ライフサイエンスコーパス: histone octamer

1 ith the DNA significantly unraveled from the histone octamer.

2 e rotational orientation with respect to the histone octamer.

3 e material made up from DNA wrapped around a histone octamer.

4 nslational and rotational positioning of the histone octamer.

5 completely blocked by interactions with the histone octamer.

6 B dimers or induce a novel alteration in the histone octamer.

7 vation energy for short-range sliding of the histone octamer.

8 individuals having the highest affinity for histone octamer.

9 NA repeat and one molecule of histone H5 per histone octamer.

10 main of residual contact between the DNA and histone octamer.

11 Unassisted, the junction is blocked by a histone octamer.

12 the extent that binding is inhibited by the histone octamer.

13 ly two coils of DNA wrapped around a central histone octamer.

14 interact with DNA on both sides flanking the histone octamer.

15 fine a discrete domain on the surface of the histone octamer.

16 NN3']n motif might resist wrapping around a histone octamer.

17 m DSB formation remained associated with the histone octamer.

18 sotropy dictates how DNA is wrapped around a histone octamer.

19 ed acetylation on the lateral surface of the histone octamer.

20 mers, facilitating uncoiling of DNA from the histone octamer.

21 maged DNA is hindered by the presence of the histone octamer.

22 ased the affinity of these sequences for the histone octamer.

23 ears to intercalate between the DNA gyre and histone octamer.

24 th the side of nucleosomal DNA away from the histone octamer.

25 ces nucleosomal DNA to provide access to the histone octamer.

26 not freely diffuse about the surface of the histone octamer.

27 the chromatin remodeler, SNF2h, distorts the histone octamer.

28 p DNA wrapped around an H2A, H2B, H3, and H4 histone octamer.

29 roximately 147 bases of DNA wrapped around a histone octamer.

30 d found that it is nearly as abundant as the histone octamer.

31 s by altering the position of DNA around the histone octamer.

32 e relative affinity of DNA sequences for the histone octamer.

33 inity of the underlying DNA sequence for the histone octamer.

34 pproximately 1.7 times around a central core histone octamer.

35 relative affinity of every site for the core histone octamer.

36 tails and the core domain/lateral surface of histone octamers.

37 nd may involve the transient displacement of histone octamers.

38 o nucleosomes and via TREs on the surface of histone octamers.

39 to sequences predicted to better accommodate histone octamers.

40 is complexed with H3/H4 tetramers than with histone octamers.

41 er but can branch migrate in regions free of histone octamers.

42 contains one DNA molecule wrapped around two histone octamers.

43 ing dimethylation at R17 in CARM1-methylated histone octamers.

44 mics of force-induced unwrapping of DNA from histone octamers.

45 enetic histone marks, and a region devoid of histone octamers.

46 y external potential and arrays of DNA-bound histone octamers.

47 histones and these have been assembled into histone octamers.

48 es H2A-H2B from preassembled Cse4-containing histone octamers.

49 In the case of mononucleosomes, the histone octamers accumulate at the DNA ends even in the

50 the translational position of the DNA on the histone octamer, accurate nucleosome positioning over re

51 a linear relationship between the extent of histone octamer acetylation and the extent of disruption

52 e sequence-dependent positions that the core histone octamer adopts when reconstituted onto DNA conta

53 ces, which were experimentally found to have histone octamer affinities comparable to the highest-aff

54 rtial, reversible unwrapping of DNA from the histone octamer, allowing hNTH1 to capture its DNA subst

55 e HSE, had unwrapped from the 3' edge of the histone octamer, allowing HSF to bind; approximately 100

56 of whether they face inward or outward from histone octamers along the DNA helix axis.

57 and H4, mediate key interactions between the histone octamer and DNA in forming the nucleosomal parti

58 sted a model in which Isw2 complex binds the histone octamer and DNA separately to generate the force

59 While the structure of the histone octamer and its interaction with the DNA remain

60 titutions to control the loading of both the histone octamer and linker histone onto the 601 DNA arra

61 y conserved Snf5 subunit associates with the histone octamer and not with nucleosomal DNA.

62 ave obtained nucleosome arrays that have one histone octamer and one H5 bound per 200 bp repeat, and

63 cule required for its tight curvature on the histone octamer and the neutralization of the DNA phosph

64 es, termed "altosomes," each composed of two histone octamers and bearing an asymmetrically located r

65 gonucleosome fragments composed of only core histone octamers and DNA possess all of the structural f

66 n average free energy of interaction between histone octamers and DNA, and an average wrapping length

67 nucleosomes assembled with human recombinant histone octamers and nucleosome-positioning DNA containi

68 resulting constructs tested for affinity for histone octamers and translational positioning in in vit

69 d nucleosomal arrays reconstituted from core histone octamers and twelve 208 bp tandem repeats of Lyt

70 ations (neutralizing the acidic patch of the histone octamer), and the removal of histone tails were

71 oxidative lesions relative to the underlying histone octamer, and (iv) the distance between the lesio

72 the Xenopus borealis 5 S rRNA gene, a single histone octamer, and 1 or 2 molecules of histone H1.

73 elix, improves positioning of the DNA on the histone octamer, and stabilizes the nucleosome against d

74 ex with two DNA molecules wrapped around two histone octamers, and an altosome complex that contains

75 ere assembled from wild type and mutant core histone octamers, and Mg(2+)-dependent oligomerization w

76 On some sequences the repositioned histone octamer appears to be moved approximately 45 bp

77 the preferred translational positions of the histone octamer are not affected by this level of UV dam

78 We also find that histone octamers are easily transferred in trans from ss

79 Transcription factors (TFs) and histone octamers are two abundant classes of DNA binding

80 istone octamer, or even partially facing the histone octamer, are fully accessible and that nucleosom

81 istone octamer, or even partially facing the histone octamer, are fully accessible for molecular reco

82 eosomes, which consist of DNA wrapped around histone octamers, are dynamic, and their structure, incl

83 sidues within the N-terminal segments of the histone octamer around which DNA is wrapped in the nucle

84 It consists of a histone octamer associated with approximately 80 base pa

85 n the kinetics and thermodynamics of the DNA-histone octamer association that are required to remodel

86 f the DNA dissociate from the surface of the histone octamer at relatively low ionic strength, under

87 yze DNA sequences that are known to position histone octamers at single translational sites.

88 2B dimers between nucleosomes, and transfers histone octamers between pieces of DNA.

89 the edge of the nucleosome, translocates the histone octamer beyond the DNA ends via a DNA bulge prop

90 sh the relationship between DNA sequence and histone octamer binding affinity.

91 ied the strength of both the chicken or frog histone octamer binding sites on each DNA, the results o

92 have compared the relative free energies for histone octamer binding to various DNA sequences; howeve

93 -K115 and H3-K122 reduces the free energy of histone octamer binding.

94 eosome remodeling factors, not only the core histone octamer but also the H3/H4 tetramer provide an n

95 positioning sequences on the surface of the histone octamer but does cause minor perturbation of nuc

96 that display low intrinsic affinity for the histone octamer, but its contribution to antagonizing RN

97 AP30 complex is active in deacetylating core histone octamers, but inactive in deacetylating nucleoso

98 hese polyamides prevent repositioning of the histone octamer by RNA polymerase, and thereby inhibit p

99 been rotationally phased with respect to the histone octamer by TG motifs.

100 rvation that supports the idea that the core histone octamer can exploit different patterns of sequen

101 h consists of 147 bp of DNA wrapped around a histone octamer composed of two copies each of the histo

102 ay disrupt histone-DNA contacts by affecting histone octamer conformation and through extensive inter

103 Histone octamers consisting of H2A, H2B, H3, and H4 are

104 Purified HeLa core histone octamers containing an average of 2, 6, or 12 ac

105 a specific rotational setting of DNA on the histone octamer core in each of two reconstituted nucleo

106 ers the rotational setting of the DNA on the histone octamer core such that the lesion faces inward,

107 unraveling of the first DNA wrap around the histone octamer, could be mechanically induced in a reve

108 adjacent GAGA factor binding sitesaround the histone octamer creates a unique local DNA conformation.

109 cupancy maps are a sensitive function of the histone octamer density (nucleosome repeat length) and f

110 ink, significantly inhibited ATP-independent histone octamer-DNA sliding.

111 that orienting the flap substrate toward the histone octamer does not significantly alter the rotatio

112 Within the core histone octamer each histone H4 interacts with each H2A-

113 The CBS interacts with the histone octamer, engaging the H2A-H2B acidic patch in a

114 Nucleosomes were reconstituted by histone octamer exchange from chicken erythocyte core pa

115 5S nucleosomes were formed via histone octamer exchange from chicken erythrocyte core p

116 ors, competition of regulatory proteins with histone octamer for access to regulatory target sites re

117 e relative free energy of association of the histone octamer for differing DNA sequences has been ava

118 t allow absolute equilibrium affinity of the histone octamer for DNA to be measured.

119 that SWI-SNF action causes a mobilization of histone octamers for both the mononucleosome and nucleos

120 SWI/SNF complex, catalyzes the transfer of a histone octamer from a nucleosome core particle to naked

121 We find that DNA methylation prevents the histone octamer from interacting with an otherwise high

122 otes histone acetylation and eviction of the histone octamer from the chromatin-assembled HTLV-1 prom

123 n substrate required for dissociation of the histone octamer from the promoter DNA.

124 and its ATPases have the ability to transfer histone octamers from donor nucleosomes to acceptor DNA.

125 n, the DNA contacts at specific sites in the histone octamer had not been changed.

126 consistent with models in which a canonical histone octamer has been 'pushed' off of the end of the

127 ich segments on the surface of reconstituted histone octamers, HMG-I(Y) binding site selection on ind

128 e of unwrapping the nucleosomal DNA from the histone octamer (HO).

129 Tight wrapping of DNA around histone octamers, however, impedes access of repair prot

130 xes can cause translocation (sliding) of the histone octamer in cis along DNA.

131 uenced, their affinities (free energies) for histone octamer in nucleosome reconstitution measured, a

132 % of bulk DNA sequences have an affinity for histone octamer in nucleosomes that is similar to that o

133 of H2A did not affect the positioning of the histone octamer in the nucleosome in either the absence

134 The path of DNA and the conformation of the histone octamer in the nucleosome remodeled or slid by I

135 DNA completes approximately 1.7 turns on the histone octamer in the presence and absence of linker hi

136 tational settings in its wrapping around the histone octamer in the two nucleosomes.

137 DNA to curve gently around proteins such as histone octamers in the nucleosome particle.

138 Here we report that Mit1 mobilizes histone octamers in vitro and requires ATP hydrolysis an

139 ver, upon methylation their affinity for the histone octamer increases and a highly positioned nucleo

140 including those containing novel asymmetric histone octamers, indicate that this cooperativity occur

141 rticle, we demonstrated that histones (H1 or histone octamers) interact with negatively charged bilay

142 ow that SWI/SNF-mediated displacement of the histone octamer is effectively blocked by a barrier intr

143 d, and then, in a slower reaction, an entire histone octamer is lost.

144 indicating that the general integrity of the histone octamer is maintained.

145 These data suggest that perturbation of the histone octamer is not a requirement or a consequence of

146 The histone octamer is predicted to be driven off chromatin

147 gher and lower ionic strengths, the complete histone octamer is transferred over the same distance by

148 Surprisingly, transfer of H2A/H2B dimers and histone octamers is initiated on a time scale of seconds

149 "intact" core histone octamers or "tailless" histone octamers lacking their N-terminal domains.

150 In addition, this mutation destabilizes the histone octamer, leading to defects in chromatin structu

151 her genetic evidence supports the model of a histone octamer-like structure within TFIID.

152 ne octamer, suggesting that TFIID contains a histone octamer-like substructure.

153 studies, the results suggest that there is a histone octamer-like TAF complex within TFIID.

154 nucleosomal barrier and displace the entire histone octamer, matching the observations in vivo.

155 f these substrates does not require dramatic histone octamer movements or displacement.

156 the relative contribution of the individual histone octamer N-terminal tails as well as the effect o

157 nucleosome formation with different types of histone octamers, namely acetylated or unacetylated, and

158 We reconstitute histone octamers, nucleosomes, and nucleosomal arrays be

159 karyotic polymerase can transcribe through a histone octamer on a simple chromatin template.

160 ientation with respect to the surface of the histone octamer on nucleosome structure and FEN1 activit

161 e of the free energy difference between core histone octamers on and off DNA.

162 -2-phenylindole) inhibited the assembly of a histone octamer onto a 192-base pair circular DNA fragme

163 cularly favored in terms of affinity for the histone octamer or for positioning of the reconstituted

164 histone H5, and either native "intact" core histone octamers or "tailless" histone octamers lacking

165 articles (NCPs) dissociate into free DNA and histone octamers (or free histones) on dilution without

166 ites on nucleosomal DNA facing away from the histone octamer, or even partially facing the histone oc

167 ites on nucleosomal DNA facing away from the histone octamer, or even partially facing the histone oc

168 nt histones in the context of free histones, histone octamers, or nucleosomal arrays.

169 a majority of the sample contained both one histone octamer per 5S rDNA repeat and one molecule of h

170 Posttranslational modifications of the histone octamer play important roles in regulating respo

171 t sequence is efficiently wrapped around the histone octamer, preferring to associate with histones a

172 The histone octamer presents different levels of constraints

173 to facilitate both translational movement of histone octamers relative to DNA and the efficient deace

174 ely unperturbed and that the position of the histone octamers relative to the DNA is not altered duri

175 While the histone octamer remains intact, the DNA is lifted from t

176 modifications in the lateral surface of the histone octamer remains unclear.

177 despite the steric constraints placed by the histone octamer remains unknown.

178 cetylation of lateral surface lysines in the histone octamer serves as a crucial regulator of nucleos

179 unchanged upon GAL4 binding, suggesting that histone octamer sliding did not occur.

180 uires a significantly higher temperature for histone octamer sliding in vitro compared to comparable

181 ng the (H3/H4)2 heterotetrameric core of the histone octamer, suggesting that TFIID contains a histon

182 and translational settings of 5S rDNA on the histone octamer surface after induction of up to 0.8 CPD

183 ange in which a stretch of DNA peels off the histone octamer surface as a result of thermal fluctuati

184 holding DNA to the superhelical ramp on the histone octamer surface is obtained from a relatively sm

185 owever, uracils at sites oriented toward the histone octamer surface were excised at much slower rate

186 ansient dynamic exposure of the DNA from the histone octamer surface.

187 peels as much as 50 bp of DNA away from the histone octamer surface.

188 artial dissociation of the DNA ends from the histone octamer surface; however, no dissociation or sub

189 Histone octamer survives moderate transcription, but is

190 ontaneous partial unwrapping of DNA from the histone octamer; that the scaffolding protein XRCC1 enha

191 thymine glycol lesion faced outward from the histone octamer, the human DNA glycosylase NTH1 (hNTH1)

192 in terms of their relative affinity for the histone octamer, their locations with respect to the gen

193 SWI ATPase to pump a DNA distortion over the histone octamer, thereby changing the translational posi

194 dent reaction that favours attachment of the histone octamer to an acceptor site on the same molecule

195 NA-translocase domain to pump DNA around the histone octamer to enable sliding.

196 omatin through its association with the core histone octamer to form the nucleosome core particle (NC

197 However, cross-linking the histone octamer to nucleosomal DNA does not inhibit remo

198 directly with an increased propensity of the histone octamer to reposition with respect to the DNA, a

199 DNA sequence that directed the deposition of histone octamers to a single site, and it was proposed t

200 level of organization, DNA is wrapped around histone octamers to form nucleosomal particles that are

201 and photoaffinity labeling using recombinant histone octamers to require the histone H4 N-terminal ta

202 ription factor Gal4-VP16 can enhance SWI/SNF histone octamer transfer activity, resulting in targeted

203 f SWI/SNF action, whereas few have described histone octamer transfer as the principal outcome.

204 e dimer or lead to alternative fates such as histone octamer transfer to another DNA or sliding along

205 chromatin remodeling complexes, the rates of histone octamer translocation and nucleosome reformation

206 re is composed of nucleosomes, or repetitive histone octamer units typically enfolded by 147 base pai

207 aining an average of two or six acetates per histone octamer was indistinguishable, while a level of

208 lesions whose minor groove faced toward the histone octamer was poor at low hNTH1 concentrations but

209 leosome array reconstituted from recombinant histone octamers, we have defined the relative contribut

210 ons between the nucleosomal DNA ends and the histone octamer were destabilized in A16 NCP.

211 ggest that these complexes each contain five histone octamers which dock to a central Np decamer.

212 Since this DNA sequence binds the histone octamer with much higher affinity than mixed seq

213 pendent on an increased mobility of the core histone octamer with respect to DNA sequence.

214 rs used in this study were derived from pure histone octamers with their native marks.

215 of the recombination signal sequence on the histone octamer, with cleavage of the 12 bp spacer RSS s

216 he increased salt-dependent stability of the histone octamer, with implications for the nucleosome as

217 base pairs remained in association with the histone octamer, with the same translational and rotatio

218 one is oriented away from the surface of the histone octamer, without significant disruption of histo