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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 pling and the import of presequence-carrying preproteins.
12 -binding pocket of Tom71 is ready to receive preproteins.
13 the outer membrane complex for mitochondrial preproteins.
14 f both photosynthetic and non-photosynthetic preproteins.
15 e unstructured states of targeting-competent preproteins.
16 resentative constitutively expressed plastid preproteins.
17  N-terminal signal peptide from translocated preproteins.
18 e general import pathway utilized by stromal preproteins.
19 Tim44 to generate a pulling force and unfold preproteins.
20  region of Toc159G are in close proximity to preproteins.
21 face showed increased cross-linking to bound preproteins.
22 (TIM23 complex) mediates the import of these preproteins.
23 nal modifications from ribosomally generated preproteins.
24 molecular motor driving translocation of the preprotein across the membrane by repeated ATP-driven cy
25 ution, mechanisms had to evolve to transport preproteins across all four membranes.
26 iogenesis requires translocation of numerous preproteins across both outer and inner membranes into t
27 In addition to its roles in translocation of preproteins across membranes, Ydj1 facilitates the matur
28 dependent mechanism for translocating folded preproteins across or into the inner membrane of Escheri
29 ase associates with the SecY complex to push preproteins across the bacterial membrane.
30 locon to allow simultaneous translocation of preproteins across the envelope.
31                             Translocation of preproteins across the Escherichia coli inner membrane r
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 ficiency of SecA2-dependent transport of the preprotein and a simultaneous increase in SecA2-independ
36        Characterization of two mitochondrial preprotein and amino acid transport proteins from Arabid
37                      A family of 17 putative preprotein and amino acid transporters designated PRAT h
38 sert into the membrane upon interaction with preprotein and ATP.
39                                    The LAP-A preprotein and mature polypeptide were overexpressed in
40 endent motor protein that interacts with the preprotein and translocon to drive protein translocation
41 m, which recognizes the signal sequence of a preprotein and uses ATP and the proton motive force to m
42 wever, they exhibited a reduced affinity for preprotein and were defective in preprotein release, as
43 crucial mtHsp70 functions, such as import of preproteins and biogenesis of Fe-S clusters.
44 ates the ATPase activity of Ssa1p to release preproteins and engineer translocation, support for this
45 ed in the cytosol as higher molecular weight preproteins and imported via the translocons in the oute
46                  Tim23p acts as receptor for preproteins and may largely constitute the preprotein-co
47         The POTRA domains also interact with preproteins and mediate the recruitment of molecular cha
48 al translocon interacts with both SecA-bound preproteins and nascent chain-ribosome complexes during
49 ntial ATP-driven motor protein that binds to preproteins and the translocon to promote protein transl
50 proteins are synthesized in the cytoplasm as preproteins and then imported into the organelles via sp
51 n with the plasma membrane containing SecYE, preprotein, and ATP, SecA undergoes cycles of membrane i
52 r binding nucleotide, mature portions of the preprotein, and the SecYEG channel.
53 olding defect caused by enhanced trapping of preproteins, and a conditionally lethal unfolding defect
54 plexes as preproteins at an early stage when preproteins are being processed to the mature size.
55                                              Preproteins are directed to the Tat pathway by signal pe
56                                          The preproteins are escorted to Tom70/Tom71 by molecular cha
57                                          The preproteins are imported by the translocase of the outer
58  the TIM23 complex during lateral sorting of preproteins are poorly understood.
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 are implicated in two key import activities, preprotein binding and driving membrane translocation, b
74 formational response element to regulate the preprotein binding and release cycle of SecA.
75  each containing GTPase domains that control preprotein binding and translocation.
76                          Candidate sites for preprotein binding are located on a surface containing t
77 these mutations did not decrease the initial preprotein binding at the receptors, but they reduced th
78 cleotide binding domain (NBD), Phe263 in the preprotein binding domain (PBD), and Tyr794 and Arg805 i
79 of the outer envelope) recognition in vitro, preprotein binding in organellar, precursor binding in v
80 stabilizing the formation of a GTP-dependent preprotein binding intermediate.
81 eproteins during import, a role for Toc34 in preprotein binding previously had not been observed.
82   Furthermore, atToc120 and atToc132 exhibit preprotein binding properties that are distinct from atT
83 es 267-340 has been proposed to comprise the preprotein binding site of Escherichia coli SecA.
84 educed the efficiency of the transition from preprotein binding to membrane translocation.
85 159 receptors regulate their selectivity for preprotein binding.
86  two nucleotide-binding domains that flank a preprotein-binding domain (PPXD), while the C-domain bin
87 ngement within Tom71, which may position the preprotein-binding pocket closer to Hsp70/Hsp90 to facil
88 e, the N-terminal domain moves away, and the preprotein-binding pocket is fully exposed.
89 could lock Tom71 in the open state where the preprotein-binding pocket of Tom71 is ready to receive p
90  changes that may increase the volume of the preprotein-binding pocket.
91 l domain of Tom70/Tom71 partially blocks the preprotein-binding pocket.
92 59 mediates preprotein import, we mapped the preprotein-binding regions on the Toc159 GTPase domain (
93  new fold and hydrophobic grooves resembling preprotein-binding sites of the SecB chaperone.
94 lly required for efficient import of various preproteins, both native and urea-denatured.
95    In contrast, depletion of Tim44p disrupts preprotein but not peptide translocation, which has no e
96 uired for translocation or processing of the preproteins but, like CcsA, they are required for the he
97 SecY copy is sufficient to bind SecA and the preprotein, but only the SecY dimer together with acidic
98 tides of these representative photosynthetic preproteins, but not representative constitutively expre
99 s the import of thousands of nuclear-encoded preproteins by essential import receptor TOC159.
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 n import by association with chaperone-bound preprotein complexes.
104  TIM23 complex and for dynamic gating of its preprotein-conducting channel.
105 r preproteins and may largely constitute the preprotein-conducting passageway.
106  pea (Pisum sativum) using cleavage by bound preproteins conjugated with the artificial protease FeBA
107                                              Preproteins contain a signal sequence with a positively
108 Pase, which powers translocation of unfolded preproteins containing Sec signal sequences through the
109 logy to two GenBank accessions that code for preproteins containing three isoinhibitors domains each
110          Here, we demonstrate that the Hep27 preprotein contains an N-terminal mitochondrial targetin
111 tin intolerance antibody-based inhibitors of preprotein convertase subtilisin/kexin 9 (PCSK9) produce
112 synthase having 84 residues deleted from the preprotein converted geranylgeranyl diphosphate and the
113 e nucleotide binding domain 2 (nbd2) and the preprotein cross-linking (ppx) domain.
114 aintained upon peptide binding; however, the preprotein cross-linking domain (PPXD) and helical wing
115 hat residues on the third alpha-helix in the preprotein cross-linking domain (PPXD) are important for
116 -binding domain encompasses a portion of the preprotein cross-linking domain but also includes region
117 pocket between NBD1 and NBD2 is open and the preprotein cross-linking domain has rotated away from bo
118  of the amino-terminal signal sequences from preproteins destined for cell export.
119 role in binding the signal peptide region of preproteins, directing preproteins to membrane-bound Sec
120  The first class of mutants was defective in preprotein docking onto a receptor site of the transloco
121 ger that has been shown to interact with the preprotein during translocation and lies at the entrance
122  Toc75 and Toc86 are known to associate with preproteins during import, a role for Toc34 in preprotei
123 with import intermediates of nuclear-encoded preproteins during posttranslational import into isolate
124 gnition and translocation of nuclear-encoded preproteins during the early stages of protein import in
125 ersibly inhibited the import of a variety of preproteins during translocation across the inner envelo
126  Arabidopsis (Arabid opsis thaliana) plastid preproteins encoded by recently duplicated genes and sho
127                              Using a plastid preprotein expressed in both leaves and roots of stable
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 y of the TIM23 complex assembly required for preprotein import and coupling of respiratory pathways.
138 9 in vitro, and in mutant koc1 chloroplasts, preprotein import efficiency was diminished.
139                                              Preprotein import intermediates quantitatively associate
140  covalent cross-linking studies with trapped preprotein import intermediates.
141 e that direct TIM23-AAC coupling may support preprotein import into mitochondria when respiratory act
142 sit-peptide motifs that specifically enhance preprotein import into root leucoplasts.
143  exhibited a strong inhibitory effect on the preprotein import reactions essential for mitochondrial
144 at phosphorylates import receptors, supports preprotein import, and contributes to efficient chloropl
145                Our data suggest that, during preprotein import, the Toc159G dimer disengages and the
146          To investigate the role of Tic20 in preprotein import, we altered the expression of the Arab
147 lecular understanding of how Toc159 mediates preprotein import, we mapped the preprotein-binding regi
148 regation assay, which we propose facilitates preprotein import.
149 in Toc159 play a direct role in facilitating preprotein import.
150 with the inner envelope TIC complex to power preprotein import.
151 t, suggesting that cardiolipin can influence preprotein import.
152 in quality control mechanism for chloroplast preprotein import.
153 therefore used a purified and urea-denatured preprotein in our import assays to bypass the requiremen
154 de as a simple motif for docking of the McjA preprotein in the maturation enzymes.
155 s of Sicily leads to loss of CI proteins and preproteins in both mitochondria and cytoplasm, respecti
156 sis for the enhanced transport efficiency of preproteins in the presence of SecB in vivo.
157 on, but none has been shown to directly bind preproteins in vivo during import, so it remains unclear
158 t of several highly expressed photosynthetic preproteins in vivo.
159 btained which encoded a putative 353-residue preprotein including an 18-residue signal peptide, which
160 ompeted by an excess of an authentic stromal preprotein, indicating that targeting to the intermembra
161 ne penetration and release with concommitant preprotein insertion.
162 gnificant insight on the mechanisms by which preproteins interact with Hsp90 and are translocated via
163 dent binding at the outer envelope membrane, preproteins interact with three known components of the
164 cA addressing a key issue regarding the SecA-preprotein interaction.
165        We show that in the cytoplasm, Sicily preprotein interacts with cytosolic Hsp90 to chaperone t
166                     Translocation of the p35 preprotein into the ER was not accompanied by cleavage o
167 of Mgr2 are essential for lateral sorting of preprotein into the inner membrane, as well as maintaini
168 hat the efficient import of a urea-denatured preprotein into the matrix requires GTP hydrolysis.
169  unfolding and complete translocation of the preprotein into the matrix.
170  A signal peptide is required for entry of a preprotein into the secretory pathway, but how it functi
171 blocks the hsc70-mediated translocation of a preprotein into yeast endoplasmic reticulum-derived micr
172  mitochondrial membrane (TIM23) translocates preproteins into and across the membrane and associates
173 post-translational import of nucleus-encoded preproteins into chloroplasts occurs through multimeric
174 ents in the translocation of nucleus-encoded preproteins into chloroplasts.
175 he recognition and import of nuclear-encoded preproteins into chloroplasts.
176         The TIM23 complex mediates import of preproteins into mitochondria, but little is known of th
177                The import of nucleus-encoded preproteins into plastids requires the coordinated activ
178  receptors for the import of nucleus-encoded preproteins into plastids.
179             Translocation of nuclear encoded preproteins into the mitochondrial matrix requires the c
180                                We classified preproteins into three groups: 1) those that comprise </
181                                 The purified preprotein is also kinetically impaired relative to the
182                  The means by which the GspB preprotein is selectively recognized by the accessory Se
183                The interaction of Toc34 with preproteins is regulated by the binding, but not hydroly
184 ave been discussed: (1) physical trapping of preproteins is sufficient to explain the various mtHsp70
185 start codons, potentially producing two PilA preprotein isoforms.
186    The deduced amino acid sequences revealed preprotein lengths of 367 residues, with an amino acid i
187 ochondrial outer membrane receptor Tom71 for preprotein loading.
188  Tic proteins in translocation, sorting, and preprotein maturation have not been defined.
189 monstrate that MPP has an additional role in preprotein maturation, beyond the removal of presequence
190 es, McjB and McjC, from a 58 amino acid (aa) preprotein, McjA, into its final 21 aa lasso topology.
191                                     Both the preprotein MTSs and their receptor site on SecA are esse
192                         We now report that a preprotein must remain at least partially unfolded prior
193 , suggesting that binding of the Asps to the preprotein occurs prior to its full glycosylation.
194 A is composed of 3,291 bases and codes for a preprotein of 1,097 amino acids with an estimated molecu
195                        This cDNA codes for a preprotein of 166 amino acids, including a predicted sig
196 ne (lk75.3) encoding a sphingomyelinase-like preprotein of 648 amino acids with cytotoxic activity fo
197  influence of the early mature region of the preprotein on SecA interactions, and the extent to which
198                                              Preprotein or signal peptide binding to the purified and
199                       Prior unfolding of the preprotein, or extension of the region between the targe
200 ted genes and show that, within a duplicated preprotein pair, the isoform bearing the leucoplast moti
201 nt to which the signal peptide region of the preprotein plays a role in SecYEG interactions is unclea
202 ctional studies show an interaction with the preprotein, preSSU, which is mediated through POTRA2-3.
203 triphosphates, the transmembrane movement of preproteins proceeds only to a point early in their tran
204 nal peptidase I activity in Escherichia coli preprotein processing in vivo by complementation assay.
205 ns unclear although it appears uninvolved in preprotein processing or Tic subunit protein turnover.
206 tional initiation site utilization and LAP-N preprotein processing.
207 ranslocase with an in vitro reaction and the preprotein proOmpA carrying a synthetic stop-transfer se
208 n the cytoplasm and chloroplast as a soluble preprotein receptor.
209  chaperone system and mitochondrial membrane preprotein receptors, thereby facilitating processing of
210 wo Toc GTPases, Toc159 and Toc33/34, mediate preprotein recognition and regulate preprotein transloca
211 or understanding the molecular basis of SecA preprotein recognition as well as elucidating the chemo-
212 actions with TOC receptors, thereby coupling preprotein recognition at the chloroplast surface with m
213 r acts as part of a GTP-regulated switch for preprotein recognition at the TOC translocon.
214                                              Preprotein recognition is mediated by the TOC GTPase rec
215 the cytosol and the chloroplast envelope for preprotein recognition.
216 s into the function of GTP as a regulator of preprotein recognition.
217 ffinity for preprotein and were defective in preprotein release, as assessed by several biochemical a
218 mport receptor for the targeting of a set of preproteins required for chloroplast biogenesis.
219 ious mtHsp70 functions, and (2) unfolding of preproteins requires an active motor function of mtHsp70
220  alanine substitution at position 152 in the preprotein showed a marked increase in bioluminescence a
221  maintains quality control of inner membrane preproteins sorting.
222 by way of its transmembrane segment) and the preprotein substrate (by the h-region in the signal sequ
223 onditions deployed, the transport of a model preprotein substrate (proSpy) occurs at 200 amino acids
224                    Once bound to SecYEG, the preprotein substrate, and ATP, SecA undergoes ATP-hydrol
225 ecA-SecYEG interactions as a function of the preprotein substrate, features that have not yet been re
226 nd the P1 and P3 specificity residues of the preprotein substrate.
227                                          The preproteins targeted to the mitochondria are transported
228 own previously unsuspected distinct roles in preprotein targeting and secretion.
229                      The cytosolic events in preprotein targeting remain largely unknown, although cy
230 functions as a selective import receptor for preproteins that are required for chloroplast developmen
231 d import of several thousand nucleus-encoded preproteins that are required for organelle biogenesis a
232 ucts is derived from ribosomally synthesized preproteins that undergo a cascade of posttranslational
233 ristics of two amino-terminal domains in the preprotein (the signal peptide and the early mature regi
234 ors for selective recognition of chloroplast preproteins, the mechanism for its targeting to the chlo
235 ve diversified to recognize distinct sets of preproteins, thereby maximizing the efficiency of target
236 ons as a primary receptor and directly binds preproteins through its dimeric GTPase domain.
237                     Tim50 and Tim23 transfer preproteins through the intermembrane space to the inner
238 lel dimer structure suggests that binding of preprotein to SecA induces an activated open conformatio
239 to SecYEG and are thus positioned to deliver preprotein to SecYEG.
240 ting in the translocation of segments of the preprotein to the trans side of the membrane.
241 a specific peptide bond of membrane-imbedded preproteins to liberate mature proteins for secretion.
242 nal peptide region of preproteins, directing preproteins to membrane-bound SecYEG and promoting trans
243 ntrast, SecB is utilized by only a subset of preproteins to prevent their premature folding and chape
244 70 of the Ssa family in the translocation of preproteins to the ER and mitochondria and in the matura
245 ponent of the mechanism to control access of preproteins to the membrane translocation channel of the
246  that this interaction is necessary for GspB preprotein trafficking to lipid membranes.
247 cket closer to Hsp70/Hsp90 to facilitate the preprotein transfer from the molecular chaperone to Tom7
248                                              Preprotein translocase catalyzes membrane protein integr
249 r membrane potential or the structure of the preprotein translocase complexes.
250 hese studies suggest that the active form of preprotein translocase is monomeric SecYEG.
251     SecA is the ATPase for the Sec-dependent preprotein translocase of many bacteria.
252                                          The preprotein translocase of the outer mitochondrial membra
253 nature of signal sequence recognition by the preprotein translocase SecA, we have characterized the i
254 teral release activities of Escherichia coli preprotein translocase with an in vitro reaction and the
255 SDH Fp] subunit, aldose reductase, and TIM17 preprotein translocase); (4) genes responsible for prote
256 e peripheral subunit of the Escherichia coli preprotein translocase, interacts with a number of ligan
257 ights into the structure and function of the preprotein translocase.
258 ther with SecA forms the minimal core of the preprotein translocase.
259 abolite carriers, but their association with preprotein translocases has been controversial.
260 ochondrial beta-barrel proteins requires two preprotein translocases, the general translocase of the
261 it remains unclear whether any function as a preprotein-translocating motor and whether they have dif
262                                  Remarkably, preprotein translocation across the outer membrane can o
263 es 864-901), both of which are essential for preprotein translocation activity.
264 sertion and deinsertion through SecYEG drive preprotein translocation at the Escherichia coli inner m
265 is for the cooperation of Tim50 and Tim23 in preprotein translocation to the protein-conducting chann
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 prevent misfolding or aggregation as the preprotein traverses the intermembrane space.
276 tly binds to the transit peptides of various preproteins undergoing active import into chloroplasts.
277 itro are not the only arbiter of whether the preprotein utilizes the Sec pathway in vivo.
278 w that disrupting the N-terminal cleavage of preprotein VI has major deleterious effects on the assem
279 Density within hexon cavities is assigned to preprotein VI, and membrane disruption assays show that
280                   Recombinant protein VI and preprotein VI, but not a deletion mutant lacking an N-te
281 ntral role in the targeting and transport of preproteins via the SecYEG channel.
282 linker was placed within the AST domain, the preprotein was found to cross-link to SecA2.
283                                 Although the preprotein was glycosylated upon entry into the ER, its
284 constructs, we confirmed that wild-type StAR preprotein was imported and processed by mitochondria, w
285 port assays demonstrated that wild-type StAR preprotein was imported and processed to mature protein
286                        The mature portion of preproteins was observed preferentially at the dimer int
287  broadly impeded SecB-dependent secretion of preproteins, we show that suppression was a direct and s
288 erae peptidase processes either EpsI or MshA preproteins when co-expressed in E. coli.
289 yristoylation occurs within a portion of the preprotein, which is subsequently removed by N-terminal
290 d the dimer interface contacts translocating preproteins, which is consistent with a model in which c
291 ic22 is nuclear-endoded and synthesized as a preprotein with a 50-amino acid N-terminal presequence.
292 1 is synthesized on cytosolic ribosomes as a preprotein with a cleavable N-terminal presequence that
293                       It is synthesized as a preprotein with a deduced M(r) of 52,000 containing a 31
294 ould be reconstituted by incubating the FRDA preprotein with rat or yeast matrix processing peptidase
295 ia coli is initiated by the interaction of a preprotein with the membrane translocase composed of a m
296 genome, synthesized as higher molecular mass preproteins with an N-terminal transit peptide, and then
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

 
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