coli clamp loader actively opens the beta-sliding clamp.

23 rystal structure, suggesting that eukaryotic clamp loaders adopt a similar autoinhibited state early

24 is subunit initiates RFC activation, and the clamp loader adopts a spiral conformation that stabilize

25 d possibly serves as a scaffold on which the clamp loader adopts the appropriate conformation for DNA

26 Clamps and clamp loaders also function in other DNA metabolic proce

27 By probing the interaction between the clamp loader and a single-stranded DNA (ssDNA) binding p

28 tion of the FRET pair in the presence of the clamp loader and ATP may be ascribed to either further o

29 eplication factor C-like complex with Rad24) clamp loader and ATP.

30 ysis, the Rad1731 clamp is released from the clamp loader and can slide across more than 1 kb of dupl

31 interaction between the E.coli gamma complex clamp loader and DNA using UV-induced protein-DNA cross-

32 g of the multistep mechanism of a eukaryotic clamp loader and furthermore facilitates comparative ana

33 The switch requires the tau subunit of the clamp loader and is regulated by different DNA structure

34 onformations that would allow binding to the clamp loader and loading onto double-stranded DNA.

35 fic interactions between S. solfataricus RFC clamp loader and PCNA permit us to superimpose our data

36 ar exchange in live cells containing labeled clamp loader and polymerase.

37 re performed to test for dissociation of the clamp loader and primase from an active replisome in vit

38 ally similar to the replication factors, RFC clamp loader and proliferating cell nuclear antigen poly

39 rom ATP-binding and interactions between the clamp loader and the beta clamp.

40 Interactions between the clamp loader and the clamp have been proposed to mirror

41 merase, (3) clamp binding to DNA followed by clamp loader and then polymerase, and (4) polymerase bin

42 ts in the sites implicated in binding to the clamp loader and to ligand proteins.

43 s and clamps coordinate their actions with a clamp loader and yet other proteins to form a replisome

44 aB by a mechanism akin to that of polymerase clamp loaders and indicate that bacterial replicative he

45 Clamp-loader and sliding clamp structures have been solv

46 presence of primase, helicase, Pol III core, clamp loader, and beta-clamp initiates DNA synthesis on

47 tion between replication factor C (RFC), the clamp loader, and DNA ligase I in human cell extracts.

48 eterodimer interacted normally with the DnaX clamp loader, and was loaded onto DNA slightly more effi

49 unit of the hRad17-RFC cell cycle checkpoint clamp loader, and with each of the subunits of its DNA s

50 DNA translocases, helicases, motor proteins, clamp loaders, and other ATP-dependent enzymes.

51 ia coli, Saccharomyces cerevisiae, and human clamp loaders, and the two protein Pyrococcus furiosus a

52 sus and Methanobacterium thermoautotrophicum clamp loaders, and thus far the site(s) responsible for

53 Therefore, ATP hydrolysis by the clamp-loader appears to open the clamp wide enough to en

54 The primase, clamp, and clamp loader are found to dissociate from the replisome

55 the subunits of the checkpoint clamp and the clamp loader are required for TLS.

56 The heteropentameric clamp loaders are circular oligomers, reflecting the cir

57 Clamp loaders are multi-protein complexes, such as the f

58 Clamp loaders are multisubunit complexes that use the en

59 Clamp loaders are thought to be specific for a 3' primed

60 Therefore, this work identifies the DNAP III clamp loader as a new target for inhibition of bacterial

61 ring interactions of the clamp with the DnaX clamp loader, as well as the replicative DNA polymerase,

62 Clamp loaders assemble sliding clamps onto 3' primed sit

63 richia coli DNA polymerase III gamma complex clamp loader assembles the ring-shaped beta sliding clam

64 ntameric tau3-delta-delta' Bacillus subtilis clamp-loader assembles via multiple pathways, which diff

65 a conformation before PCNA opening, with the clamp loader ATPase modules forming an overtwisted spira

66 eds to be opened and installed onto DNA by a clamp loader ATPase of the AAA+ family.

67 onserved both in bacterial and in eukaryotic clamp loader ATPases appears to play a critical role.

68 cificity, as we illustrate for bacterial DNA clamp loader ATPases.

69 ow that four ATP ligands must bind to the T4 clamp loader before the loader can be fully "activated"

70 Clamp loaders belong to a family of proteins known as AT

71 In the first stage of clamp loading, clamp loaders bind and stabilize clamps in an open confo

72 amps that have transiently opened or whether clamp loaders bind closed clamps and actively open clamp

73 x binding to DNA followed by polymerase, (2) clamp loader binding to DNA followed by clamp and then p

74 ree-step 'bind-open-lock' model in which the clamp loader binds a closed clamp, the clamp opens, and

75 The ATP-bound clamp loader binds both elongation-proficient and defici

76 During the reaction, the clamp loader binds primer-template DNA and positions it

77 itionally, the S. aureus delta wrench of the clamp loader binds to E. coli beta.

78 The structure of the E. coli clamp loader bound to DNA reveals the formation of an AT

79 ot due to altered interactions with the DnaX clamp loader, but rather was the result of impaired beta

80 osed of either form of DnaX are fully active clamp loaders, but tau confers important replicase funct

81 ovides a unique perspective into the E. coli clamp loader by providing a measure of the relative timi

82 here that the Escherichia coli gamma complex clamp loader can load the beta clamp onto a 5' primed si

83 An unresolved question is whether clamp loaders capture clamps that have transiently opene

84 defect was measured with a mutant RFC-Rad24 clamp loader carrying a rfc4K55R ATP-binding mutation, w

85 In most organisms, clamp loaders catalyze both the loading of sliding clamp

86 Clamp loaders catalyze clamp assembly onto DNA, and the

87 tudies, charged/polar amino acids inside the clamp loader chamber interact with the double-stranded (

88 We reveal an additional role for the DnaX clamp loader: chaperoning of the replicative polymerase

89 the protein that distinguishes it from other clamp loader clade AAA+ proteins.

90 on identifies MgsA enzymes as members of the clamp loader clade of AAA+ proteins, but structural info

91 A AAA+ ATPase in the clamp loader clade, RarA protein is part of a highly con

92 ation of a functional holoenzyme on DNA: (1) clamp loader-clamp complex binding to DNA followed by po

93 ent conformational rearrangements 'lock' the clamp loader-clamp complex in a stable open conformation

94 neither facilitates the formation of an open clamp loader-clamp complex in experiments presented here

95 o determine whether the formation of an open clamp loader-clamp complex is dependent on spontaneous c

96 To load clamps onto DNA, an open clamp loader-clamp complex must form.

97 4) polymerase binding to DNA followed by the clamp loader-clamp complex.

98 Importantly, fewer open clamp loader-clamp complexes are formed when PCNA is bou

99 mate in the ATPase site and lie close to the clamp loader-clamp-binding interface.

100 y new crystal structures of bacteriophage T4 clamp loader-clamp-DNA complexes that capture two distin

101 structural work has been carried out on the clamp-loader-clamp-DNA polymerase alpha interactions in

102 ains of the delta and delta' subunits of the clamp loader close to each other in the inactive state,

103 riants stimulated the ATPase function of the clamp loader, complemented cell growth of a temperature-

104 Rad17, a component of the checkpoint clamp loader complex (Rad17/Rfc2-5), is required for the

105 ication complex, initiation factors, and the clamp loader complex (replication factor C) remained tet

106 rt the crystal structure of the five-protein clamp loader complex (replication factor-C, RFC) of the

107 lements are involved, the tau subunit of the clamp loader complex and an OB domain within the DNA pol

108 ntrast, the ATPase rate profile of the clamp-clamp loader complex exhibits a marked peak at an input

109 nt structures for the ATP-bound state of the clamp loader complex from bacteriophage T4, bound to an

110 The crystal structure of the pentameric clamp loader complex from Escherichia coli (the gamma co

111 The prokaryotic DNA polymerase III clamp loader complex loads the beta clamp onto DNA to li

112 This model, in which the clamp loader complex locks onto primed DNA in a screw-ca

113 The clamp loader complex reconstituted from the three subuni

114 inhibited by replication factor C (RFC), the clamp loader complex that loads PCNA onto DNA.

115 stigate the structural changes in the E.coli clamp loader complex that result from ATP-binding and in

116 and are loaded onto DNA by an ATP-dependent clamp loader complex that ruptures the interface between

117 ust be opened and resealed around DNA by the clamp loader complex to fulfil their function.

118 y proteins: gp45 (sliding clamp), gp44/gp62 (clamp loader complex), gp55 (late sigma-factor), and gp3

119 e-dimensional models of one form of the full clamp loader complex, gamma3deltadelta'psichi (254 kDa).

120 sembly of this holoenzyme, the seven-subunit clamp loader complex, is responsible for loading the sli

121 clamp is loaded onto DNA and unloaded by the clamp loader complex, the delta subunit of which by itse

122 t with the spiral interaction surface of the clamp loader complex, we have performed molecular dynami

123 Rad17 is a subunit of the Rad9-Hus1-Rad1 clamp loader complex, which is required for Chk1 activat

124 s need to be opened and loaded onto DNA by a clamp loader complex-a process, which involves disruptio

125 , a sliding clamp processivity factor, and a clamp loader complex.

126 ial tau, delta, and delta' components of the clamp loader complex.

127 sequent hydrolysis of ATP by the clamp-bound clamp loader complex.

128 i heterodimer serves as a bridge between the clamp-loader complex and the single-stranded DNA-binding

129 e describe crystal structures of the E. coli clamp-loader complex bound to the ATP analog ATPgammaS (

130 We speculate that psi is linked to the clamp-loader complex by this flexible, but conserved, N-

131 The base of the clamp-loader complex has an open C-shaped structure, and

132 The clamp-loader complex plays a crucial role in DNA replica

133 s are similar to that of the nucleotide-free clamp-loader complex.

134 he replicative helicase, DNA polymerase, and clamp loader complexes are consistent with the presence

135 Implications to eukaryotic clamp loader complexes are proposed.

136 mps, which are loaded onto DNA by pentameric clamp loader complexes belonging to the AAA+ family of a

137 there may be a conserved need for alternate clamp loader complexes during DNA damaging conditions.

138 The action of ATP-dependent clamp loader complexes is required to open the circular

139 Sliding clamps are placed on DNA by clamp loader complexes, in which the clamp-interacting e

140 ganization reminiscent of the DNA polymerase clamp loader complexes.

141 clamp onto DNA is overcome by ATP-dependent clamp loader complexes.

142 Clamp-loader complexes are heteropentameric AAA+ ATPases

143 re associated with three molecules of tau, a clamp loader component that trimerizes polymerase.

144 it and one large subunit, the M. acetivorans clamp loader comprises two similar small subunits (M. ac

145 ither yeast RFC itself nor two other related clamp loaders, containing either Rad24 or Elg1, catalyze

146 fc1p, and by inactivation of the alternative clamp loaders CTF18, RAD24, and ELG1.

147 previously and led to the proposal that the clamp-loader cycles between an inactive state, in which

148 Our results show a novel mechanism for clamp-loader-dependent fork progression, mediated by the

149 ggest that the more open form of the E. coli clamp loader described earlier and in the present work c

150 interplay between gp32, primase, clamp, and clamp loader dictates the rate and efficiency of primer

151 obacter viability, and identifies a role for clamp loader diversity in responding to DNA damage.

152 dy-state FRET measurements, we show that the clamp loader-DNA complex is functional in clamp loading.

153 ities between the replication and checkpoint clamp loader/DNA clamp pairs.

154 ition of nucleotide and clamp to the labeled clamp loader does not appreciably alter these FRET dista

155 uggested that the similarity between the two clamp loaders does not translate into the complete conse

156 targeting the delta subunit of the DNAP III clamp loader; E. coli mutations conferring gp8 resistanc

157 nitiates a slow conformational change in the clamp loader, enabling it to bind and open PCNA and to b

158 ding to RFC initiates slow activation of the clamp loader, enabling it to open PCNA (at ~2 s(-1)) and

159 bution of subunits in this new member of the clamp loader family.

160 i subunit also increases the affinity of the clamp loader for the clamp in assays in which ATPgammaS

161 not appear to be due to DNA binding, as the clamp loader forms an avid complex with beta at a 5' sit

162 Here, we describe a new form of clamp loader from the archaeon Methanosarcina acetivoran

163 Clamp loaders from all domains of life load clamps onto

164 ta in the gamma complex may be true also for clamp loaders from other organisms.

165 insights into the evolution of more complex clamp loaders from simpler ones as more complex organism

166 tearothermophilus and the tau subunit of the clamp-loader from Bacillus subtilis we show that changes

167 ignal indicated that the dissociation of the clamp-loader from this complex occurred after guiding th

168 Escherichia coli gamma complex clamp loader functions to load the beta sliding clamp on

169 The clamp loader, gamma complex (gamma 3 delta delta'chi psi

170 The Escherichia coli clamp loader, gamma complex (gamma(3)deltadelta'lambdaps

171 asuring the activities of three forms of the clamp loader, gamma(3)deltadelta', gamma(3)deltadelta'ps

172 sed assay in which the E. coli gamma complex clamp loader (gamma3deltadelta'chipsi) was labeled with

173 a clamp loading pathway that utilizes the T4 clamp loader (gp44/62) and ATP hydrolysis initially to f

174 ture of the nucleotide-free Escherichia coli clamp loader had been determined previously and led to t

175 ot impair clamp loading activity, any mutant clamp loader harboring a mutation in MacRFCS1 was devoid

176 Crystal structures of an Escherichia coli clamp loader have provided insight into the mechanism by

177 The clamp-loader-helicase interaction is an important featur

178 alpha interactions in Escherichia coli, the clamp-loader-helicase interaction is poorly understood b

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

180 he 9-1-1 DNA damage response complex and its clamp loader, HPR-17.

181 Rad17 is best known as a checkpoint clamp loader in the activation of ATR kinase signaling.

182 orresponds to a stable inactive state of the clamp loader in which the ATPase domains are prevented f

183 tic analyses further support the role of the clamp-loader in bacteriophage T4 as a catalyst which loa

184 The eukaryotic replication factor C (RFC) clamp loader is an AAA+ spiral-shaped heteropentamer tha

185 Instead, the function of the clamp loader is dependent on the selective stabilization

186 The S. aureus clamp loader is even capable of loading E. coli and Stre

187 nterestingly, the chi subunit of the E. coli clamp loader is not required for SSB to inhibit clamp lo

188 tion between DNA ligase I and the checkpoint clamp loader is regulated by post-translational modifica

189 The clamp loader is required to load the clamp onto DNA for

190 The Escherichia coli clamp loader is the DnaX complex (DnaX(3)deltadelta'chip

191 lecule bound to the Saccharomyces cerevisiae clamp loader is unknown.

192 lamp-opening subunit in the Escherichia coli clamp loader, is not required to open PCNA.

193 remarkable progress in our understanding of clamp loaders, it is still unclear how recognition of pr

194 h budding yeast showed that the 'alternative clamp loader' known as Ctf18-RFC acts by an unknown mech

195 As eukaryotic and archaeal clamp loaders lack most of these key residues, it appear

196 be suppressed by overexpression of the PCNA clamp loader large subunit, Rfc1p, and by inactivation o

197 We find that clamp and clamp loader levels affect both primer utilization and O

198 sion and signaling mechanisms as the gp44/62 clamp loader levels changed but was insensitive to chang

199 Clamp loaders load ring-shaped sliding clamps onto DNA w

200 Clamp loaders load ring-shaped sliding clamps onto DNA.

201 Clamp loaders load sliding clamps onto primer-template D

202 In Escherichia coli, the gamma complex clamp loader loads the beta-sliding clamp onto DNA.

203 er that is associated with the ATP-dependent clamp-loader machinery.

204 ge subunit) suggests that the M. acetivorans clamp loader may be an intermediate form in the archaeal

205 clamp loader, suggesting that the S. aureus clamp loader may have difficulty ejecting from heterolog

206 has been done studying the sliding clamp and clamp loader mechanism, kinetic analysis of the events f

207 ments are not a significant component of the clamp loader mechanism.

208 Here clues to underlying clamp loader mechanisms are obtained through Bayesian in

209 the RFC structure, provides clues regarding clamp-loader mechanisms--suggesting, for example, that R

210 The tau subunit of the clamp-loader mediates the interaction with DnaB.

211 d resealed at primer-template junctions by a clamp loader molecular machine, replication factor C (RF

212 Clamp loaders must quickly and efficiently load clamps a

213 neither the function of the Rad24 checkpoint-clamp loader nor the Rad6-Rad18-mediated ubiquitination

214 There is widespread agreement that the clamp loader of the Escherichia coli replicase has the c

215 r C (RFC) is a heteropentameric AAA+ protein clamp loader of the proliferating cell nuclear antigen (

216 Implications of these results to clamp loaders of other systems are discussed.

217 SSBs inhibit clamp loading by both clamp loaders on the incorrect polarity of DNA (5'DNA).

218 e phage T4 sliding clamp gp45 by the gp44/62 clamp loader onto DNA to form the holoenzyme and their d

219 o each other in the inactive state, with the clamp loader opening in a crab-claw-like fashion upon AT

220 The delta subunit of the clamp loader opens the beta ring and is referred to as t

221 svirus processivity factors do not require a clamp loader or ATP to bind to template DNA.

222 e/function of the Methanosarcina acetivorans clamp loader or replication factor C (RFC) homolog.

223 Clamp loaders orchestrate the switch from distributive t

224 To understand how clamp loaders perform this complex task, here we focused

225 open conformation, and in the second stage, clamp loaders place the open clamps around DNA so that t

226 To form a productive holoenzyme complex, clamp loader protein gp44/62 is required for the loading

227 Due to the closed ring shape of the clamp, a clamp loader protein, belonging to the AAA+ class of ATP

228 Clamp loader proteins catalyze assembly of circular slid

229 r results were obtained with antisera to the clamp loader proteins Rfc3 and Rfc4, and to PCNA, i.e. L

230 ame site as that of the delta-subunit of the clamp loader, providing the basis for a switch between t

231 as Rad24, members of the putative checkpoint clamp loader (Rad24) and sliding clamp (Rad17, Mec3) com

232 actor C (RFC), and the DNA damage checkpoint clamp loader, Rad24-RFC, using two separate fluorescence

233 Instead, we find that clamp loader recognition of a 3' site lies in the duplex

234 s led to the hypothesis that a similar clamp-clamp loader relationship exists for the DNA damage resp

235 nd simple modeling studies indicate that the clamp loader releases DNA prior to the clamp and that DN

236 The human clamp loader replication factor C (RFC) and sliding clam

237 The DNA damage clamp loader replication factor C (RFC-Rad24) consists o

238 s proliferating cell nuclear antigen and the clamp loader replication factor C facilitated DNA synthe

239 with the proliferating cell nuclear antigen clamp loader replication factor C, DNA polymerase delta,

240 DNA loop and provides a binding site for the clamp-loader Replication Factor C.

241 l structure of a nucleotide-bound eukaryotic clamp loader [replication factor C (RFC)] revealed a dif

242 A onto duplex DNA requires the activity of a clamp-loader [replication factor C (RFC)] complex and th

243 and opening by the Saccharomyces cerevisiae clamp loader, replication factor C (RFC), and the DNA da

244 unit-subunit interfaces by the ATP-dependent clamp loader, Replication Factor C, whose clamp-interact

245 omyces cerevisiae replication factor C (RFC) clamp loader, respectively, and assessed the impact on m

246 proposed to mirror those of the replication clamp loader RFC and the sliding clamp proliferating cel

247 protein RPA, the sliding clamp PCNA, and the clamp loader RFC slightly increase the processivity of y

248 We have purified the putative checkpoint clamp loader RFC-Rad24 and the putative clamp Rad1731 fr

249 te that the replication factor C (RFC)-CTF18 clamp loader (RFC(CTF18)) controls the velocity, spacing

250 nce assays to study the clamp (PCNA) and the clamp loader (RFC) from the mesophilic archaeon Methanos

251 The clamp loader (RFC) loads a sliding clamp (PCNA) onto a p

252 All clamp loaders share a core structure in which five subun

253 R ATP-binding mutation, whereas the rfc4K55E clamp loader showed partial loading activity, in agreeme

254 ng, and ATP hydrolysis-implying a remarkably clamp-loader-specific function.

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

256 scherichia coli and Saccharomyces cerevisiae clamp loader specificity toward 3'DNA, fluorescent beta

257 nct conformations of the ATPase domains, the clamp loader spiral is symmetric and is set up to trigge

258 mble models of psichi-SSB4 (108 kDa) and the clamp loader-SSB4 (340 kDa) consistent with IM data.

259 asured collision cross-section (~10%) of the clamp loader-SSB4 complex upon DNA binding suggests larg

260 with the presence of psichi, stabilises the clamp loader-SSB4 complex.

261 In Escherichia coli, the ATP-binding clamp loader subunit DnaX exists as both long (tau) and

262 ase epsilon and the C-terminal domain of the clamp loader subunit tau.

263 lymerases, PolC and DnaE, and a processivity clamp loader subunit, DnaX.

264 The gamma complex structure shows that the clamp loader subunits are arranged as a circular heterop

265 the clamp can easily match the spiraling of clamp loader subunits, a feature that is intrinsic to th

266 ects of abolishing ATP binding in individual clamp loader subunits.

267 In particular, studies of sliding clamps and clamp-loader subunits elucidate the mechanisms of replis

268 mpare the constraints imposed on various RFC clamp-loader subunits, each of which performs a related

269 t marked similarity to the structures of the clamp-loader subunits.

270 nt on the presence of the chi subunit of the clamp loader, suggesting recruitment of Pol III HE at si

271 en they are loaded onto DNA by the S. aureus clamp loader, suggesting that the S. aureus clamp loader

272 selectivity to differing degrees for the two clamp loaders, suggesting variations in the mechanism by

273 that ATP utilization by the checkpoint clamp/clamp loader system is effectively different from that b

274 This parallelism with a clamp-clamp loader system that functions in DNA replication ha

275 has been suggested that clamp opening by the clamp loader takes advantage of spontaneous opening-clos

276 gesting variations in the mechanism by which clamp loaders target 3'DNA.

277 h a free 3'OH (3'DNA), but it is unclear how clamp loaders target these sites.

278 tion in the C-terminal domain of the E. coli clamp loader that contributes to DNA binding and helps d

279 son to promote conformational changes in the clamp loader that drive clamp loading.

280 reminiscent of the minimal Escherichia coli clamp loader that exists in space as three gamma-subunit

281 By stabilizing a conformation of the clamp loader that is consistent with the ATPase spiral o

282 Using mutant clamp loaders that are deficient in either ATP binding o

283 e loaded onto primer-template DNA (ptDNA) by clamp loaders that open and close clamps around ptDNA in

284 re ring-shaped; therefore, they have cognate clamp loaders that open and load them onto DNA.

285 DnaB is attached to the tau subunit of the clamp-loader that loads the beta clamp and interconnects

286 ase activity drives interactions between the clamp loader, the clamp, and the ptDNA, leading to topol

287 ase, the Pol epsilon DNA polymerase, the RFC clamp loader, the PCNA sliding clamp, and the RPA single

288 de that gp59 acts in a manner similar to the clamp loader to ensure proper assembly of the replisome

289 nduced conformational changes that allow the clamp loader to pry open the clamp.

290 the psi protein, essential for coupling the clamp loader to single-stranded DNA-binding protein (SSB

291 ighlight a common role for SSBs in directing clamp loaders to 3'DNA, as well as uncover nuances in th

292 Sliding clamps are loaded onto DNA by clamp loaders to serve the critical role of coordinating

293 The clamp loader traps a spiral conformation of the open cla

294 s, including DnaA, helicase, primase and the clamp loader, TrfA interaction with the beta-clamp contr

295 restingly, the Rad.RFC DNA damage checkpoint clamp loader unloads PCNA clamps from DNA.

296 ow how the different subunits of an archaeal clamp loader use ATP binding and hydrolysis in distinct

297 The clamp loader uses the energy of ATP binding and hydrolys

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

299 e relatedness of the archaeal and eukaryotic clamp loaders (which are made up of four similar small s

300 Unlike previously described archaeal clamp loaders, which are composed of one small subunit a