ライフサイエンスコーパス: histone tail

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

2 dapted for specific recognition of the basic histone tail.

3 lusive with H3K36 trimethylation on the same histone tail.

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

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

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

7 S) methods to resolve such isomers for model histone tails.

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

9 metric dimethylation of arginine residues on histone tails.

10 -trans conversion of proline residues within histone tails.

11 the interaction of BET BRDs with acetylated histone tails.

12 the post-translational modifications to the histone tails.

13 range, particularly involving their flexible histone tails.

14 their recognition of acetyl-lysine modified histone tails.

15 ranslational modifications that occur in the histone tails.

16 by removing covalent acetylation marks from histone tails.

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

18 ational histone modifications and unmodified histone tails.

19 Mediator subunits, histone deacetylases, and histone tails.

20 scription corepressors through deacetylating histone tails.

21 methylation of methylated lysine residues on histone tails.

22 NA others have been found to bind unmodified histone tails.

23 scription by binding methylarginine marks on histone tails.

24 of acetyl groups from lysine residues within histone tails.

25 n chromatin compaction by binding with basic histone tails.

26 dependent on nucleosomal features other than histone tails.

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

28 tin structure and the modification status of histone tails.

29 ers that interact with acetylated lysines of histone tails.

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

31 governing post-translational modification of histone tails.

32 required for its ability to bind methylated histone tails.

33 4p is to overcome repression mediated by the histone tails.

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

35 oligonucleosomes that incorporates flexible histone tails.

36 means of post-translational modification of histone tails.

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

38 to the covalent modifications of nucleosomal histone tails.

39 e Sir3 and Sir4 proteins with hypoacetylated histone tails.

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

41 sidue-specific alterations in acetylation of histone tails.

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

43 et genes by methylating arginine residues on histone tails.

44 ne (KAc) post-translational modifications on histone tails.

45 protein shows altered binding to acetylated histone tails.

46 reviously shown for acetylated lysines in H3 histone tails.

47 The initial evaluation for complete histone tails (50 residues) with diverse post-translatio

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

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

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

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

52 histones and DNA with and without increased histone tail acetylation.

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

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

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

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

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

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

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

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

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

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

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

68 However, the relative role of histone tails and regulatory proteins in the simultaneou

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

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

73 Histone tails and their epigenetic modifications play cr

74 Histone tails and their posttranslational modifications

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

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

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

78 Clec2d recognized poly-basic sequences in histone tails and this recognition was sensitive to post

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

80 6me3 and H3K27me3 rarely coexist on the same histone tail, and that this antagonism is functionally i

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

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

83 zymes show spurious activity on histones and histone tails, and it is unknown how they obtain specifi

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 Although histone tails are important substrates of these enzymes,

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

119 2b and ADA3 for the efficient acetylation of histone tails by GCN5.

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

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

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

123 actor), which involves reading of acetylated histone tails by the bromodomain-containing proteins SMA

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

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

126 k from Farrelly et al. (2019) indicates that histone tails can be serotonylated, suggesting a previou

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

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

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

147 The core histone tail domains mediate inter-nucleosomal interacti

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

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

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

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

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

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

154 ucleosomal interactions mediated by the core histone tail domains.

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

156 quantify interarray interactions mediated by histone tail domains.

157 trate that reconstituted chromatin undergoes histone tail-driven liquid-liquid phase separation (LLPS

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

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

160 While disorder in the histone tails enables a large variation of inter-nucleos

161 and highlight the complex interplay between histone tails, epigenetic enzymes, and modulators of enz

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

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

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

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

166 6 enzymatic activity on synthetic acetylated histone tails (H3K9Ac) by measuring products of the deac

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

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

169 cture via post translational modification of histone tails has been implicated in learning, memory an

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

186 Modifications of histone tails, including lysine/arginine methylation, pr

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

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

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

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

191 lay between DNA-bending nonhistone proteins, histone tails, intrachromatin electrostatic, and other i

192 rinsically disordered, positively charged H4 histone tail is important for chromatin structure and fu

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

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

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

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

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

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

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

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

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

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

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

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

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

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

207 Specific sites of histone tail methylation are associated with transcripti

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

209 arking of chromatin domains with distinctive histone tail modifications (PTMs) and their recognition

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

211 matin accessibility, nucleosome positioning, histone tail modifications and enhancer-promoter interac

212 DNA methylation and histone tail modifications are interrelated mechanisms i

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

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

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

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

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

218 Histone tail modifications control many nuclear processe

219 Because histone tail modifications in chromatin are linked to ge

220 apped the locations of nucleosomes and their histone tail modifications in SV40 minichromosomes and i

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

222 hod for mapping genome-wide distributions of histone tail modifications, histone variants, and chroma

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 tity genes by regulating chromatin state via histone tail modifications.

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

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

229 Histone-tail modifications play a fundamental role in th

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

231 ning acetylated or methylated lysines in the histone tails of H3 and H4 present in the chromatin from

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

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

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

235 histone tails within the same nucleosome or histone tails on neighboring nucleosomes.

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

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

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

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

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

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

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

243 Histone tails play an important role in gene transcripti

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

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

246 Histone tail post-translational modification results in

247 eC/pgRNA) and by assessing cccDNA-associated histone tails post-transcriptional modifications (PTMs)

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

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

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

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

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

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

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

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

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

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

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

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

272 Histone tails, the intrinsically disordered terminal reg

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

289 nd to specific acetylated lysine residues on histone tails where they facilitate the assembly of tran

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

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

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

293 fundamental regulatory role, apart from the histone "tails," which modulate gene activity.

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 d by their ability to sense modifications on histone tails within the same nucleosome or histone tail

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