ライフサイエンスコーパス: ORC

1 ORC is also involved in other cell functions.

2 ORC remained associated with the internal regions of HMR

3 ORC sites in early and late replicating regions have sim

4 ORC, Cdc6 and Cdt1 act together to load hexameric MCM, t

5 ORC, Cdc6, and MCM are members of the AAA+ family of ATP

6 ORC, together with Cdc6 and Cdt1, mediate pre-replicativ

7 ORC-associated sequences are enriched for the histone va

8 identified a urea-thiophene carboxamide, 1 (ORC-001), as protective against aminoglycoside antibioti

9 e present the optimization of 1 to yield 90 (ORC-13661).

10 nsequently the Cdt1-MCM2-7 complex activates ORC/Cdc6 ATP-hydrolysis to promote helicase loading.

11 Additionally, ORC is bound at many regions that do not undergo amplifi

12 We address ORC binding selectivity in vivo by mapping approximately

13 ic behavior creates a feedback loop allowing ORC/CDC-6 to repeatedly load MCM-2-7 and distribute lice

14 Extending mitosis allows ORC to become more equally associated with origins and l

15 appropriate chromatin structure that allows ORC binding and subsequent origin firing.

16 Although ORC is conserved from yeast to humans, the DNA sequence

17 Although ORC-dependent loading of the replicative MCM helicase at

18 Consistent with this prediction, although ORC associated exclusively with origin sequences in the

19 sisting of an ORC-Cdc6-Mcm2-7 complex and an ORC-Cdc6-Mcm2-7-Mcm2-7 complex are reported, which toget

20 o initiate DNA replication, or cells have an ORC-independent, CDC6-dependent mechanism to load MCM2-7

21 the 'initial' complex is transformed into an ORC/Cdc6/MCM2-7 (OCM) complex.

22 le human ORC(2-5) complex in the nucleus, an ORC(1-5) complex bound to chromatin, and an Orc6 protein

23 evidence for intermediates consisting of an ORC-Cdc6-Mcm2-7 complex and an ORC-Cdc6-Mcm2-7-Mcm2-7 co

24 atin loading was irreversible, but CDC-6 and ORC turned over rapidly, consistent with ORC/CDC-6 loadi

25 ributed substantially to origin activity and ORC binding.

26 disrupted the interaction between EBNA1 and ORC.

27 elomeres, and a loss of histone H3 K9me3 and ORC at telomere repeat DNA.

28 Lrwd1 and ORC are known to co-purify with repressive histone marks

29 antly, the data suggest that nucleosomes and ORC have opposite preferences for DNA sequence and struc

30 gration were still observed between ONRC and ORC (p < 0.05).

31 lts support a model in which Orc6, Orc1, and ORC(2-5) are transported independently to the nucleus wh

32 eplication origins prior to Cdt1 release and ORC-Cdc6-Mcm2-7 complex formation, but how the second Mc

33 iminate between ORC-associated sequences and ORC-free sequences based solely on primary sequence.

34 replication timing, early origin usage, and ORC binding.

35 f ORC hexamers, interfering with appropriate ORC functions.

36 g elements, both viral and cellular, such as ORCs, MCMs, and latency-associated nuclear antigen (LANA

37 stigate the functional role of the bacterial ORC and examine whether it mediates low-affinity DnaA-or

38 pproaches to accurately discriminate between ORC-associated sequences and ORC-free sequences based so

39 rDNA minichromosome, the interaction between ORC and the non-rDNA ARS1 chromosome changed across the

40 matches to this consensus than actually bind ORC or function as origins in vivo.

41 n absolute pH decline was observed with both ORC and ONRC after 1 hour.

42 r data support a model in which origin-bound ORC and Cdc6 recruit two Cdt1 molecules to initiate doub

43 Origin-bound ORC recruits Cdc6, and this ternary complex then promote

44 ntial for initiation of DNA replication, but ORC has non-essential functions outside of DNA replicati

45 ely compared to the standards established by ORC.

46 are disfavored by nucleosomes but favored by ORC.

47 The assistance given by ORC is directed primarily to proximal weak sites and req

48 trical loading of individual MCM hexamers by ORC and directed MCM translocation into double hexamers

49 We show that helicase loading by ORC is inhibited by two distinct CDK-dependent mechanism

50 y of the pre-replication complex (pre-RC) by ORC-Cdc6 and Cdt1.

51 Here we show that MCM2-7 recruitment by ORC/Cdc6 is blocked by an autoinhibitory domain in the C

52 tats such as oxidized regenerated cellulose (ORC, TABOTAMP) and oxidized non-regenerated cellulose (O

53 The Saccharomyces cerevisiae ORC recognizes the ARS (autonomously replicating sequenc

54 In Saccharomyces cerevisiae, ORC binds to specific DNA elements; however, in higher e

55 tored in the Orbivirus Reference Collection (ORC) at IAH Pirbright, shows >99% nucleotide identity in

56 ned from the Orbivirus Reference Collection (ORC) at IAH, Pirbright, United Kingdom.

57 We show that origin recognition complex (ORC) and Cdc6 recruit multiple Cdt1 molecules to the ori

58 both subunits of origin recognition complex (ORC) and Cdc6, which are required to create a prereplica

59 suggest that the origin-recognition complex (ORC) and cell-division cycle 6 (Cdc6) proteins recognize

60 heterohexameric origin recognition complex (ORC) and functions as a replicative helicase.

61 presence of the origin recognition complex (ORC) and MCM proteins at these origins.

62 sphorylating the origin recognition complex (ORC) and promotes CMG formation by phosphorylating Sld2

63 y to recruit the origin recognition complex (ORC) and stimulate OriP replication.

64 alization of the origin recognition complex (ORC) and the minichromosome maintenance (MCM)2-7 complex

65 6, Cdt1, and the origin-recognition complex (ORC) assemble two heterohexameric Mcm2-7 complexes into

66 begins with the origin recognition complex (ORC) binding DNA sites called origins of replication.

67 The origin recognition complex (ORC) binds sites from which DNA replication is initiated

68 en a six-subunit origin recognition complex (ORC) binds to DNA.

69 The origin recognition complex (ORC) binds to the specific positions on chromosomes that

70 mena thermophila origin recognition complex (ORC) contains an integral RNA subunit, 26T RNA, which co

71 The origin recognition complex (ORC) defines origins of replication and also interacts w

72 e specificity in origin recognition complex (ORC) DNA binding complicates genome-scale chromatin immu

73 f binding of the origin recognition complex (ORC) in a differentiated metazoan tissue, we find that O

74 cruitment of the origin recognition complex (ORC) in a manner dependent on Suv4-20h and H4K20me3.

75 The origin recognition complex (ORC) is a 6-subunit complex required for the initiation

76 The origin recognition complex (ORC) is a DNA replication initiator protein also known t

77 The origin recognition complex (ORC) is an essential DNA replication initiation factor c

78 The six-subunit Origin Recognition Complex (ORC) is believed to be an essential eukaryotic ATPase th

79 heterohexameric origin recognition complex (ORC) is essential for coordinating replication onset.

80 ORC1, the Origin Recognition Complex (ORC) large subunit, is inherited into newly born cells a

81 d binding of the origin recognition complex (ORC) occur in a broad domain and that acetylation is hig

82 The origin recognition complex (ORC) of Saccharomyces cerevisiae binds origin DNA and co

83 x facilitated by Origin Recognition Complex (ORC) onto the chromatin during G1 phase of the cell cycl

84 The origin recognition complex (ORC) plays a key role during the initiation of DNA repli

85 Origin recognition complex (ORC) plays critical roles in the initiation of DNA repli

86 The origin recognition complex (ORC) specifies replication origin location.

87 pitation against origin recognition complex (ORC) subunits 2 and 3 showed 93% of initiation peaks to

88 CDKs) target two origin recognition complex (ORC) subunits, Orc2 and Orc6, to inhibit helicase loadin

89 a subunit of the origin recognition complex (ORC) that is a key component of the DNA replication lice

90 its the cellular origin recognition complex (ORC) through an RNA-dependent interaction with EBNA1 lin

91 y binding of the origin recognition complex (ORC) to DNA, but how ORC coordinates symmetrical MCM loa

92 NA1 recruits the origin recognition complex (ORC) to establish a replication origin at one element of

93 Binding of the Origin Recognition Complex (ORC) to origins of replication marks the first step in t

94 Binding of the Origin Recognition Complex (ORC) to replication origins is essential for initiation

95 ion requires the origin recognition complex (ORC), a six-subunit assembly that promotes replisome for

96 alization of the origin recognition complex (ORC), and histone acetylation, yielding important insigh

97 and bound by the origin recognition complex (ORC), and subsequently activated by a cascade of events

98 re-RC) proteins: origin recognition complex (ORC), CDC-6, and CDT-1.

99 The origin recognition complex (ORC), Cdc6 and Cdt1 load Mcm2-7 into a double hexamer bo

100 Origin recognition complex (ORC), Cdc6, and Cdt1 assemble two MCM2-7 hexamers into o

101 DNA requires the origin recognition complex (ORC), Cdc6, and Cdt1, and depends on ATP.

102 Cs) requires the Origin Recognition Complex (ORC), Cdc6, and Cdt1.

103 he action of the origin recognition complex (ORC), Cdc6, Cdt1, and the Mcm2-7 complex.

104 e hexamer by the origin recognition complex (ORC), Cdt1 and Cdc6; the helicase is then activated by a

105 t subunit of the origin recognition complex (ORC), directly binds to septin complex and facilitates s

106 We identify the origin recognition complex (ORC), including LRWD1 as a subunit, to be a methylation-

107 re marked by the origin recognition complex (ORC), which coordinates Mcm2-7 helicase loading to form

108 are bound by the origin recognition complex (ORC), which scaffolds assembly of a pre-replicative comp

109 taining protein, origin recognition complex (ORC)-associated (ORCA/LRWD1), plays a crucial role in st

110 cursors, and the origin recognition complex (ORC)-Cdc6-Cdt1-Mcm2-7 (OCCM) intermediate showed that ea

111 by a six-protein origin recognition complex (ORC).

112 teracts with the origin replication complex (ORC), a protein complex involved in both initiation of D

113 plex components (origin recognition complex [ORC] and minichromosome maintenance [MCM] complex).

114 proteins form origin recognition complexes (ORCs) that bind to replication origins during most of th

115 lation of TRF2 is important for coordinating ORC binding with chromatin remodeling during the early S

116 Open radical cystectomy (ORC) and pelvic lymph node dissection (PLND) is the stan

117 The complex sequence features that define ORC binding sites are highly correlated with nucleosome

118 DAFC-34B occurs in the absence of detectable ORC, although MCMs are present, suggesting a new amplifi

119 describe the crystal structure of Drosophila ORC at 3.5 A resolution, showing that the 270 kilodalton

120 The smallest Drosophila ORC subunit, Orc6, is important for both DNA replication

121 ima facie, our data indicate that Drosophila ORC can switch between active and autoinhibited conforma

122 s loaded onto DNA as a single hexamer during ORC/Cdc6/Cdt1/MCM2-7 complex formation prior to MCM2-7 d

123 1 appears to act independently of the entire ORC, as other subunits of the complex, Orc4 and Orc5, ar

124 defined positions adjacent to the essential ORC-binding site within Saccharomyces cerevisiae origin

125 DNA elements; however, in higher eukaryotes, ORC exhibits little sequence specificity in vitro or in

126 At first, ORC/Cdc6 recruits with the help of Cdt1 a single MCM2-7

127 st that Orc1 acts as a nucleating center for ORC assembly and then pre-replication complex assembly b

128 s highly dependent on the Orc1BAH domain for ORC association (orc1bahDelta-sensitive origins).

129 resent a preferred nucleosomal landscape for ORC association.

130 ow that the Orc1BAH domain was necessary for ORC's stable association with yeast chromosomes, and was

131 sential for nuclear localization but not for ORC assembly.

132 acterized domain of Orc3 and is required for ORC function and MCM2-7 loading in vivo.

133 This study describes additional roles for ORC in the architecture of silenced chromatin.

134 observed have not been described before: GFP-ORC-1 bound chromatin independently of ORC-2-5, and CDC-

135 for examining conserved mechanisms governing ORC's selection of origins within eukaryotic chromosomes

136 in recognition complex (ORC) to DNA, but how ORC coordinates symmetrical MCM loading is unclear.

137 in proteins in a variety of species, but how ORC functions in heterochromatin assembly remains unclea

138 l. use single-molecule imaging to reveal how ORC, Cdc6, and Cdt1 cooperate to load MCM2-7 onto DNA, e

139 maintain a nucleosome-free origin; however, ORC is required for the precise positioning of nucleosom

140 isolated proteins that interact with the HP1/ORC-associated protein (HOAP) capping protein, and ident

141 rt the structure of the active form of human ORC determined by X-ray crystallography and cryo-electro

142 Previous studies identified a soluble human ORC(2-5) complex in the nucleus, an ORC(1-5) complex bou

143 ulation of stochastic firing from identified ORC sites is in accord with replication timing data.

144 m2-7 release if components are missing or if ORC has been inactivated by cyclin-dependent kinase phos

145 ctly regulating pre-RC components, including ORC, Cdc6, Cdt1, and Mcm2-7.

146 gesting other chromosomal features influence ORC binding.

147 for the switch between active and inhibited ORC function at the G1-to-S-phase transition.

148 fined, only single roadblocks that inhibited ORC-DNA binding showed helicase loading defects.

149 a single MCM2-7 hexamer to form an 'initial' ORC/Cdc6/Cdt1/MCM2-7 complex.

150 only the OCM complex, but not the 'initial' ORC/Cdc6/Cdt1/MCM2-7 complex, is competent for MCM2-7 di

151 Instead, ORC binds nonspecifically to open (DNase I-hypersensitiv

152 nucleus where they can either assemble into ORC(1-6) or function individually.

153 der, impedes proper recruitment of Orc6 into ORC; biochemical studies reveal that this region of Orc6

154 ited to the silencers at HML and HMR via its ORC interacting region (OIR), which binds the bromo adja

155 ukaryote, appears to express an archaea-like ORC consisting of a single Orc1/Cdc6-like protein.

156 the presence of competitor DNA and limiting ORC concentrations, replication becomes origin-dependent

157 The helicase loaders ORC-Cdc6 function to recruit a single Cdt1-Mcm2-7 heptam

158 In contrast, dynamic domains exhibited low ORC densities in both cell types, suggesting that origin

159 Using high-throughput sequencing to map ORC binding and nucleosome positioning, we show that yea

160 sion yeast and show that similar to metazoa, ORC binding is periodic during the cell cycle, increasin

161 l overlap between budding yeast and metazoan ORC has been unclear.

162 atin must play an important role in metazoan ORC's ability to recognize origins, it is unclear whethe

163 ermined the subunit organization of metazoan ORC, revealing that it adopts a global architecture very

164 In particular, metazoan ORC shows no obvious DNA sequence specificity, whereas y

165 In metazoans, ORC associates with origin DNA during G1 and with hetero

166 e similar properties, but there are far more ORC sites in early replicating regions.

167 Moreover, ORC could be recruited to the silencers lacking an ACS t

168 We show that, in human cells, multiple ORC subunits associate with hetereochromatin protein 1 (

169 y number restored, neither transcription nor ORC binding is reinstated.

170 ntigen (PCNA), and polymerase delta, but not ORC and MCM proteins.

171 onto DNA requires the combined activities of ORC, Cdc6, and Cdt1.

172 s with and stimulates the ATPase activity of ORC-Cdc6.

173 Genome-wide analyses of ORC binding in ORC1 and orc1bahDelta cells revealed that

174 G1/S boundary, Orc3 facilitates assembly of ORC/HP1 proteins to chromatin.

175 results suggest ORCA-mediated association of ORC to chromatin is critical to initiate preRC assembly

176 h ORC and modulates chromatin association of ORC.

177 However, what regulates the binding of ORC to chromatin is not understood.

178 lation of some lysines depends on binding of ORC to the origin, suggesting that multiple histone acet

179 Here we show that ORC1--a component of ORC (origin of replication complex), which mediates pre-

180 tor, TbORC1B, is not a static constituent of ORC but displays S-phase restricted nuclear localization

181 r cell cycle and/or developmental control of ORC functions.

182 The density of ORC binding along the chromosome is reflected in the tim

183 plicating sequences having a high density of ORC binding.

184 destruction, with subsequent dissociation of ORC from chromosomes.

185 se loading is accompanied by dissociation of ORC, Cdc6, and Cdt1 from origin DNA.

186 investigated the genome-wide distribution of ORC in Drosophila and found that ORC localizes to specif

187 me mutations in Orc6 impair the formation of ORC hexamers, interfering with appropriate ORC functions

188 on an intact WD40 domain but independent of ORC proteins.

189 , and CDC-6 bound chromatin independently of ORC, whereas CDT-1 and MCM-2-7 DNA binding was interdepe

190 : GFP-ORC-1 bound chromatin independently of ORC-2-5, and CDC-6 bound chromatin independently of ORC,

191 on of helicase loading without inhibition of ORC-DNA binding only when roadblocks were placed on both

192 itiation peaks to localize at/within 1 kb of ORC binding sites.

193 and embryonic stem cells results in loss of ORC association to chromatin, concomitant reduction of M

194 molecule of ORCA can bind to one molecule of ORC, one molecule of Cdt1, and two molecules of geminin.

195 Large genomic regions with a paucity of ORC sites are strongly associated with common fragile si

196 ing helicase loading, CDK phosphorylation of ORC causes a twofold reduction of initial Cdt1/Mcm2-7 re

197 mportantly, CDK-dependent phosphorylation of ORC inhibits OCM establishment to ensure once per cell c

198 We propose that differential recruitment of ORC to origins during mitosis followed by competition am

199 nding affinity and functional recruitment of ORC.

200 lify, a consequence of distant repression of ORC binding and origin activation.

201 r results demonstrate that specific sites of ORC and MCM enrichment can be detected within a mammalia

202 initiation activity surrounding the sites of ORC and MCM enrichment.

203 we found a high concordance between sites of ORC binding and cohesin loading, suggesting that, in add

204 udies indicate that multiple subcomplexes of ORC exist at heterochromatin, with Orc1 stably associati

205 s, the level of Orc1, the largest subunit of ORC, is regulated during the cell division cycle, and th

206 The largest subunit of ORC, Orc1, is particularly interesting because it contai

207 In contrast, one ORC molecule directs loading of both helicases in each d

208 , an ancient unicellular eukaryote, only one ORC-related initiator, TbORC1/CDC6, has been identified

209 It colocalized GABA and MIP but not AT or ORC immunoreactivity.

210 epeat domain-containing protein 1 (LRWD1) or ORC-associated (ORCA) in human cells that interacts with

211 ecule pull-down assays demonstrate that ORCA-ORC (Origin Recognition Complex) and multiple H3K9 KMTs

212 oinhibitory peptides (MIPs), and orcokinins (ORCs) were part of both entrainment pathways, whereas al

213 pairs ORC1 occupancy at replication origins, ORC chromatin loading and cell-cycle progression.

214 otein that binds weakly, if at all, to other ORC subunits.

215 h heterochromatin in G1 phase, whereas other ORC subunits have transient interactions throughout the

216 t proteins that did not co-purify with other ORC subunits.

217 In G(2) phase, ORC bound to all tested sequences in a 60 kb interval sp

218 During S phase, ORC and CDC-6 were excluded from nuclei, and DNA was ove

219 rotein occupancy profiles resolved a precise ORC-dependent footprint at 269 origins in G2.

220 ture of yeast origin architecture to promote ORC binding and origin activity, and helps explain why a

221 ding yeast, the eukaryotic initiator protein ORC (origin recognition complex) binds to a bipartite se

222 BNA1's DNA-binding domain is able to recruit ORC to DS, but either this step or subsequent replicatio

223 hat TRF2 amino-terminal GAR domain recruited ORC to telomeres.

224 ion status plays a direct role in recruiting ORC through the binding properties of ORC1 and ORCA/LRWD

225 e demonstrate that ORCA efficiently recruits ORC to chromatin.

226 MCM-2-7 chromatin loading further reduced ORC and CDC-6 DNA binding.

227 involved in helicase loading or in releasing ORC from loaded MCM2-7.

228 Remarkably, ORC and Mcm6 associated with just the ARS1-A replicator

229 esting that, in addition to DNA replication, ORC may be required for the loading of cohesin on DNA in

230 This reaction requires ORC and Cdc6 ATPase activity, but it is unknown how thes

231 e hexamer at origins in a reaction requiring ORC, Cdc6, and Cdt1, also called pre-replicative complex

232 re defined at the level of origin selection (ORC binding) and likely mediated by chromatin accessibil

233 Significantly, ORC is bound across domains spanning 10 or more kilobase

234 n interactions exist between four of the six ORC subunits, unanticipated features are also evident.

235 mans, the DNA sequence elements that specify ORC binding are not.

236 at being an NDR is not sufficient to specify ORC binding.

237 contribute in an additive manner to specify ORC-binding sites.

238 C-associated protein (ORCA/LRWD1) stabilizes ORC on chromatin.

239 /LRWD1), plays a crucial role in stabilizing ORC to chromatin.

240 occupancy only in G1, suggesting that stable ORC chromatin association in G2 is a determinant of orig

241 Here we show that stable ORC(1-6) complexes also can be purified from human cell

242 Here, we have mapped sites of biotin-tagged ORC and MCM protein binding in G1-synchronized populatio

243 We find that ORC and ONRC inhibit fibroblast proliferation, migration

244 differentiated metazoan tissue, we find that ORC binding is dramatically reduced within these large d

245 ribution of ORC in Drosophila and found that ORC localizes to specific chromosomal locations in the a

246 precipitation (ChIP) analysis, we found that ORC physically interacts throughout the internal regions

247 The results indicate that ORC binding sites and other essential origin sequences a

248 Comparative analyses indicate that ORC encircles DNA, using its winged-helix domain face to

249 We propose that ORC is stochastically deposited onto newly replicated no

250 itioning information in silico revealed that ORC and MCM map to regions of low measured and predicted

251 Here we show that ORC and Cdc6 mutants defective in ATP hydrolysis are com

252 We show that ORC can locate and stably bind origins within large trac

253 ng a chemical biology approach, we show that ORC-Cdc6-Cdt1-dependent helicase loading occurs through

254 This work shows that ORC architecture and regulation are diverged features of

255 binding to heterochromatin, suggesting that ORC and HP1 proteins are mutually required for each othe

256 cific transcription factors, suggesting that ORC is not bound or recruited to specific DNA sequences.

257 complementarity to 26T RNA, suggesting that ORC is recruited to these sites by an RNA-independent me

258 action at satellite repeats, suggesting that ORC together with HP1 proteins may be involved in organi

259 The ORC binding profile is broader than those of sequence-sp

260 The ORC-associated protein (ORCA/LRWD1) stabilizes ORC on ch

261 yotic replication origins are defined by the ORC-dependent loading of the Mcm2-7 helicase complex ont

262 Thus, either the ORC ring lacking a subunit, even its ATPase subunit, can

263 edicted to affect ATP binding, influence the ORC-Cdc6 interaction and MCM2-7 recruitment.

264 in, Orc1b, as an additional component of the ORC and showed that both Orc1b and Orc1/Cdc6 associate w

265 lpha-satellite sequences for proteins of the ORC complex, suggesting that CENP-B may have a role in r

266 We further show that the dynamics of the ORC-Cdc6 interaction dictate Mcm2-7 loading specificity

267 ATP-hydrolysis promotes the formation of the ORC/Cdc6/MCM2-7 (OCM) complex, which functions in MCM2-7

268 and helps explain why a strong match to the ORC binding site is insufficient to identify origins wit

269 active helicase complex, associate with the ORC, and regulate DNA replication remains unknown.

270 ted during the cell division cycle, and thus ORC is a dynamic complex.

271 In addition to binding to ORC, ORCA associates with Cdt1 and its inhibitor, gemini

272 al recruitment of the Cdt1/Mcm2-7 complex to ORC.

273 ealed that the Orc1BAH domain contributed to ORC's association with most yeast origins, including a c

274 s into how the Orc1BAH domain contributes to ORC's selection of replication origins, as well as new t

275 n E/Cdk2 activity were strictly localized to ORC binding sites.

276 with sufficient follow-up to compare MIRC to ORC for the treatment of invasive BCa before the oncolog

277 that replication timing is due primarily to ORC density and stochastic firing of origins.

278 there is a vast excess of Mcm2-7 relative to ORC assembled onto chromatin in G1.

279 fficient MCM loading requires binding of two ORC molecules to two ORC binding sites.

280 requires binding of two ORC molecules to two ORC binding sites.

281 e complex provides a basis for understanding ORC activity as well as molecular defects observed in Me

282 CM open for DNA entry and bound to ATP until ORC-Cdc6 triggers ATP hydrolysis by MCM, promoting both

283 itional origin sequence known to be a weaker ORC-DNA-binding site.

284 ilar among developmental stages during which ORC is or is not bound, indicating that being an NDR is

285 ORCA colocalizes with ORC and shows similar cell-cycle dynamics.

286 trongly inhibited by ONRC when compared with ORC (p < 0.05).

287 with locally advanced disease compared with ORC series.

288 ng were observed for ONRC when compared with ORC.

289 and ORC turned over rapidly, consistent with ORC/CDC-6 loading multiple MCM-2-7 complexes.

290 that TERRA facilitates TRF2 interaction with ORC and plays a central role in telomere structural main

291 ed (ORCA) in human cells that interacts with ORC and modulates chromatin association of ORC.

292 to the MCM2-7 double-hexamer, interacts with ORC/Cdc6 and is salt-sensitive, classifying the arrested

293 omplexes exhibit little co-localization with ORC or replication foci and can function as dormant orig

294 ivated origins, and interact physically with ORC, providing a plausible mechanism to cluster origins.

295 atch the lower pH values typically seen with ORC and ONRC, significant differences in cell proliferat

296 sts grown in collagen-gels were treated with ORC or ONRC, and ECM contraction was measured utilizing

297 al fibroblasts were inoculated in vitro with ORC and ONRC.

298 -studied replication origin with and without ORC binding.

299 lear whether chromatin plays a role in yeast ORC's recognition of origins.

300 ious DNA sequence specificity, whereas yeast ORC binds to a specific DNA sequence within all yeast or