ライフサイエンスコーパス: clamp loader

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

2 9-1-1) clamp complex together with Rad17-RFC clamp loader.

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

4 n conformation to be assembled onto DNA by a 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 assembly at primer-template junctions by its clamp loader.

13 ep groove or cleft and is similar to the RFC 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 ght-handed spiral to match the spiral of the clamp loader.

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

18 mp processivity factor, and the DnaX complex clamp-loader.

19 the mechanism of eukaryotic and prokaryotic clamp loaders.

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

46 Clamp-loader and sliding clamp structures have been solv

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

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

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

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

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

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

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

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

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

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

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

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

59 Clamp loaders are multisubunit complexes that use the en

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

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

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

63 Clamp loaders assemble sliding clamps onto 3' primed sit

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

84 Clamp loaders catalyze clamp assembly onto DNA, and the

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

110 The clamp loader complex reconstituted from the three subuni

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

131 Implications to eukaryotic clamp loader complexes are proposed.

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

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

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

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

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

137 ganization reminiscent of the DNA polymerase clamp loader complexes.

138 Clamp-loader complexes are heteropentameric AAA+ ATPases

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

156 d previously: replication factor C (the PCNA clamp loader), family B DNA polymerase, and flap endonuc

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

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

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

160 Clamp loaders from all domains of life load clamps onto

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

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

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

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

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

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

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

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

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

170 e sigma factor), gp45 (sliding clamp), gp44 (clamp loader), gp2 (DNA end protein), and gp23 (major ca

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

199 Clamp loaders load sliding clamps onto primer-template D

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

201 imental evidence that, indeed, the RFC-Rad24 clamp loader loads the Rad1731 clamp around partial dupl

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

203 ta.beta and the gamma 3 delta delta' minimal clamp loader make predictions of the clamp loader mechan

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 minimal clamp loader make predictions of the clamp loader mechanism, which are tested in this report

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

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

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

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

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

213 Clamp loaders must quickly and efficiently load clamps a

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

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

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

217 mino acid and structural similarities to the clamp loaders of DNA polymerase sliding clamps, have sug

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

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

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

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

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

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

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

225 Clamp loaders orchestrate the switch from distributive t

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

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

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

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

230 Clamp loader proteins catalyze assembly of circular slid

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

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

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

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

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

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

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

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

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

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

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

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

243 A sliding clamps that are loaded onto DNA by clamp loaders [replication factor C (RFC) in eukaryotes]

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

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

246 ir ability to interact with their associated clamp loader, replication factor C (RFC).

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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