ライフサイエンスコーパス: chaperonin

1 the method to the Methonococcus maripaludis chaperonin.

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

3 e as much Rubisco protein recovered with the chaperonin.

4 th the structural properties of an effective chaperonin.

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

6 suggest active mechanisms for the molecular chaperonin.

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

8 ransfer to downstream chaperones such as the chaperonins.

9 mal and stress-related metabolic function of chaperonins.

10 an optimized synthetic gene and cold-adapted chaperonins.

11 rate during the nucleotide cycle of group II chaperonins.

12 l studies, is unique to eukaryotic cytosolic chaperonins.

13 driving the conformational cycle of group II chaperonins.

14 units and promote their association with CCT chaperonins.

15 II chaperonins as compared with the group I chaperonins.

16 arkable structural conservation of bacterial chaperonins.

17 TPases, GHL proteins, actin-fold enzymes and chaperonins.

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

19 for the overexpression of other recombinant chaperonins.

20 ith the large subunit as it is released from 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 PCR targeting the 16S rRNA-encoding gene and chaperonin-60 (cpn60) showed that the plants were infect

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

27 How chaperonins accelerate protein folding remains controver

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

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

30 Chaperonin and cochaperonin, represented by E. coli GroE

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

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

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

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

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

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

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

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

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

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

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

42 Chaperonins are a family of chaperones that encapsulate

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

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

45 Chaperonins are cage-like complexes in which nonnative p

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

47 Group II chaperonins are essential mediators of cellular protein

48 Chaperonins are intricate allosteric machines formed of

49 Chaperonins are large protein complexes consisting of tw

50 Chaperonins are large, cylindrical complexes that provid

51 Chaperonins are molecular machines that use ATP-driven c

52 Chaperonins are nanomachines that facilitate protein fol

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

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

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

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

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

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

59 ubstrates fold upon sequestration inside the chaperonin barrel, the precise mechanism by which confin

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

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

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

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

64 ng intermediates downstream of the cytosolic chaperonin CCT (1, 2).

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

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

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

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

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

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

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

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

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

74 overall rate of renaturation relative to the chaperonin chamber, where such associations cannot occur

75 ulates substrate proteins within the central chaperonin chamber.

76 s not block the formation of a functional co-chaperonin/chaperonin complex but limits self-aggregatio

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

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

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

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

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

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

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

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

85 The cytosolic chaperonin complex chaperonin containing t-complex prote

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

107 The eukaryotic cytosolic chaperonin containing TCP-1 (CCT) has an important funct

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

123 ng chaperones, including prefoldin (PFD) and chaperonin-containing TCP-1 (CCT).

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

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

126 Chaperonins (CPN) are ubiquitous oligomeric protein mach

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

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

129 The chaperonins (CPNs) are megadalton sized hollow complexes

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

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

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

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

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

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

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

137 Chaperonins engulf other proteins and accelerate their f

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

139 Inhibition of chaperonin expression sensitized bacteria to aminoglycos

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

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

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

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

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

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

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

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

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

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

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

151 supporting the iterative annealing model of chaperonin function.

152 CCT chaperonin further binds and disassembles subcomplexes o

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

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

155 The bacterial chaperonin GroEL and the co-chaperonin GroES assist in t

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

157 The chaperonin GroEL assists the folding of nascent or stres

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

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

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

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

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

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

164 ntal assays of the activity of the bacterial chaperonin GroEL to demonstrate that a chaperonin's abil

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

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

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

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

169 TP-driven catalytic cycle of the prokaryotic chaperonin GroEL.

170 prevent them from aggregation similar to the chaperonin GroEL.

171 hich originated from Buchnera, including the chaperonin GroEL.

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

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

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

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

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

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

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

179 The bacterial chaperonin GroEL and the co-chaperonin GroES assist in the folding of a number of st

180 Then, binding of ATP and co-chaperonin GroES to that ring ejects the non-native prot

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

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

183 5 (PP5, PPP5C) is known to interact with the chaperonin heat shock protein 90 (HSP90) and is involved

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

185 The mitochondrial chaperonin Hsp60 is a ubiquitous molecule with multiple

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

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

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

189 ependent, and disrupting the function of the chaperonin in yeast leads to loss of CCT-septin interact

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

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

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

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

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

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

196 Thus, chaperonin independence correlates with folding properti

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

198 osome, cell adhesion complexes and the TCP-1 chaperonin involved in protein folding.

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

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

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

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

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

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

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

206 vestigate the effect of confinement inside a chaperonin-like cavity on the configurational free energ

207 We now show that Fab1, through its chaperonin-like domain, binds to Vac14 and Fig4 and form

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

209 In the absence of SP, the chaperonin machine idles in the resting state, but in th

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

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

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

213 Our findings suggest that one function of chaperonins may involve trapping unfolded proteins and s

214 Chaperonins mediate protein folding in a cavity formed b

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

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

217 Chaperonin-mediated protein folding is critically depend

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

219 We examine the possibility that the chaperonin mediates a favorable reorganization of the so

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

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

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

223 In a study of the timing mechanism of the chaperonin nanomachine we show that the hemicycle time (

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

225 How chaperonins orchestrate the successful folding of even t

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

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

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

229 Co-chaperonin protein 10 (cpn10, GroES in Escherichia coli)

230 The chaperonin proteins GroEL and GroES are cellular nanomac

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

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

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

234 01, which encodes a caseinolytic peptidase B chaperonin required for thermotolerance.

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

236 Thus, chaperonin rings are not obligate confining antiaggregat

237 erial chaperonin GroEL to demonstrate that a chaperonin's ability to facilitate folding is correlated

238 properties is more critical to the GroEL/ES chaperonin's function.

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

240 In the absence of chaperonins, SP folds by the kinetic partitioning mechan

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

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

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

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

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

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

247 Although it has long been known that chaperonin substrates fold upon sequestration inside the

248 binding and hydrolysis are required for some chaperonin substrates.

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

250 The abundance of a chaperonin subunit, CpkB, was much reduced in the Deltar

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

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

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

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

255 bstrate proteins can be refolded both by the chaperonin system and while free in solution.

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

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

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

259 The GroE chaperonin system in Escherichia coli comprises GroEL an

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

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

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

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

264 under "nonpermissive" conditions, where the chaperonin system was absolutely required and substrate

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

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

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

268 systems may resemble mammalian mitochondrial chaperonin systems.

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

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

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

272 Moreover, the chaperonin tetradecamers show a different interring subu

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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 proteins by the Tcp1-containing ring complex chaperonin, TriC.

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