ライフサイエンスコーパス: preprotein

1 e GspB signal peptide for trafficking of the preprotein.

2 the N-terminal signal peptide of an exported preprotein.

3 ies in this area typically employ the entire preprotein.

4 ATP hydrolysis for physical movement of the preprotein.

5 nce and portions of the mature domain of the preprotein.

6 dentify a CPPase clone that encoded a 45-kDa preprotein.

7 l Ala-X-Ala sites are not cleaved within the preprotein.

8 MP increased 32P incorporation into the StAR preprotein.

9 Hsp93 also binds to the mature region of a preprotein.

10 es two isoforms (short and long) of the PilA preprotein.

11 -binding pocket of Tom71 is ready to receive preproteins.

12 the outer membrane complex for mitochondrial preproteins.

13 region of Toc159G are in close proximity to preproteins.

14 f both photosynthetic and non-photosynthetic preproteins.

15 face showed increased cross-linking to bound preproteins.

16 resentative constitutively expressed plastid preproteins.

17 e unstructured states of targeting-competent preproteins.

18 N-terminal signal peptide from translocated preproteins.

19 e general import pathway utilized by stromal preproteins.

20 Tim44 to generate a pulling force and unfold preproteins.

21 (TIM23 complex) mediates the import of these preproteins.

22 nal modifications from ribosomally generated preproteins.

23 pling and the import of presequence-carrying preproteins.

24 ing translocation in the presence of ATP and preprotein, a 65-kDa N-terminal domain of SecA is protec

25 molecular motor driving translocation of the preprotein across the membrane by repeated ATP-driven cy

26 ution, mechanisms had to evolve to transport preproteins across all four membranes.

27 iogenesis requires translocation of numerous preproteins across both outer and inner membranes into t

28 In addition to its roles in translocation of preproteins across membranes, Ydj1 facilitates the matur

29 dependent mechanism for translocating folded preproteins across or into the inner membrane of Escheri

30 ase associates with the SecY complex to push preproteins across the bacterial membrane.

31 locon to allow simultaneous translocation of preproteins across the envelope.

32 ly of Tic complexes and the translocation of preproteins across the inner envelope membrane.

33 coordinating the sorting of nucleus-encoded preproteins across the inner membrane and coordinating t

34 e presequence is an early event in import of preproteins across the mitochondrial inner membrane by t

35 r targets of cross-linking upon insertion of preproteins across the outer envelope membrane, supporti

36 ficiency of SecA2-dependent transport of the preprotein and a simultaneous increase in SecA2-independ

37 Characterization of two mitochondrial preprotein and amino acid transport proteins from Arabid

38 A family of 17 putative preprotein and amino acid transporters designated PRAT h

39 sert into the membrane upon interaction with preprotein and ATP.

40 The LAP-A preprotein and mature polypeptide were overexpressed in

41 endent motor protein that interacts with the preprotein and translocon to drive protein translocation

42 m, which recognizes the signal sequence of a preprotein and uses ATP and the proton motive force to m

43 wever, they exhibited a reduced affinity for preprotein and were defective in preprotein release, as

44 crucial mtHsp70 functions, such as import of preproteins and biogenesis of Fe-S clusters.

45 ates the ATPase activity of Ssa1p to release preproteins and engineer translocation, support for this

46 ed in the cytosol as higher molecular weight preproteins and imported via the translocons in the oute

47 Tim23p acts as receptor for preproteins and may largely constitute the preprotein-co

48 The POTRA domains also interact with preproteins and mediate the recruitment of molecular cha

49 al translocon interacts with both SecA-bound preproteins and nascent chain-ribosome complexes during

50 ntial ATP-driven motor protein that binds to preproteins and the translocon to promote protein transl

51 proteins are synthesized in the cytoplasm as preproteins and then imported into the organelles via sp

52 n with the plasma membrane containing SecYE, preprotein, and ATP, SecA undergoes cycles of membrane i

53 r binding nucleotide, mature portions of the preprotein, and the SecYEG channel.

54 olding defect caused by enhanced trapping of preproteins, and a conditionally lethal unfolding defect

55 plexes as preproteins at an early stage when preproteins are being processed to the mature size.

56 Preproteins are directed to the Tat pathway by signal pe

57 The preproteins are escorted to Tom70/Tom71 by molecular cha

58 The preproteins are imported by the translocase of the outer

59 The means by which the glycosylated preproteins are selectively recognized by the accessory

60 OTRA domains serve as a binding site for the preprotein as it emerges from the Toc75 channel and prov

61 eneral role in the import of nuclear-encoded preproteins as a common component of Tic complexes.

62 ion of membrane translocation of chloroplast preproteins as part of the molecular mechanism of GTP-re

63 est that the domain forms a docking site for preproteins as they emerge from the Tic translocon.

64 d that subunit COX VIa-L is synthesized as a preprotein, as are other COX subunits.

65 at Hsp93 is present in the same complexes as preproteins at an early stage when preproteins are being

66 cpHsc70 is present in the same complexes as preproteins at both the early stage and a later stage af

67 ase functions to cleave signal peptides from preproteins at the cell membrane.

68 Proteolysis eliminates detectable binding of preproteins at the chloroplast surface, which is consist

69 been shown to covalently cross-link to bound preproteins at the chloroplast surface.

70 main selectively associates with chloroplast preproteins at the late stages of membrane translocation

71 TOC mediates initial recognition of preproteins at the outer membrane and includes a core me

72 Abietadiene synthase is translated as a preprotein bearing an N-terminal plastidial targeting se

73 All three enzymes appear to be translated as preproteins bearing an amino-terminal plastid targeting

74 are implicated in two key import activities, preprotein binding and driving membrane translocation, b

75 formational response element to regulate the preprotein binding and release cycle of SecA.

76 each containing GTPase domains that control preprotein binding and translocation.

77 Candidate sites for preprotein binding are located on a surface containing t

78 these mutations did not decrease the initial preprotein binding at the receptors, but they reduced th

79 cleotide binding domain (NBD), Phe263 in the preprotein binding domain (PBD), and Tyr794 and Arg805 i

80 of the outer envelope) recognition in vitro, preprotein binding in organellar, precursor binding in v

81 stabilizing the formation of a GTP-dependent preprotein binding intermediate.

82 eproteins during import, a role for Toc34 in preprotein binding previously had not been observed.

83 Furthermore, atToc120 and atToc132 exhibit preprotein binding properties that are distinct from atT

84 es 267-340 has been proposed to comprise the preprotein binding site of Escherichia coli SecA.

85 educed the efficiency of the transition from preprotein binding to membrane translocation.

86 159 receptors regulate their selectivity for preprotein binding.

87 two nucleotide-binding domains that flank a preprotein-binding domain (PPXD), while the C-domain bin

88 l third of SecA, which includes the proposed preprotein-binding domain, is subject to modulation by A

89 ngement within Tom71, which may position the preprotein-binding pocket closer to Hsp70/Hsp90 to facil

90 e, the N-terminal domain moves away, and the preprotein-binding pocket is fully exposed.

91 could lock Tom71 in the open state where the preprotein-binding pocket of Tom71 is ready to receive p

92 changes that may increase the volume of the preprotein-binding pocket.

93 l domain of Tom70/Tom71 partially blocks the preprotein-binding pocket.

94 59 mediates preprotein import, we mapped the preprotein-binding regions on the Toc159 GTPase domain (

95 lly required for efficient import of various preproteins, both native and urea-denatured.

96 In contrast, depletion of Tim44p disrupts preprotein but not peptide translocation, which has no e

97 uired for translocation or processing of the preproteins but, like CcsA, they are required for the he

98 SecY copy is sufficient to bind SecA and the preprotein, but only the SecY dimer together with acidic

99 tides of these representative photosynthetic preproteins, but not representative constitutively expre

100 ecific recognition of the transit peptide of preproteins by the coordinate activities of two homologo

101 ny mitochondrial proteins are synthesized as preproteins carrying amino-terminal presequences in the

102 They are typically synthesized as preproteins, carrying signal peptides N-terminally fused

103 in translocation and SecA's proximity to the preprotein channel are discussed.

104 n import by association with chaperone-bound preprotein complexes.

105 TIM23 complex and for dynamic gating of its preprotein-conducting channel.

106 r preproteins and may largely constitute the preprotein-conducting passageway.

107 pea (Pisum sativum) using cleavage by bound preproteins conjugated with the artificial protease FeBA

108 Preproteins contain a signal sequence with a positively

109 Pase, which powers translocation of unfolded preproteins containing Sec signal sequences through the

110 logy to two GenBank accessions that code for preproteins containing three isoinhibitors domains each

111 Here, we demonstrate that the Hep27 preprotein contains an N-terminal mitochondrial targetin

112 tin intolerance antibody-based inhibitors of preprotein convertase subtilisin/kexin 9 (PCSK9) produce

113 synthase having 84 residues deleted from the preprotein converted geranylgeranyl diphosphate and the

114 e nucleotide binding domain 2 (nbd2) and the preprotein cross-linking (ppx) domain.

115 aintained upon peptide binding; however, the preprotein cross-linking domain (PPXD) and helical wing

116 hat residues on the third alpha-helix in the preprotein cross-linking domain (PPXD) are important for

117 -binding domain encompasses a portion of the preprotein cross-linking domain but also includes region

118 pocket between NBD1 and NBD2 is open and the preprotein cross-linking domain has rotated away from bo

119 of the amino-terminal signal sequences from preproteins destined for cell export.

120 role in binding the signal peptide region of preproteins, directing preproteins to membrane-bound Sec

121 The first class of mutants was defective in preprotein docking onto a receptor site of the transloco

122 ger that has been shown to interact with the preprotein during translocation and lies at the entrance

123 Toc75 and Toc86 are known to associate with preproteins during import, a role for Toc34 in preprotei

124 with import intermediates of nuclear-encoded preproteins during posttranslational import into isolate

125 gnition and translocation of nuclear-encoded preproteins during the early stages of protein import in

126 ersibly inhibited the import of a variety of preproteins during translocation across the inner envelo

127 (-)-4S-Limonene synthase preprotein from spearmint bears a long plastidial target

128 rrin efficiently extracted the IgA1 protease preprotein from the bacterial outer membrane.

129 t result in the transport of nuclear-encoded preproteins from the cytoplasm into the stroma of chloro

130 ntact sites that mediate direct transport of preproteins from the cytoplasm to the stromal compartmen

131 asts initiates the import of nuclear-encoded preproteins from the cytosol into the organelle.

132 clization or mutation of Ile8 to alanine via preprotein gene replacement resulted in a 4-fold and 2-f

133 The Arabidopsis acetyl-CoA synthetase preprotein has a calculated mass of 76,678 D, an apparen

134 eptidase, which removes signal peptides from preproteins, has a substrate specificity for small uncha

135 be anchored to the core by interactions with preprotein IIIa.

136 apsid, a connection which may be mediated by preproteins IIIa and VI.

137 9 in vitro, and in mutant koc1 chloroplasts, preprotein import efficiency was diminished.

138 Preprotein import intermediates quantitatively associate

139 covalent cross-linking studies with trapped preprotein import intermediates.

140 e that direct TIM23-AAC coupling may support preprotein import into mitochondria when respiratory act

141 exhibited a strong inhibitory effect on the preprotein import reactions essential for mitochondrial

142 at phosphorylates import receptors, supports preprotein import, and contributes to efficient chloropl

143 Our data suggest that, during preprotein import, the Toc159G dimer disengages and the

144 To investigate the role of Tic20 in preprotein import, we altered the expression of the Arab

145 lecular understanding of how Toc159 mediates preprotein import, we mapped the preprotein-binding regi

146 regation assay, which we propose facilitates preprotein import.

147 in Toc159 play a direct role in facilitating preprotein import.

148 with the inner envelope TIC complex to power preprotein import.

149 t, suggesting that cardiolipin can influence preprotein import.

150 in quality control mechanism for chloroplast preprotein import.

151 Difficulty expressing the full-length preprotein in Escherichia coli is encountered because of

152 therefore used a purified and urea-denatured preprotein in our import assays to bypass the requiremen

153 de as a simple motif for docking of the McjA preprotein in the maturation enzymes.

154 s of Sicily leads to loss of CI proteins and preproteins in both mitochondria and cytoplasm, respecti

155 sis for the enhanced transport efficiency of preproteins in the presence of SecB in vivo.

156 on, but none has been shown to directly bind preproteins in vivo during import, so it remains unclear

157 t of several highly expressed photosynthetic preproteins in vivo.

158 btained which encoded a putative 353-residue preprotein including an 18-residue signal peptide, which

159 ompeted by an excess of an authentic stromal preprotein, indicating that targeting to the intermembra

160 ne penetration and release with concommitant preprotein insertion.

161 gnificant insight on the mechanisms by which preproteins interact with Hsp90 and are translocated via

162 dent binding at the outer envelope membrane, preproteins interact with three known components of the

163 cA addressing a key issue regarding the SecA-preprotein interaction.

164 We show that in the cytoplasm, Sicily preprotein interacts with cytosolic Hsp90 to chaperone t

165 Translocation of the p35 preprotein into the ER was not accompanied by cleavage o

166 hat the efficient import of a urea-denatured preprotein into the matrix requires GTP hydrolysis.

167 unfolding and complete translocation of the preprotein into the matrix.

168 A signal peptide is required for entry of a preprotein into the secretory pathway, but how it functi

169 blocks the hsc70-mediated translocation of a preprotein into yeast endoplasmic reticulum-derived micr

170 mitochondrial membrane (TIM23) translocates preproteins into and across the membrane and associates

171 post-translational import of nucleus-encoded preproteins into chloroplasts occurs through multimeric

172 ents in the translocation of nucleus-encoded preproteins into chloroplasts.

173 he recognition and import of nuclear-encoded preproteins into chloroplasts.

174 The TIM23 complex mediates import of preproteins into mitochondria, but little is known of th

175 The import of nucleus-encoded preproteins into plastids requires the coordinated activ

176 receptors for the import of nucleus-encoded preproteins into plastids.

177 Translocation of nuclear encoded preproteins into the mitochondrial matrix requires the c

178 We classified preproteins into three groups: 1) those that comprise </

179 The purified preprotein is also kinetically impaired relative to the

180 The means by which the GspB preprotein is selectively recognized by the accessory Se

181 The interaction of Toc34 with preproteins is regulated by the binding, but not hydroly

182 ave been discussed: (1) physical trapping of preproteins is sufficient to explain the various mtHsp70

183 start codons, potentially producing two PilA preprotein isoforms.

184 The deduced amino acid sequences revealed preprotein lengths of 367 residues, with an amino acid i

185 ochondrial outer membrane receptor Tom71 for preprotein loading.

186 Tic proteins in translocation, sorting, and preprotein maturation have not been defined.

187 es, McjB and McjC, from a 58 amino acid (aa) preprotein, McjA, into its final 21 aa lasso topology.

188 damental to the study of the role of SecA in preprotein movement.

189 Both the preprotein MTSs and their receptor site on SecA are esse

190 We now report that a preprotein must remain at least partially unfolded prior

191 , suggesting that binding of the Asps to the preprotein occurs prior to its full glycosylation.

192 A is composed of 3,291 bases and codes for a preprotein of 1,097 amino acids with an estimated molecu

193 This cDNA codes for a preprotein of 166 amino acids, including a predicted sig

194 ne (lk75.3) encoding a sphingomyelinase-like preprotein of 648 amino acids with cytotoxic activity fo

195 influence of the early mature region of the preprotein on SecA interactions, and the extent to which

196 Preprotein or signal peptide binding to the purified and

197 Prior unfolding of the preprotein, or extension of the region between the targe

198 nt to which the signal peptide region of the preprotein plays a role in SecYEG interactions is unclea

199 ctional studies show an interaction with the preprotein, preSSU, which is mediated through POTRA2-3.

200 triphosphates, the transmembrane movement of preproteins proceeds only to a point early in their tran

201 nal peptidase I activity in Escherichia coli preprotein processing in vivo by complementation assay.

202 ns unclear although it appears uninvolved in preprotein processing or Tic subunit protein turnover.

203 tional initiation site utilization and LAP-N preprotein processing.

204 32P incorporation from labeled ATP into StAR preprotein produced by in vitro transcription/translatio

205 ranslocase with an in vitro reaction and the preprotein proOmpA carrying a synthetic stop-transfer se

206 n the cytoplasm and chloroplast as a soluble preprotein receptor.

207 chaperone system and mitochondrial membrane preprotein receptors, thereby facilitating processing of

208 wo Toc GTPases, Toc159 and Toc33/34, mediate preprotein recognition and regulate preprotein transloca

209 or understanding the molecular basis of SecA preprotein recognition as well as elucidating the chemo-

210 actions with TOC receptors, thereby coupling preprotein recognition at the chloroplast surface with m

211 r acts as part of a GTP-regulated switch for preprotein recognition at the TOC translocon.

212 Preprotein recognition is mediated by the TOC GTPase rec

213 s into the function of GTP as a regulator of preprotein recognition.

214 anslocation at the outer membrane as well as preprotein recognition.

215 the cytosol and the chloroplast envelope for preprotein recognition.

216 ffinity for preprotein and were defective in preprotein release, as assessed by several biochemical a

217 mport receptor for the targeting of a set of preproteins required for chloroplast biogenesis.

218 ious mtHsp70 functions, and (2) unfolding of preproteins requires an active motor function of mtHsp70

219 istent with the necessity for formation of a preprotein-SecB-SecA complex.

220 alanine substitution at position 152 in the preprotein showed a marked increase in bioluminescence a

221 by way of its transmembrane segment) and the preprotein substrate (by the h-region in the signal sequ

222 Once bound to SecYEG, the preprotein substrate, and ATP, SecA undergoes ATP-hydrol

223 nd the P1 and P3 specificity residues of the preprotein substrate.

224 The preproteins targeted to the mitochondria are transported

225 own previously unsuspected distinct roles in preprotein targeting and secretion.

226 The cytosolic events in preprotein targeting remain largely unknown, although cy

227 functions as a selective import receptor for preproteins that are required for chloroplast developmen

228 d import of several thousand nucleus-encoded preproteins that are required for organelle biogenesis a

229 ucts is derived from ribosomally synthesized preproteins that undergo a cascade of posttranslational

230 ristics of two amino-terminal domains in the preprotein (the signal peptide and the early mature regi

231 ors for selective recognition of chloroplast preproteins, the mechanism for its targeting to the chlo

232 ve diversified to recognize distinct sets of preproteins, thereby maximizing the efficiency of target

233 ons as a primary receptor and directly binds preproteins through its dimeric GTPase domain.

234 Tim50 and Tim23 transfer preproteins through the intermembrane space to the inner

235 lel dimer structure suggests that binding of preprotein to SecA induces an activated open conformatio

236 to SecYEG and are thus positioned to deliver preprotein to SecYEG.

237 ting in the translocation of segments of the preprotein to the trans side of the membrane.

238 a specific peptide bond of membrane-imbedded preproteins to liberate mature proteins for secretion.

239 nal peptide region of preproteins, directing preproteins to membrane-bound SecYEG and promoting trans

240 ntrast, SecB is utilized by only a subset of preproteins to prevent their premature folding and chape

241 70 of the Ssa family in the translocation of preproteins to the ER and mitochondria and in the matura

242 ponent of the mechanism to control access of preproteins to the membrane translocation channel of the

243 cket closer to Hsp70/Hsp90 to facilitate the preprotein transfer from the molecular chaperone to Tom7

244 Preprotein translocase catalyzes membrane protein integr

245 r membrane potential or the structure of the preprotein translocase complexes.

246 Escherichia coli preprotein translocase contains a membrane-embedded trim

247 hese studies suggest that the active form of preprotein translocase is monomeric SecYEG.

248 SecA is the ATPase for the Sec-dependent preprotein translocase of many bacteria.

249 The preprotein translocase of the outer mitochondrial membra

250 nature of signal sequence recognition by the preprotein translocase SecA, we have characterized the i

251 teral release activities of Escherichia coli preprotein translocase with an in vitro reaction and the

252 SDH Fp] subunit, aldose reductase, and TIM17 preprotein translocase); (4) genes responsible for prote

253 e peripheral subunit of the Escherichia coli preprotein translocase, interacts with a number of ligan

254 ights into the structure and function of the preprotein translocase.

255 ther with SecA forms the minimal core of the preprotein translocase.

256 h affinity at SecYEG, the integral domain of preprotein translocase.

257 abolite carriers, but their association with preprotein translocases has been controversial.

258 ochondrial beta-barrel proteins requires two preprotein translocases, the general translocase of the

259 it remains unclear whether any function as a preprotein-translocating motor and whether they have dif

260 Remarkably, preprotein translocation across the outer membrane can o

261 es 864-901), both of which are essential for preprotein translocation activity.

262 sertion and deinsertion through SecYEG drive preprotein translocation at the Escherichia coli inner m

263 We conclude that SecA functions in preprotein translocation only through cycling at SecYEG.

264 is for the cooperation of Tim50 and Tim23 in preprotein translocation to the protein-conducting chann

265 eptide chain) cycle into the membrane during preprotein translocation, as well as the distinction bet

266 Azide blocks preprotein translocation, in vivo and in vitro, through

267 vity, which interferes with both peptide and preprotein translocation.

268 mediate preprotein recognition and regulate preprotein translocation.

269 that can penetrate into the membrane during preprotein translocation.

270 al roles in mitochondrial activities besides preprotein translocation.

271 is well established that SecA is crucial for preprotein transport and thus cell viability, its oligom

272 MINOS interacts with both preprotein transport machineries of the outer membrane,

273 Whereas pea S expression, preprotein transport, and processing and assembly result

274 e activation of SecA, which is necessary for preprotein transport.

275 to covalently cross-link to nuclear-encoded preproteins trapped at an intermediate stage in import a

276 to prevent misfolding or aggregation as the preprotein traverses the intermembrane space.

277 tly binds to the transit peptides of various preproteins undergoing active import into chloroplasts.

278 itro are not the only arbiter of whether the preprotein utilizes the Sec pathway in vivo.

279 w that disrupting the N-terminal cleavage of preprotein VI has major deleterious effects on the assem

280 Density within hexon cavities is assigned to preprotein VI, and membrane disruption assays show that

281 Recombinant protein VI and preprotein VI, but not a deletion mutant lacking an N-te

282 ntral role in the targeting and transport of preproteins via the SecYEG channel.

283 linker was placed within the AST domain, the preprotein was found to cross-link to SecA2.

284 Although the preprotein was glycosylated upon entry into the ER, its

285 constructs, we confirmed that wild-type StAR preprotein was imported and processed by mitochondria, w

286 port assays demonstrated that wild-type StAR preprotein was imported and processed to mature protein

287 The mature portion of preproteins was observed preferentially at the dimer int

288 broadly impeded SecB-dependent secretion of preproteins, we show that suppression was a direct and s

289 erae peptidase processes either EpsI or MshA preproteins when co-expressed in E. coli.

290 yristoylation occurs within a portion of the preprotein, which is subsequently removed by N-terminal

291 d the dimer interface contacts translocating preproteins, which is consistent with a model in which c

292 ic22 is nuclear-endoded and synthesized as a preprotein with a 50-amino acid N-terminal presequence.

293 1 is synthesized on cytosolic ribosomes as a preprotein with a cleavable N-terminal presequence that

294 It is synthesized as a preprotein with a deduced M(r) of 52,000 containing a 31

295 ould be reconstituted by incubating the FRDA preprotein with rat or yeast matrix processing peptidase

296 ia coli is initiated by the interaction of a preprotein with the membrane translocase composed of a m

297 es of mitochondrial import pathways: whereas preproteins with bipartite targeting sequences are impor

298 ated the interactions of two nuclear-encoded preproteins with the chloroplast protein import machiner

299 ort pathway to ensure engagement of incoming preproteins with the mtHsp70p/PAM complex, a step that i

300 embrane and coordinating the interactions of preproteins with the processing and folding machineries