ライフサイエンスコーパス: histone tail

1 4R/V selectively affects H3K36me on the same histone tail.

2 lated at lysine 23, H3K23ac) within the same histone tail.

3 dapted for specific recognition of the basic histone tail.

4 site, possibly due to its interaction with a histone tail.

5 range, particularly involving their flexible histone tails.

6 their recognition of acetyl-lysine modified histone tails.

7 ranslational modifications that occur in the histone tails.

8 by removing covalent acetylation marks from histone tails.

9 in the absence of repression mediated by the histone tails.

10 ational histone modifications and unmodified histone tails.

11 DACs) are known to remove acetyl groups from histone tails.

12 scription corepressors through deacetylating histone tails.

13 methylation of methylated lysine residues on histone tails.

14 scription by binding methylarginine marks on histone tails.

15 of acetyl groups from lysine residues within histone tails.

16 n chromatin compaction by binding with basic histone tails.

17 sidue-specific alterations in acetylation of histone tails.

18 dependent on nucleosomal features other than histone tails.

19 and the affinity of Sir3/4 for deacetylated histone tails.

20 t studies have focused on the acetylation of histone tails.

21 tin structure and the modification status of histone tails.

22 on through the removal of acetyl groups from histone tails.

23 governing post-translational modification of histone tails.

24 required for its ability to bind methylated histone tails.

25 4p is to overcome repression mediated by the histone tails.

26 t or improperly treated in models with rigid histone tails.

27 oligonucleosomes that incorporates flexible histone tails.

28 means of post-translational modification of histone tails.

29 s as a result of the spatial distribution of histone tails.

30 to the covalent modifications of nucleosomal histone tails.

31 e Sir3 and Sir4 proteins with hypoacetylated histone tails.

32 roteins is regulated by their affinities for histone tails.

33 HD1 chromodomains, and its interactions with histone tails.

34 Sir3, and Sir4 proteins with each other and histone tails.

35 lycomb proteins requires nucleosomes but not histone tails.

36 erlap among the gene sets regulated by these histone tails.

37 et genes by methylating arginine residues on histone tails.

38 protein shows altered binding to acetylated histone tails.

39 reviously shown for acetylated lysines in H3 histone tails.

40 6 (PRMT6) is a nuclear enzyme that modifies histone tails.

41 rete acetyllysine residues on the N-terminal histone tails.

42 metric dimethylation of arginine residues on histone tails.

43 -trans conversion of proline residues within histone tails.

44 the interaction of BET BRDs with acetylated histone tails.

45 the post-translational modifications to the histone tails.

46 ctions: 1) nucleosome positioning by binding histone tails; 2) recruitment of histone deacetylases; a

47 Although the correlation between histone tail acetylation and gene activation is firmly e

48 modifications that have been characterized, histone tail acetylation is most strongly correlated wit

49 al tails as well as the effect of a targeted histone tail acetylation on the compaction state of the

50 t on telomere replication timing mediated by histone tail acetylation.

51 ated with chromatin modifications (increased histone-tail acetylation).

52 g throughout the nucleosome, suggesting that histone tails affect a common step at most points during

53 Covalent modifications of histone-tail amino acid residues communicate information

54 s dual functions of binding the unmethylated histone tail and activating DNA methyltransferase.

55 This liberates positive charges on the histone tail and allows for tighter winding of DNA, prev

56 pon extended time of association between the histone tail and COMPASS.

57 ate kinetics of peptides representing the H4 histone tail and demonstrate that a C-terminally conjuga

58 ncreasing the effective concentration of the histone tail and permitting successive cycles of H4 tail

59 tion does not change the charge state of the histone tail and such aromatic-cage mediated recognition

60 acetylation modifies the disordered state of histone tails and affects their function.

61 complexes, but archaeal histones do not have histone tails and archaeal genome sequences provide no e

62 lyze the demethylation of lysine residues on histone tails and are associated with diverse human dise

63 proteins bind acetylated lysine residues on histone tails and are involved in the recruitment of add

64 enosylmethionine (SAM) to lysine residues in histone tails and core histones.

65 analyzed their effect on the organization of histone tails and linker histone H1 in nucleosomes.

66 ated in the recognition of lysine-methylated histone tails and nucleic acids.

67 g chromatin subunits, especially between the histone tails and parental nucleosome cores.

68 ing transcription through reading acetylated histone tails and recruiting transcription complexes.

69 been unable to detect an interaction between histone tails and the chromodomain of Tf1 IN, it is poss

70 Lysines are acetylated in histone tails and the core domain/lateral surface of his

71 Covalent modifications of the histone tails and the cross talk between these modificat

72 the coupling between the conformation of the histone tails and the DNA geometry.

73 The distinct contributions of histone tails and their acetylation to nucleosomal stabi

74 molecular level description of the effect of histone tails and their charge modifications on chromati

75 Histone tails and their epigenetic modifications play cr

76 Histone tails and their posttranslational modifications

77 s opens new avenues for studying the role of histone tails and their variants in mediating gene expre

78 omains bind to acetylated lysine residues on histone tails and thereby facilitate the reading of the

79 ethyl groups from the lysine residues of the histone tails and thereby regulate the transcriptional a

80 and analyzed their affinities to acetylated histone tails and to the BET inhibitor JQ1 using several

81 6me3 and H3K27me3 rarely coexist on the same histone tail, and that this antagonism is functionally i

82 leosomal and linker DNA, unburied regions of histone tails, and exposed chromatin surfaces; ionic scr

83 atalyzes the removal of acetyl moieties from histone tails, and is critically involved in regulating

84 tic marks (DNA methylation, modifications of histone tails, and noncoding RNAs) work in concert with

85 Posttranslational modifications of histone tails are an important factor regulating chromat

86 In contrast, the histone tails are compacted in H2A.B nucleosomes compare

87 internucleosomal interactions involving the histone tails are essential for highly efficient, long-r

88 While acetylated lysines in histone tails are frequently recognized by other factors

89 In epigenetic signaling pathways, histone tails are heavily modified, resulting in the rec

90 Histone tails are highly flexible N- or C-terminal protr

91 covalent posttranslational modifications of histone tails are interpreted by the cell to yield a ric

92 Histone tails are known to be mono- and dimethylated on

93 Regions in PRC2 that interact with modified histone tails are localized near the methyltransferase s

94 sing a discrete elastic chain model; and the histone tails are modeled using a bead/chain hydrodynami

95 Analyses indicate that the H4 histone tails are most important in terms of mediating i

96 lvent models show that large portions of the histone tails are not bound to DNA, supporting the compl

97 ystallography at near-atomic resolution, the histone tails are not observed in this structure.

98 On a molecular scale histone tails are polyelectrolytes with high degree of c

99 it is not known what binding elements in the histone tails are recognized by the individual Importins

100 N-terminal histone tails are subject to many posttranslational modi

101 cleosomes yields positional distributions of histone tails around nucleosomes and illuminates the nat

102 better than its predecessors, which modeled histone tails as rigid entities.

103 ng sequential modification of and binding to histone tails, as observed for other silencing proteins.

104 and dynamics of the corresponding atomistic histone tails at different salt conditions.

105 o knockdown, we found that citrullination of histone tails at H4R3 and H3R2/8/17 were markedly reduce

106 f HT can be negated by either removal of the histone tails at low salt concentrations or disruption o

107 ut the macrophage genome, HDAC3 deacetylates histone tails at regulatory regions, leading to repressi

108 ne activity by posttranslationally modifying histone tails at target promoters.

109 Mono-ubiquitination of H2B in the histone tail (at Lys-123 in yeast or Lys-120 in humans)

110 both the structural and dynamical aspects of histone tails, because of which their conformational beh

111 Therefore, this is a prime example of histone tail binding by a PHD finger (of Pygo) being mod

112 gy (BAH) domain of Sir3 is a nucleosome- and histone-tail-binding domain and that its binding to nucl

113 y in the absence of an activating methylated histone tail bound to the complex.

114 ly activates transcription by modifying core histone tails but also terminates hormone signaling by d

115 in interaction required the presence of core histone tails but binding was independent of the presenc

116 Most of these occur within the histone tails, but a few have been identified within the

117 (HDACs) tightly regulate the acetylation of histone tails, but little is known about the functional

118 ranslational modifications (PTMs) present on histone tails, but these methods do not generally reveal

119 of increasing acetylation on the isolated H4 histone tail by characterizing the conformational ensemb

120 neral mechanism, e.g., in the recognition of histone tails by bromodomains.

121 2b and ADA3 for the efficient acetylation of histone tails by GCN5.

122 the interaction of the packaged DNA and the histone tails by increasing the buffer's ionic strength.

123 may result in specific recognition of the H4 histone tails by protein or DNA binding partners.

124 budding yeast involves the deacetylation of histone tails by Sir2 and the association of the Sir3 an

125 stic insights into recognition of methylated histone tails by tudor domains and reveals the structura

126 ed by chromatin and that hyperacetylation of histone tails, by allowing the access of positively acti

127 terminal domain of EED specifically binds to histone tails carrying trimethyl-lysine residues associa

128 Acetylation of the histone tails, catalyzed by histone acetyltransferases (

129 omplexes or mutations directly affecting the histone tails, causes developmental disorders or has a r

130 embryo development transitions by catalyzing histone tail citrullination, which facilitates early emb

131 However, the significance and regulation of histone tail clipping largely remains unclear.

132 esence of multiple modifications on a single-histone tail (combinatorial codes).

133 We found that certain histone tail conformations promoted DNA bulging near its

134 NA methylation and covalent modifications of histone tails contribute to changes in chromatin archite

135 In particular, our model with flexible histone tails: correctly accounts for salt-dependent con

136 Histone tail covalent modifications have been extensivel

137 iating internucleosomal interactions, the H3 histone tails crucially screen the electrostatic repulsi

138 -stimulated vulval development: sumoylation, histone tail deacetylation, methylation, and acetylation

139 ions are modulated by salts (KCl, MgCl2) and histone tail deletions (H3, H4 N-terminal), using small-

140 the folded histone core since removal of the histone tails did not perturb the charge transport dynam

141 Post-translational modifications of histone tails direct nuclear processes including transcr

142 specifically altered by regulated changes in histone tail-DNA interactions in chromatin.

143 e the acetylated status of brain nucleosomal histone tail domains and (ii) to regulate brain histone-

144 The core histone tail domains are known to be key regulators of c

145 We conclude that the unmodified core histone tail domains directly negatively influence TFIII

146 We examined whether the removal of the core histone tail domains from nucleosomes reconstituted with

147 We report here that removal of the core histone tail domains increases the exposure of the DNA b

148 Lysine acetylation within the core histone tail domains inhibits self-association, an effec

149 The core histone tail domains mediate inter-nucleosomal interacti

150 The core histone tail domains play a central role in chromatin st

151 ailless core histones indicate that the core histone tail domains play a direct role in restricting t

152 tylation of specific lysines within the core histone tail domains plays a critical role in regulating

153 st an additional mechanism by which the core histone tail domains regulate the binding of trans-actin

154 sing reconstituted templates, removal of the histone tail domains stimulates TFIIIA binding to the 5S

155 ional repositioning upon removal of the core histone tail domains under physiological conditions, ind

156 conformational complexity of linker DNA and histone tail domains upon compact folding of the fiber.

157 r, HMGNs affect the interactions of the core histone tail domains with nucleosomal DNA, redirecting t

158 ty that is partially redundant with the core histone tail domains.

159 ucleosomal interactions mediated by the core histone tail domains.

160 e genome were not altered by removal of core histone tail domains.

161 quantify interarray interactions mediated by histone tail domains.

162 esidues embedded in intrinsically disordered histone tail domains.

163 dynamic interplay among epigenetic marks on histone tails during transcription.

164 Therefore, the histone tail dynamics may function to regulate the flexi

165 the nucleosome core, and (2) the N-terminal histone tails for effective silencing at telomeres.

166 clamp that induces the detachment of the H3 histone tail from the nucleosomal DNA to make it availab

167 yme binds nucleosomes to disengage substrate histone tails from nucleosomal DNA.

168 it allows for the characterization of intact histone tails (>50 aa) rather than short (<20 aa) peptid

169 6 enzymatic activity on synthetic acetylated histone tails (H3K9Ac) by measuring products of the deac

170 We performed simulations for all four histone tails, H4, H3, H2A, and H2B, isolated and with i

171 dynamics (REMD) simulations for each of four histone tails, H4, H3, H2B, and H2A, and probed their in

172 Clipping of histone tails has been reported in several organisms.

173 n recent years, the covalent modification of histone tails has emerged as a crucial step in controlli

174 Covalent modifications of histone tails have a key role in regulating chromatin st

175 synergistically to histone binding while the histone tails have a slightly repressive effect on bindi

176 s of post-translational modifications of the histone tails have been revealed, but a few modification

177 induced by acetylation and deacetylation of histone tails have gained wide attention.

178 The role of each histone tail in regulating chromatin structure is elucid

179 Posttranslational modifications of histone tails in chromatin template can result from envi

180 ublicly available experimental structures of histone tails in complex with human proteins.

181 ar dynamics simulations of dinucleosomes and histone tails in explicit solvent and ions, performed wi

182 We also determine roles for the histone tails in free histone and nucleosome binding by

183 n and recognition of the unmodified state on histone tails in general might be just as crucial as pos

184 covalent modifications are known to occur on histone tails in HTLV-1 infection (i.e., histone acetylt

185 s that continuously modify and de-modify the histone tails in nucleosomes.

186 ating a requirement for one or both of these histone tails in Rpd3p-mediated regulation for many gene

187 Here, we investigated the conformation of histone tails in the nucleosome by solution NMR.

188 ystematic computational study of the role of histone tails in the nucleosome, using replica exchange

189 e (SAGA) coactivator complex hyperacetylates histone tails in vivo in a manner that depends upon hist

190 ion (DiSCO) model of the nucleosome with all histone tails incorporated to describe by Monte Carlo si

191 However, the structural mechanisms by which histone tails influence the interconversion between acti

192 ying the salt concentration and removing the histone tails influence the structure of the NCP in know

193 e bromodomains, motifs for acetyl-lysine and histone tail interaction.

194 We also find that bromodomain/acetylated histone tail interactions can contribute to this targeti

195 btain a systems-level view of the histone H3 histone tail interactome.

196 We suggest that the charge of the histone tail is a major determinant in allowing INHAT to

197 Acetylation of histone tails is a major post-translational modification

198 Methylation of lysine residues on histone tails is an epigenetic mark that influences chro

199 Methylation of lysine residues on histone tails is an important epigenetic modification th

200 force fields, the secondary structure of the histone tails is destabilized.

201 Methylation of lysine residues in histone tails is dynamically regulated by the opposing a

202 Post-translational acetylation of histone tails is often required for the recruitment of A

203 The acetylation status of lysine residues in histone tails is one of a number of epigenetic post-tran

204 Methylation of specific amino acids in histone tails is responsible for packaging DNA into cond

205 ted by covalent modifications present on the histone tail itself.

206 Covalent modifications of histone tails known thus far include acetylation, phosph

207 regions, and a catalytic core targeting the histone tails, LSD1-CoREST (lysine-specific demethylase

208 lase 1 (LSD1)-catalyzed demethylation of the histone tail lysine (H3K4), with flavin adenine dinucleo

209 yields the experimentally obtained values of histone-tail mediated core/core attraction energies; and

210 Both features have been suggested to reflect histone tail-mediated internucleosomal interactions; the

211 Specific sites of histone tail methylation are associated with transcripti

212 provide direct evidence that the epigenetic histone tail modification of H3S10 phosphorylation at in

213 ore and linker DNA modulate the processes of histone tail modifications and binding of the effector p

214 DNA bound into nucleosomes is facilitated by histone tail modifications and chromatin remodeling comp

215 we found that genome-wide levels of specific histone tail modifications are markedly altered in postd

216 This model suggests that histone tail modifications associated with activation of

217 l mechanism by which various combinations of histone tail modifications can be used to control access

218 tageous for epigenetic control because their histone tail modifications can have a greater effect com

219 ays revealed RNA polymerase II occupancy and histone tail modifications consistent with transcription

220 Histone tail modifications control many nuclear processe

221 Because histone tail modifications in chromatin are linked to ge

222 atency, particularly with regard to specific histone tail modifications such as acetylation and dimet

223 such as DNA methylation, post-translational histone tail modifications, noncoding RNA control of chr

224 tags, including DNA methylation and covalent histone tail modifications, such as acetylation, methyla

225 A methylation, DNA demethylation, and common histone tail modifications.

226 e extensively and significantly enriched for histone-tail modifications and transcription factor bind

227 Local changes in histone-tail modifications are not apparent.

228 Histone-tail modifications play a fundamental role in th

229 or nucleosome mobilization; instead, the H2A histone tail negatively regulates nucleosome movement by

230 association of the CTD with the deacetylated histone tails of H3 and H4 that is necessary for the rec

231 The binding to histone tails of the human class A paralogue, which has

232 promising alternative to model the effect of histone tails on chromatin folding.

233 We determined the effect of the N-terminal histone tails on nucleosome traversal by yeast and human

234 ggests that ING4 can bind simultaneously two histone tails on the same or different nucleosomes.

235 he lysine acetylation specificity of GCN5 on histone tails or full-length histones was not changed wh

236 accomplished by covalent modification of the histone tails or the replacement of the canonical histon

237 ely followed by a Ser residue are present in histone tails, our studies reveal a potential new mechan

238 t two tyrosines (Y24 and Y48) bind to a Kme3-histone tail peptide via cation-pi interactions, but lin

239 or endogenous hATAC or hSAGA complexes using histone tail peptides and full-length histones as substr

240 Epigenetic modifications of histone tails play an essential role in the regulation o

241 Histone tails play an important role in gene transcripti

242 Localized chromatin modifications of histone tails play an important role in regulating gene

243 Comparing the effects of asymmetric histone tail point mutants with those of symmetric doubl

244 Histone tail post-translational modification results in

245 portant for successful mitosis and implicate histone tail posttranslational modifications in regulati

246 preferentially recognizes unmethylated H3K4 histone tail, product of KDM5A-mediated demethylation of

247 remove acetyl groups from lysine residues on histone tails, promoting transcriptional repression via

248 tion of the "histone code" in which distinct histone tail-protein interactions promote engagement of

249 We conclude that histone tails provide a significant part of the nucleoso

250 The structural genomics of histone tail recognition web server is an open access re

251 rent H3K4me peptides reveal a unique mode of histone tail recognition: efficient histone binding requ

252 tin formation that includes deacetylation of histone tails, recruitment and deacetylation of histone

253 Variation in patterns of methylations of histone tails reflects and modulates chromatin structure

254 omparable changes in the charge state of the histone tail regions have relatively little effect on th

255 urther demonstrate that HAT-B binding to the histone tail regions is not sufficient for this enhanced

256 Posttranslational modifications of histone tails regulate numerous biological processes inc

257 h" is the only portion of any amino-terminal histone tail required for both target-specific associati

258 ting that domains recognizing the acetylated histone tails reside at the interface between the two lo

259 moving acetyl groups from lysine residues in histone tails, resulting in chromatin condensation.

260 rvations of extensive helical structure in a histone tail, revealing the inherent ability of the H3 t

261 nd combinations of modifications on a single histone tail sequence, identification of a single modifi

262 , di-, and trimethylated lysines on a single histone tail sequence, identification of different modif

263 Reversible methylation of histone tails serves as either a positive signal recogni

264 ally regulated by chromatin modifications on histone tails, such as acetylation.

265 ignificant conformational flexibility of the histone tails suggests that they remain available for pr

266 igenome - a collection of marks on DNA or on histone tails that are established during embryogenesis.

267 n modifiers mediate dynamic modifications of histone tails that are vital to reprogramming cells towa

268 on adds a negative charge to residues of the histone tails that interact with the negatively charged

269 ween Dnmt3-ADD domain with H3K4 unmethylated histone tails that is disrupted by histone H3K4 methylat

270 ranslational modification of the nucleosomal histone tails that is regulated by the balance of histon

271 of an oligonucleosome incorporating flexible histone tails that reproduces the conformational and dyn

272 llers, this involves an interplay between H4 histone tails, the AutoN and NegC motifs of the motor do

273 Histone tails, the intrinsically disordered terminal reg

274 vestigate how each nucleosomal component-the histone tails, the specific histone-DNA contacts, and th

275 to describe the conformational landscape of histone tails, their roles in chromatin compaction, and

276 he BET proteins are known to bind acetylated histone tails, these results also suggest a role of epig

277 mode whereby a disordered peptide binds the histone tail through hydrophobic interactions facilitate

278 complex deposits activating methyl marks on histone tails through a methyltransferase (MT) activity.

279 We find the histone tails to be dispensable for binding to both nucl

280 ls and suggests that compaction, rather than histone tail ubiquitylation, confers Hox gene silencing.

281 We characterized the dynamics of the histone tails upon their condensation on the core and li

282 tterns of conformational dynamics of various histone tails using ideas from physics of polyelectrolyt

283 d, mono-, di-, tri-, and tetra-acetylated H4 histone tails using Replica Exchange Molecular Dynamics

284 It binds to acetylated histone tails via its tandem bromodomains BD1 and BD2 an

285 BET proteins bind acetylated histone tails via their bromodomain, bringing the elonga

286 DH2 transcription induced by deletion of the histone tails was transcription factor- and Snf1-indepen

287 nd linker DNA-nucleosome attractions require histone tails; we find that the H3 tails, in particular,

288 also note that 4% of PTM minimotif sites in histone tails were common variants, which has the potent

289 of the histone octamer), and the removal of histone tails were investigated.

290 ucleosomes, 2) enhances acetylation of an H3 histone tail when the other H3 tail within a nucleosome

291 uration of binding to DNA for the H4 and H2A histone tails, whereas H3 and H2B show multiple binding

292 chanism occurs through lysine acetylation of histone tails which are recognized by bromodomains.

293 Histone tails, which are the terminal segments of the hi

294 Association of the histone tails with 601 DNA at low salt concentrations sh

295 H4K16), suggesting that interactions of the histone tails with the core and linker DNA modulate the

296 switch that induces the local interaction of histone tails with the Dnmt3 ATRX-DNMT3-DNMT3L (ADD) dom

297 Multiple modifications decorate each histone tail within the nucleosome, including some amino

298 this cooperativity occurs only when both H3 histone tails within a nucleosome are properly oriented

299 is responsible for making contacts with the histone tails within nucleosomes for the HAT to catalyze

300 salt-dependent conformational changes in the histone tails; yields the experimentally obtained values