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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
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
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
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
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
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
53 olding defect caused by enhanced trapping of preproteins, and a conditionally lethal unfolding defect
60 OTRA domains serve as a binding site for the preprotein as it emerges from the Toc75 channel and prov
62 ion of membrane translocation of chloroplast preproteins as part of the molecular mechanism of GTP-re
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
68 Proteolysis eliminates detectable binding of preproteins at the chloroplast surface, which is consist
70 main selectively associates with chloroplast preproteins at the late stages of membrane translocation
73 are implicated in two key import activities, preprotein binding and driving membrane translocation, b
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
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
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
89 could lock Tom71 in the open state where the preprotein-binding pocket of Tom71 is ready to receive p
92 59 mediates preprotein import, we mapped the preprotein-binding regions on the Toc159 GTPase domain (
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
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
106 pea (Pisum sativum) using cleavage by bound preproteins conjugated with the artificial protease FeBA
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
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
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
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
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
132 clization or mutation of Ile8 to alanine via preprotein gene replacement resulted in a 4-fold and 2-f
134 eptidase, which removes signal peptides from preproteins, has a substrate specificity for small uncha
137 y of the TIM23 complex assembly required for preprotein import and coupling of respiratory pathways.
141 e that direct TIM23-AAC coupling may support preprotein import into mitochondria when respiratory act
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
147 lecular understanding of how Toc159 mediates preprotein import, we mapped the preprotein-binding regi
153 therefore used a purified and urea-denatured preprotein in our import assays to bypass the requiremen
155 s of Sicily leads to loss of CI proteins and preproteins in both mitochondria and cytoplasm, respecti
157 on, but none has been shown to directly bind preproteins in vivo during import, so it remains unclear
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
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
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.
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
184 ave been discussed: (1) physical trapping of preproteins is sufficient to explain the various mtHsp70
186 The deduced amino acid sequences revealed preprotein lengths of 367 residues, with an amino acid i
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.
194 A is composed of 3,291 bases and codes for a preprotein of 1,097 amino acids with an estimated molecu
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
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.
207 ranslocase with an in vitro reaction and the preprotein proOmpA carrying a synthetic stop-transfer se
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
217 ffinity for preprotein and were defective in preprotein release, as assessed by several biochemical a
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
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
225 ecA-SecYEG interactions as a function of the preprotein substrate, features that have not yet been re
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
238 lel dimer structure suggests that binding of preprotein to SecA induces an activated open conformatio
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
247 cket closer to Hsp70/Hsp90 to facilitate the preprotein transfer from the molecular chaperone to Tom7
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
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
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
271 is well established that SecA is crucial for preprotein transport and thus cell viability, its oligom
276 tly binds to the transit peptides of various preproteins undergoing active import into chloroplasts.
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
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
287 broadly impeded SecB-dependent secretion of preproteins, we show that suppression was a direct and s
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
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