ライフサイエンスコーパス: chaperonin

1 and in vivo by the TCP-1 ring complex (TRiC) chaperonin.

2 e beta-subunit is likely a substrate for the chaperonin.

3 the method to the Methonococcus maripaludis chaperonin.

4 e, suggesting that GroEL1, like GroEL2, is a chaperonin.

5 e as much Rubisco protein recovered with the chaperonin.

6 f the LSm2-8 protein complex or the CCT/TRiC chaperonin.

7 suggest active mechanisms for the molecular chaperonin.

8 ith the large subunit as it is released from chaperonins.

9 ransfer to downstream chaperones such as the chaperonins.

10 mal and stress-related metabolic function of chaperonins.

11 an optimized synthetic gene and cold-adapted chaperonins.

12 nd quality control mechanisms, which include chaperonins.

13 rate during the nucleotide cycle of group II chaperonins.

14 l studies, is unique to eukaryotic cytosolic chaperonins.

15 driving the conformational cycle of group II chaperonins.

16 units and promote their association with CCT chaperonins.

17 II chaperonins as compared with the group I chaperonins.

18 arkable structural conservation of bacterial chaperonins.

19 particles, ferritin, heat-shock proteins and chaperonins.

20 for the overexpression of other recombinant chaperonins.

21 nd endocytosis of Escherichia coli, LPS, and chaperonin 60 (GroEL) as revealed by both FACS analysis

22 form whose accumulation requires a specific chaperonin 60 isoform.

23 , the formation of which requires a specific chaperonin 60-kDa isoform.

24 n with cell wall LPS but also with cytosolic chaperonin 60.

25 demonstrated that Mycobacteria tuberculosis chaperonin 60.1 inhibits leucocyte diapedesis and bronch

26 PCR targeting the 16S rRNA-encoding gene and chaperonin-60 (cpn60) showed that the plants were infect

27 ntaining TCP1 or TCP1-Ring complex (CCT/TRiC chaperonin), a complex known to function in protein fold

28 How chaperonins accelerate protein folding remains controver

29 The GroEL chaperonin accounted for >65% of the spectral counts in

30 hlight a new and unconventional role for the chaperonin activity of Hsp70 in the localization of a ke

31 Chaperonin and cochaperonin, represented by E. coli GroE

32 equiring the TCP1 Ring Complex (TriC or CCT) chaperonin and five tubulin-specific chaperones, tubulin

33 2 subunit is integral to the activity of the chaperonin and is needed for tumorigenesis.

34 circadian clock, ATP-dependent TCP/TRiC/CCT chaperonin and mitochondrial electron transport chain co

35 simulations of the complete system including chaperonin and substrate protein.

36 ed mechanism of mHTT inhibition between TRiC chaperonin and the CCT5 complex: cap and contain.

37 of proteins, for example, in the interior of chaperonins and in amyloid formation.

38 , BBS10, and BBS12) have homology to type II chaperonins and interact with CCT/TRiC proteins and BBS7

39 that a controlled modulation of the GroEL/ES chaperonins and Lon protease levels affects the intracel

40 ubunit diversification from simpler archaeal chaperonins appears linked to proteome expansion.

41 CCT has a classic chaperonin architecture, with two heterogeneous 8-member

42 cells expressing this protein as their only chaperonin are viable.

43 Among these, the chaperonins are 1-MDa ring-shaped oligomeric complexes t

44 Chaperonins are a family of chaperones that encapsulate

45 Group II chaperonins are ATP-ases indispensable for the folding o

46 Group II chaperonins are ATP-dependent ring-shaped complexes that

47 Chaperonins are cage-like complexes in which nonnative p

48 Our study shows that chaperonins are essential for the cell-to-cell trafficki

49 Group II chaperonins are essential mediators of cellular protein

50 Chaperonins are intricate allosteric machines formed of

51 Chaperonins are large protein complexes consisting of tw

52 Chaperonins are large, cylindrical complexes that provid

53 Chaperonins are molecular machines that use ATP-driven c

54 Chaperonins are nanomachines that facilitate protein fol

55 milar result is obtained by representing the chaperonin as a simple spherical cavity.

56 y distinct closing mechanism in the group II chaperonins as compared with the group I chaperonins.

57 d proved not to disturb the structure of the chaperonin, as demonstrated by size-exclusion chromatogr

58 The GroE chaperonins assist substrate protein (SP) folding by cyc

59 The implications of these findings for chaperonin-assisted folding mechanisms are discussed.

60 ctors, which functioned with the chloroplast chaperonin, AtCpn60alpha(7)beta(7).

61 DNAJ-PKAc, a chimeric enzyme consisting of a chaperonin-binding domain fused to the Calpha subunit of

62 CCT in free solution using the emission from chaperonin-bound fluorescent nucleotides and closed-loop

63 eronin-sized complexes of both WT and mutant chaperonins, but with reduced recovery of C450Y CCT4 sol

64 s and green algae is a curiosity as both the chaperonin cage and its lid are encoded by multiple gene

65 tein substrate stability inside the GroEL/ES chaperonin cage have not been reported.

66 tions, we show that protein stability in the chaperonin cage is reduced dramatically by more than 5 k

67 Recent work shows how chaperonins can rescue innovative mutants, with implicat

68 t to require the assistance of the cytosolic chaperonin CCT and a cochaperone, phosducin-like protein

69 Here we identify the chaperonin CCT as a novel physiological substrate for p9

70 The cytosolic chaperonin CCT is a 1-MDa protein-folding machine essent

71 Here we report that the eukaryotic chaperonin CCT plays a key role in mTORC assembly and si

72 een oncogene and growth factor signaling and chaperonin CCT-mediated cellular activities.

73 e p53 is promoted by an interaction with the chaperonin CCT.

74 Here, we identify the chaperonin CCT/TRiC as a critical regulator of telomeras

75 on the more poorly characterized eukaryotic chaperonin CCT/TRiC.

76 f inefficient interaction with the cytosolic chaperonin, CCT, and, in several cases, a failure to sta

77 p III CPN, Carboxydothermus hydrogenoformans chaperonin (Ch-CPN), is able to refold denatured protein

78 ulates substrate proteins within the central chaperonin chamber.

79 ene might have originally coded for an HSP70 chaperonin (class II aaRS homolog) and an NAD-specific G

80 that distinct allosteric behavior of the two chaperonin classes originates from different wiring of i

81 eric kinetics has been described for the two chaperonin classes.

82 mation occurs more generally for chloroplast chaperonin cofactors, perhaps adapting the chaperonin sy

83 domonas reinhardtii (Cr), three genes encode chaperonin cofactors, with cpn10 encoding a single appro

84 ) works as a co-chaperone with the cytosolic chaperonin complex (CCT) to fold Gbeta and mediate its i

85 ball-shaped, double-ring human mitochondrial chaperonin complex at 3.15 A, which is a novel intermedi

86 RiC (chaperonin containing TCP-1/TCP-1 ring) chaperonin complex can inhibit aggregation and cellular

87 The cytosolic chaperonin complex chaperonin containing t-complex prote

88 , which encodes a subunit of the chloroplast chaperonin complex CPN60.

89 fied, including the well-studied GroEL-GroES chaperonin complex found in Escherichia coli.

90 subunit of the CCT/TCP-1 ring complex (TRiC) chaperonin complex is involved in regulating aggregation

91 assembly intermediates, we show that the BBS-chaperonin complex plays a role in BBS7 stability.

92 inactivation of components of the cytosolic chaperonin complex that induce increased longevity also

93 ces cerevisiae, we found that mutants of the chaperonin complex TRiC and the functionally related pre

94 Polypeptides are known to fold inside the chaperonin complex, but the conformation of an encapsula

95 re we show that KN1 trafficking requires the chaperonin complex, which belongs to a group of cytosoli

96 also activated by downregulation of the TCP1 chaperonin complex, whose normal function is to promote

97 t1/2 approximately 1 s), and released by the chaperonin complex.

98 ns and BBS7 to form a complex termed the BBS-chaperonin complex.

99 has been published for any mammalian type I chaperonin complex.

100 release from bacterial, yeast, and mammalian chaperonin complexes but appears to be incompletely fold

101 Here we present structures of gp23-chaperonin complexes, showing both the initial captured

102 nt model may provide clues about the role of chaperonin confinement in smoothing folding landscapes b

103 ATP and GroES, both GroEL and the eukaryotic chaperonin containing t-complex polypeptide 1 (CCT/TRiC)

104 The eukaryotic chaperonin containing t-complex polypeptide 1 (CCT/TRiC)

105 The cytosolic chaperonin complex chaperonin containing t-complex protein 1 (CCT) was iden

106 ns inside the protein-folding chamber of the chaperonin containing t-complex protein 1.

107 Plasmodium folding machinery in silico, the chaperonin containing t-complex protein-1 complex, highl

108 ke protein, a co-chaperone for the cytosolic chaperonin containing tailless complex polypeptide 1 (CC

109 ed, we have identified three subunits of the Chaperonin containing TCP-1 (CCT) complex as new direct

110 Chaperonin containing TCP-1 (CCT) is a complex that assi

111 Chaperonin containing TCP-1 (CCT) is a large multisubuni

112 This system includes cytosolic chaperonin containing TCP-1 (CCT; also called TRiC) and

113 Plasmodium falciparum TCP-1 ring complex or chaperonin containing TCP-1 (TRiC/CCT), an essential het

114 We identified chaperonin containing TCP-1 subunit eta (CCT7) as an int

115 plex 1 (TCP-1) ring complex (TRiC or CCT for chaperonin containing TCP-1) have been shown to reduce m

116 rings, each formed from eight different CCT (chaperonin containing TCP-1) subunits.

117 in, TRiC/CCT (TRiC, TCP-1 ring complex; CCT, chaperonin containing TCP-1), uses a built-in lid to med

118 rolled by various chaperones, including CCT (chaperonin containing TCP-1)/TCP-1/TRiC.

119 The CCT/TRiC (chaperonin containing TCP-1/TCP-1 ring) chaperonin compl

120 Cmr1--together with Mrc1/Claspin, Pph3, the chaperonin containing TCP1 (CCT) and 25 other proteins--

121 tarvation) and two genetic mutations [in the chaperonin containing TCP1 (CCT) complex and in the prot

122 , OXR1, RPS6KA3, SNX27 and 9 subunits of the chaperonin containing TCP1 complex (CCT) were found to i

123 releases Cdc20 from MCC and identified it as chaperonin containing TCP1 or TCP1-Ring complex (CCT/TRi

124 Importantly, we identified chaperonin containing TCP1 subunit 6A (CCT6A) as an inhi

125 protein 2, fructose-bisphosphate aldolase C, chaperonin-containing T-complex polypeptide 1 subunit ze

126 Chaperonin-containing TCP-1 (CCT or TRiC) is a multi-sub

127 The eukaryotic chaperonin-containing TCP-1 (CCT) folds the cytoskeletal

128 utations were identified as LCA-causative in chaperonin-containing TCP-1, subunit 2 (CCT2), a gene th

129 n phosphatase 1 (PP1)-associated proteins, a chaperonin-containing Tcp1 complex, and other uncharacte

130 Chaperonins (CPN) are ubiquitous oligomeric protein mach

131 e histone-like protein HU form B, the 10 kDa chaperonin Cpn10, and the 50S ribosomal protein L24.

132 Here, we investigated how the chloroplast chaperonin (Cpn60) facilitated the thylakoid integration

133 med distinct bacterial and archaeal branches.Chaperonins (CPNs) are ATP-dependent protein-folding mac

134 The chaperonins (CPNs) are megadalton sized hollow complexes

135 the native state for any given round of the chaperonin cycle.

136 relatively simple model systems but also for chaperonin dependence and folding in vivo.

137 of minimally frustrated sequences can reduce chaperonin dependence and improve protein expression lev

138 n factors and demonstrates the importance of chaperonin-dependent protein trafficking for plant stem

139 isms are different from other group I and II chaperonins despite their similar architecture.

140 struction and modeling of Mm-cpn, a group II chaperonin, determined to 4.3 A resolution.

141 le unstable compared to many other bacterial chaperonins, do act as oligomers in vivo, and that there

142 g and/or sequestering the large subunit from chaperonins early in the assembly process.

143 over-representation of secondary alleles in chaperonin-encoding genes-a finding corroborated by the

144 of TRiC substrate is identified, and how the chaperonin exploits its different subunits to extend its

145 Inhibition of chaperonin expression sensitized bacteria to aminoglycos

146 facilitated survival, whereas inhibition of chaperonin expression sensitized bacteria.

147 ly, and we propose two alternatives: (a) the chaperonin facilitates unfolding of kinetically and topo

148 cialization of function of the mycobacterial chaperonins following gene duplication.

149 which is extremely conserved among group II chaperonins, forms interactions with the gamma-phosphate

150 Group II chaperonins, found in archaea and eukaryotes, contain a

151 We have obtained structures of the archaeal chaperonin from Methanococcus maripaludis in both a pept

152 The crystal structure of the archaeal chaperonin from Methanococcus maripaludis in several nuc

153 ng of a cysteine-less mutant of the group II chaperonin from methanogenic archaeon Methanococcus mari

154 nd active alphabeta-thermosome, the class II chaperonin from Thermoplasma acidophilum, by introducing

155 YbbN acts as a mild inhibitor of GroESL chaperonin function and ATPase activity, suggesting that

156 is beginning to shed light on key aspects of chaperonin function and how their unique properties unde

157 tion assays indicate a mechanistic basis for chaperonin function during the posttranslocational refol

158 supporting the iterative annealing model of chaperonin function.

159 CCT chaperonin further binds and disassembles subcomplexes o

160 ts establish for the first time that a human chaperonin gene defect can be reproduced and studied at

161 BD depended on expression of the groEL/groES chaperonin genes, which are regulated by the repressor H

162 HrcA is required for the full expression of chaperonin genes.

163 itrate to facilitate the derepression of the chaperonin genes.

164 In mediating protein folding, chaperonin GroEL and cochaperonin GroES form an enclosed

165 The chaperonin GroEL and its co-chaperonin GroES form both G

166 The prototypical chaperonin GroEL assists protein folding through an ATP-

167 The chaperonin GroEL assists the folding of nascent or stres

168 The double ring-shaped chaperonin GroEL binds a wide range of non-native polype

169 he need of Escherichia coli proteins for the chaperonin GroEL can be predicted with 86% accuracy.

170 mass spectrometry (HDX-MS) to access E. coli chaperonin GroEL conformation.

171 al machines in general, and Escherichia coli chaperonin GroEL in particular, undergo large-scale conf

172 tructure of the 800 kDa Thermus thermophilus chaperonin GroEL is preserved in aqueous solution over t

173 The mechanism whereby the prototypical chaperonin GroEL performs work on substrate proteins has

174 ATP-dependent binding of the chaperonin GroEL to its cofactor GroES forms a cavity in

175 studied the interaction of the prototypical chaperonin GroEL with the prion domain of the Het-s prot

176 force originating from ATP hydrolysis in the chaperonin GroEL, by applying forces originating from th

177 prevent them from aggregation similar to the chaperonin GroEL.

178 hich originated from Buchnera, including the chaperonin GroEL.

179 nealing mechanism of action proposed for the chaperonin GroEL.

180 s C, several times slower than the canonical chaperonin GroEL.

181 The bacterial chaperonin GroEL/GroES assists folding of a broad spectr

182 omplex kinetics of Pi and ADP release by the chaperonin GroEL/GroES is influenced by the presence of

183 cause cytosolic protein misfolding and that chaperonin GroEL/GroES overexpression counters this defe

184 We find that chaperonins GroEL/ES and protease Lon compete for bindin

185 of these proteins with the Escherichia coli chaperonin, GroEL, which normally cooperates with GroES,

186 ofilms requires multiple factors including a chaperonin (GroEL1) and a nucleoid-associated protein (L

187 likely functions as the general housekeeping chaperonin, GroEL1 is dispensable, but its structure and

188 The chaperonin GroEL and its co-chaperonin GroES form both GroEL-GroES bullet-shaped and

189 ging chemical synthesis of the 97-residue co-chaperonin GroES, which contains a highly insoluble C-te

190 n each ring, whereas archaeal and eukaryotic chaperonins (group II) undergo sequential subunit motion

191 5 (PP5, PPP5C) is known to interact with the chaperonin heat shock protein 90 (HSP90) and is involved

192 lysis, because sufficient cellular chaperone/chaperonin holdase activity is created by rapid ATP depl

193 The mitochondrial chaperonin Hsp60 is a ubiquitous molecule with multiple

194 The chaperonin Hsp60, together with its cofactor Hsp10, cata

195 ojection images of Methonococcus maripaludis chaperonin in a mix of open and closed states.

196 be the first crystal structure of a group II chaperonin in an open conformation.

197 raction data show a functional relevance for chaperonins in KNOX family-dependent stem cell maintenan

198 glycoside action and reveal that chaperones, chaperonins in particular, help bacteria cope during ear

199 al for BBSome assembly, and knockdown of CCT chaperonins in zebrafish results in BBS phenotypes.

200 cellular proteins requires the assistance of chaperonins (in Escherichia coli, GroEL and GroES), doub

201 ) structures of Mm-cpn, an archaeal group II chaperonin, in the nucleotide-free (open) and nucleotide

202 In contrast with group I chaperonins, in which the equatorial domains share a sim

203 Thus, chaperonin independence correlates with folding properti

204 ivation results in overexpression of PrsA, a chaperonin involved in posttranslational maturation of S

205 The TRiC/CCT chaperonin is a 1-MDa hetero-oligomer of 16 subunits tha

206 This cellular chaperonin is frequently up-regulated in cancers.

207 Encapsulation of proteins in chaperonins is an important mechanism by which the cell

208 ers despite the fact that oligomerization of chaperonins is regarded as essential for their function.

209 ntial proteins cannot fold without help from chaperonins, like the GroELS system of Escherichia coli.

210 c in nature and appear to revolve around the chaperonin-like activities of the ATPases in the 19 S re

211 show that a novel complex composed of three chaperonin-like BBS proteins (BBS6, BBS10, and BBS12) an

212 Chaperonin-like BBS proteins interact with a subset of B

213 richia coli to investigate whether they form chaperonin-like double ring complexes.

214 ific as protein folding can be guided by the chaperonin machine in a way largely independent of subst

215 icles are the folding functional form of the chaperonin machine in vivo.

216 ar proteins fold only with the assistance of chaperonin machines like the GroEL-GroES system of Esche

217 Chaperonins mediate protein folding in a cavity formed b

218 Group II chaperonins mediate protein folding in an ATP-dependent

219 partitioning in vivo between spontaneous and chaperonin-mediated folding.

220 Chaperonin-mediated protein folding is critically depend

221 findings strongly support an active model of chaperonin-mediated protein folding, where partial unfol

222 (BBS6, BBS10, and BBS12) and CCT/TRiC family chaperonins mediates BBSome assembly, which transports v

223 ative to the single-ring human mitochondrial chaperonin mtHsp60-mtHsp10, and will provide insights in

224 The CCT/TRiC chaperonin nanomachine undergoes ATP-driven conformation

225 gen Mycobacterium tuberculosis expresses two chaperonins, one (Cpn60.1) dispensable and one (Cpn60.2)

226 How chaperonins orchestrate the successful folding of even t

227 oglycoside exposure to exponential cultures, chaperonin overexpression protected the bacterial membra

228 ork capacity of cells by consuming chaperone/chaperonin pathway and degradation pathway capacity.

229 he (betaalpha)8 TIM-barrel fold, but how the chaperonin promotes folding of these proteins is not kno

230 The chaperonin proteins GroEL and GroES are cellular nanomac

231 ng complexes coexisting in the mHsp60-mHsp10 chaperonin reaction cycle.

232 folding from the beginning to the end of the chaperonin reaction cycle.

233 ther subunits, and these complexes carry out chaperonin reactions without other partner subunits.

234 nding of this highly conserved and essential chaperonin remains elusive.

235 01, which encodes a caseinolytic peptidase B chaperonin required for thermotolerance.

236 A major recurring problem within group II chaperonin research, especially with the hetero-oligomer

237 Thus, chaperonin rings are not obligate confining antiaggregat

238 e role of specific subunits in promoting the chaperonin's function in cancer.

239 Sucrose gradient centrifugation revealed chaperonin-sized complexes of both WT and mutant chapero

240 pologically trapped intermediates or (b) the chaperonin stabilizes interactions that promote knotting

241 is not able to fold gp23 and showing how the chaperonin structure distorts to enclose a large, physio

242 al fusion constructs with actin, an obligate chaperonin substrate, we show that TRiC can mediate fold

243 The chaperonin substrate-binding sites are exposed, and the

244 nd modeling provided a structural model of a chaperonin-substrate complex.

245 hamber of approximately 70 kDa, but numerous chaperonin substrates are substantially larger.

246 binding and hydrolysis are required for some chaperonin substrates.

247 l domains, the three domains of the archaeal chaperonin subunit reorient as a single rigid body.

248 Bacterially expressed CCT5 chaperonin subunits, which form biologically active homo

249 the mechanism of this biologically important chaperonin, such as that the conformational transitions

250 Bacterial (group I) chaperonins, such as GroEL, undergo concerted subunit mo

251 Our early studies of chaperonins support such a philosophy, as detailed in th

252 The GroE chaperonin system facilitates protein folding in an ATP-

253 t chaperonin cofactors, perhaps adapting the chaperonin system for the folding of specific client pro

254 Here, we focus on the GroEL/GroES chaperonin system from Escherichia coli and, to a lesser

255 The GroEL/ES chaperonin system functions as a protein folding cage.

256 The GroE chaperonin system in Escherichia coli comprises GroEL an

257 The GroEL/ES chaperonin system is required for the assisted folding o

258 turb protein stability without affecting the chaperonin system itself.

259 The chloroplast chaperonin system of plants and green algae is a curiosi

260 The effect of the GroEL/GroES chaperonin system on the folding pathway of an 82-kDa sl

261 Human mitochondria harbor a single type I chaperonin system that is generally thought to function

262 in cyanobacteria is mediated by the GroEL/ES chaperonin system, and assembly to holoenzyme requires s

263 studies on functional single-ring bacterial chaperonin systems are informative to the single-ring hu

264 lights key divergences between the different chaperonin systems that likely underpins this incomplete

265 systems may resemble mammalian mitochondrial chaperonin systems.

266 Subunits of the cytosolic chaperonin T-complex 1 (TCP-1) ring complex (TRiC or CCT

267 that in cells transfected with PS-ASOs, the chaperonin T-complex 1 (TCP1) proteins interact with PS-

268 The ubiquitous eukaryotic chaperonin, TCP-1 ring complex (TRiC), is a hetero-oligo

269 Moreover, the chaperonin tetradecamers show a different interring subu

270 GroEL is a group I chaperonin that facilitates protein folding and prevents

271 shock protein 60 (hsp60) is a tetradecameric chaperonin that folds proteins in the mitochondrial matr

272 form aggregates associated with cytoplasmic chaperonins that can be suppressed by ADAT2 overexpressi

273 cs to identify the TCP-1 ring complex (TRiC) chaperonin, the mitochondrial electron transport chain c

274 r and double-ring structures of the archaeal chaperonin thermosome and GroEL.

275 We have been studying chaperonins these past twenty years through an initial d

276 The capacity of the eukaryotic chaperonin to overcome the size limitation of the foldin

277 The eukaryotic chaperonin TRiC (also called CCT) is the obligate chaper

278 multiple subunits of the mammalian cytosolic chaperonin TRiC (or CCT), primarily through its DNA bind

279 by interaction with the essential eukaryotic chaperonin TRiC (or CCT).

280 cess that can be inhibited by the eukaryotic chaperonin TRiC (TCP1-ring complex) in vitro and in vivo

281 The human chaperonin TRiC consists of eight non-identical subunits

282 (mhttQ51), and resolve 3-D structures of the chaperonin TRiC interacting with mhttQ51.

283 in the subunits of the eukaryotic cytosolic chaperonin TRiC, a protein machine responsible for foldi

284 ase 2 (VRK2) is known to negatively regulate chaperonin TRiC, and VRK2-facilitated degradation of TRi

285 the resulting cross-linked peptides for the chaperonin TRiC/CCT and the 26S proteasome.

286 To understand how the essential ring-shaped chaperonin TRiC/CCT cooperates with the chaperone prefol

287 es of the mammalian double-ring multisubunit chaperonin TRiC/CCT in free solution using the emission

288 The eukaryotic group II chaperonin TRiC/CCT is a 16-subunit complex with eight d

289 In eukaryotes, the chaperonin TRiC/CCT is hetero-oligomeric, consisting of

290 nce through high levels of the ATP-dependent chaperonin TRiC/CCT.

291 The eukaryotic chaperonin, TRiC/CCT (TRiC, TCP-1 ring complex; CCT, cha

292 the ring-shaped hetero-oligomeric eukaryotic chaperonin, TRiC/CCT, which contributes to its biosynthe

293 Our findings suggest that the mitochondrial chaperonins use a mechanism that is distinct from the me

294 of large macromolecular assemblies (such as chaperonins, viruses, etc.) that remain conformationally

295 Interestingly, the mitochondrial chaperonin was captured in a state that exhibits subunit

296 otein A, 30S ribosomal protein s1 and 60 kDa chaperonin) were identified.

297 an adenosine-5'-triphosphate-driven group II chaperonin, which resembles a barrel with a built-in lid

298 We conclude that the essential mycobacterial chaperonins, while unstable compared to many other bacte

299 Thus, the combined action of CCT chaperonin with that of TRIP13 ATPase promotes the compl

300 h CCT assists folding is distinct from other chaperonins, with no hydrophobic wall lining a potential