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1 folding of the particles and inactivation of peptidyl transferase.
2 NA selection and binding, translocation, and peptidyl transferase.
3 s the conserved 2555 loop of 23S rRNA at the peptidyl transferase A site and suggests that peptide bo
4  directly or indirectly, helps to create the peptidyl transferase A site.
5 s of 23S rRNA likely provide elements of the peptidyl transferase active center that bind the reactan
6  of the bacterial 50S subunit, can reach the peptidyl transferase active site and contribute to its f
7 onserved 23S rRNA nucleotides located in the peptidyl transferase active site for transpeptidation an
8 venient, and sensitive method for monitoring peptidyl transferase activity (SPARK).
9 results in decreased 60S ribosome associated peptidyl transferase activity and inhibition of total pr
10 bunits with mutated A2451 showed significant peptidyl transferase activity in several independent ass
11 mal function, including the presumed site of peptidyl transferase activity in the 23S rRNA.
12                                       Though peptidyl transferase activity in the absence of protein
13 efects in E. coli and in decreased levels of peptidyl transferase activity in vitro.
14 t indicates that His343 is not essential for peptidyl transferase activity in yeast mitochondria.
15                             In addition, the peptidyl transferase activity of 70 S ribosomes containi
16  fragment and cause a modest decrease in the peptidyl transferase activity of reconstituted ribosomes
17 tion sytem has been used to characterize the peptidyl transferase activity of site-directed mutations
18 titution results in dramatic decrease of the peptidyl transferase activity of the assembled subunits.
19    However, the antibiotic failed to inhibit peptidyl transferase activity of the H. halobium ribosom
20 ile pre-steady-state kinetic analysis of the peptidyl transferase activity of the mutant ribosomes re
21 l ortholog EFP, is proposed to stimulate the peptidyl transferase activity of the ribosome and facili
22 , A2602 (Escherichia coli numbering), on the peptidyl transferase activity of the ribosome.
23                                              Peptidyl transferase activity of Thermus aquaticus ribos
24 lity of ribosome-bound tryptophan to inhibit peptidyl transferase activity rather than by reducing th
25   In neither case was the loss of binding or peptidyl transferase activity suppressed by mutations in
26 ing of the wild-type (CCA) tRNA fragment and peptidyl transferase activity using the wild-type tRNA f
27             Finally, 60S ribosome-associated peptidyl transferase activity, a key enzyme for peptide
28  a decrease in growth rate, an impairment in peptidyl transferase activity, and a sharp decline in th
29 air has significant deleterious effects upon peptidyl transferase activity, but because G*U mutation
30 ribosomal P-site, showed drastically reduced peptidyl transferase activity, whereas clindamycin resis
31 s been implicated in a direct involvement in peptidyl transferase activity.
32 rase center, where bound tryptophan inhibits peptidyl transferase activity.
33 ribosomal subunit association as well as its peptidyl-transferase activity) caused accumulation of mR
34  within 18 A from the active site, revealing peptidyl transferase as an RNA enzyme.
35 scribed rRNAs exhibited high activity in the peptidyl transferase assay and in a poly(U)-dependent ce
36                              This simplified peptidyl transferase assay follows a rapid equilibrium r
37  that of assisting the assembly of ribosomal peptidyl transferase by correctly positioning functional
38 inding, including significant changes in the peptidyl-transferase catalytic site.
39 idyl-tRNA analog to form a peptide bond in a peptidyl transferase-catalyzed reaction.
40 RNAs containing deleterious mutations in the peptidyl transferase center (25S NRD).
41 beling, and mutational analyses revealed the peptidyl transferase center (PTC) as the focal point of
42 its peptide-bond formation in the ribosome's peptidyl transferase center (PTC) during its own transla
43        The effect of AAP and Arg on ribosome peptidyl transferase center (PTC) function was analyzed
44  ribosomal exit tunnel and the A-site of the peptidyl transferase center (PTC) in halting translation
45 the CCA-end of the A-site tRNA away from the peptidyl transferase center (PTC) is functionally signif
46       Here we demonstrate that the ribosomal peptidyl transferase center (PTC) is supported by a fram
47 x RNA helicase specifically activated by the peptidyl transferase center (PTC) of 23S rRNA.
48   Peptide bond formation is catalyzed at the peptidyl transferase center (PTC) of the large ribosomal
49 protein synthesis inhibitors that target the peptidyl transferase center (PTC) on the large subunit o
50 nding of neither nucleotide (ATP or ADP) nor peptidyl transferase center (PTC) RNA, the presumed phys
51 ribosomal RNA (rRNA) helix 89 of the nascent peptidyl transferase center (PTC) through Nsa2.
52 tion axes for both subunits pass through the peptidyl transferase center (PTC), indicating a tendency
53 and catalyzing peptide bond formation at the peptidyl transferase center (PTC).
54 none molecule within its binding site in the peptidyl transferase center (PTC).
55             Thus, eIF5B interaction with the peptidyl transferase center A loop increases the accurac
56  All three are at or have been linked to the peptidyl transferase center according to the literature.
57 eptide exit tunnel at some distance from the peptidyl transferase center agrees with the proposed mod
58 contributes to the tertiary structure of the peptidyl transferase center and influences the conformat
59 he C-terminal domain of EF4 reaches into the peptidyl transferase center and interacts with the accep
60 the protein that interacts with the ribosome peptidyl transferase center and mimics the 3'-acceptor s
61                 Both antibiotics bind at the peptidyl transferase center and sterically occlude the C
62 nd the subsequent expansions that shaped the peptidyl transferase center and the conserved core.
63 n of essential functional sites, such as the peptidyl transferase center and the decoding site.
64  end in tRNA interactions with the ribosomal peptidyl transferase center and the elongation factor Tu
65 ubunit along the path it follows between the peptidyl transferase center and the exit site on the dis
66         Two hydrophobic crevices, one at the peptidyl transferase center and the other at the entranc
67  a catalytic water can be coordinated in the peptidyl transferase center and, together with previous
68 d that the ribosome dynamics detected at the peptidyl transferase center are highly inhomogeneous.
69 es of tRNA substrate located in the ribosome peptidyl transferase center around the 2-fold axis, we h
70 oRNA binding causes little distortion of the peptidyl transferase center but do provide suggestive ev
71 fined to the nascent peptide residues in the peptidyl transferase center but not to the peptide segme
72 e ribosome is catalyzed in the large subunit peptidyl transferase center by release factors on recogn
73  confirm the topographical separation of the peptidyl transferase center from the E site domain.
74 bosomal subunits and the conformation of the peptidyl transferase center in the context of the intact
75 ce of these results for the structure of the peptidyl transferase center is considered.
76 ce of these results for the structure of the peptidyl transferase center is considered.
77 s to block assembly at a late stage when the peptidyl transferase center is formed, indicating a poss
78                                The ribosomal peptidyl transferase center is responsible for two funda
79 gest that the positioning of Pro-tRNA in the peptidyl transferase center is the major determinant for
80 nity for CCdApPuro comparable to that of the peptidyl transferase center itself (Kd approximately 10
81           Three additional sites were at the peptidyl transferase center itself.
82  to interact with nucleotide residues in the peptidyl transferase center of domain V.
83 to pseudouridine (Psi) in a stem-loop at the peptidyl transferase center of Escherichia coli 23S rRNA
84 lmN and Cfr, both methylate A2503 within the peptidyl transferase center of prokaryotic ribosomes, yi
85 ance of pseudouridine formation (Psi) in the peptidyl transferase center of rRNA was examined by depl
86        These findings directly implicate the peptidyl transferase center of the 50S subunit in the me
87 on binding sites of the 30S subunit with the peptidyl transferase center of the 50S subunit via rRNA-
88 , inhibit protein synthesis by targeting the peptidyl transferase center of the bacterial ribosome.
89  has been implicated as a constituent of the peptidyl transferase center of the Escherichia coli 50 S
90                            The action of the peptidyl transferase center of the large ribosomal unit
91 ffectively an unbranched tube connecting the peptidyl transferase center of the large subunit and the
92 lation of an adenosine nucleotide within the peptidyl transferase center of the ribosome mediated by
93 ired for introducing specific changes in the peptidyl transferase center of the ribosome that activat
94     This nucleotide is positioned within the peptidyl transferase center of the ribosome, which is a
95 of domain V, which forms a major part of the peptidyl transferase center of the ribosome.
96  catalytically productive orientation in the peptidyl transferase center of the ribosome.
97 o acids are polymerized into peptides in the peptidyl transferase center of the ribosome.
98          This modification is located in the peptidyl transferase center of the ribosome.
99 ndividual point mutations, in either the 25S peptidyl transferase center or 18S decoding site, that a
100 aphic structures of antibiotics bound to the peptidyl transferase center or the exit tunnel of archae
101 es specific nucleotides within the ribosomal peptidyl transferase center that appear to be essential
102 e essential macromolecular components of the peptidyl transferase center to 23S rRNA and ribosomal pr
103 s a hydrolytic reaction in the large subunit peptidyl transferase center to release the finished poly
104  subunit surface, connecting the tRNA in the peptidyl transferase center to the distally located nasc
105  changes occur at several nucleotides in the peptidyl transferase center upon alterations in pH, temp
106 es of 8 rRNA-modifying enzymes targeting the peptidyl transferase center were individually inactivate
107 rom the back of the 50 S particle toward the peptidyl transferase center within the 50 S subunit.
108 ming the three- dimensional structure of the peptidyl transferase center within the ribosome.
109 omain V (which is known to be a component of peptidyl transferase center) and a loop of the helix 35
110 ther universally conserved nucleotide in the peptidyl transferase center, A2451.
111 itionally, a nucleotide located close to the peptidyl transferase center, A2572, which was protected
112  the A loop and P loop, respectively, of the peptidyl transferase center, and G1735A, mapping near a
113 , including the neighborhood surrounding the peptidyl transferase center, and stable association of r
114 ons of two other nucleotide positions in the peptidyl transferase center, C2471 and U2519 (C2452 and
115 S rRNA nucleotides in the 2585 region of the peptidyl transferase center, G2583A and U2584C, were obs
116 onstruct that comprises much of the 23S rRNA peptidyl transferase center, including the central loop
117 -bound tRNAs, whose 3' termini reside in the peptidyl transferase center, label primarily nucleotides
118  in 23S rRNA, which is situated close to the peptidyl transferase center, may participate in one or m
119                     Such placement, near the peptidyl transferase center, provides a rationale for th
120  discovered near the decoding center and the peptidyl transferase center, respectively.
121 mes, and their effect on conformation in the peptidyl transferase center, the GTPase-associated cente
122 erichia coli 23S rRNA, 14 are located in the peptidyl transferase center, the main antibiotic target
123 iary interactions between nucleotides in the peptidyl transferase center, the SRD, and the GTPase-ass
124 reates a free tryptophan-binding site in the peptidyl transferase center, where bound tryptophan inhi
125  as a function of the distance away from the peptidyl transferase center.
126 m to pause before allowing entrance into the peptidyl transferase center.
127 e accommodation of decoding factors into the peptidyl transferase center.
128 may generalize to other aaRS, as well as the peptidyl transferase center.
129 entified group thought to reside in the rRNA peptidyl transferase center.
130 the L27 N-terminus, which protrudes into the peptidyl transferase center.
131 to the E site but remains temporarily in the peptidyl transferase center.
132 re with another activity associated with the peptidyl transferase center.
133 n establishing the tertiary structure of the peptidyl transferase center.
134 ics on the scale of seconds at the ribosomal peptidyl transferase center.
135  is located in the immediate vicinity of the peptidyl transferase center.
136  is known to be a component of the ribosomal peptidyl transferase center.
137 oning the activated ends of tRNAs within the peptidyl transferase center.
138 ial for the successful assembly of ribosomal peptidyl transferase center.
139 via tertiary interactions to features of the peptidyl transferase center.
140 f the A-tRNA from entering the A site of the peptidyl transferase center.
141 f the acceptor end of the A-site tRNA at the peptidyl transferase center.
142  within domains IV and V, which contains the peptidyl transferase center.
143 o position helices 77 and 78 relative to the peptidyl transferase center.
144 omal tunnel to the exit port, ~100A from the peptidyl transferase center.
145 S rRNA A-loop, an essential component of the peptidyl transferase center.
146 are elongated, one residue at a time, at the peptidyl transferase center.
147 he modern ribosome this remnant includes the peptidyl transferase center.
148 esidue was separated by 14 residues from the peptidyl transferase center.
149 l RNA (rRNA) that includes hairpin 92 of the peptidyl transferase center.
150 y conserved GGQ motif packs tightly into the peptidyl transferase center.
151 ents are normally performed in the ribosomal peptidyl transferase center.
152  23S ribosomal RNA, an important part of the peptidyl transferase center.
153 somal subunit in the cleft that contains the peptidyl transferase center.
154  the RNA-mediated catalysis of the ribosomal peptidyl transferase center.
155 3S rRNA at three sites, all located near the peptidyl transferase center.
156 inhibition of TnaC-tRNA(Pro) cleavage at the peptidyl transferase center.
157  interplay between the nascent chain and the peptidyl transferase center.
158 he subunit interface, and junctions near the peptidyl transferase center.
159 f the ribosome such as the tRNA path and the peptidyl transferase center.
160         Nucleotide A2572 is in the ribosomal peptidyl transferase center.
161  binding sites of several antibiotics in the peptidyl transferase center.
162 l differences are in the conformation of the peptidyl-transferase center (PTC) and the interface betw
163 the sarcin/ricin loop (SRL) and A2531 in the peptidyl-transferase center (PTC) has adverse effects on
164 owing a disruption of the A-site side of the peptidyl-transferase center (PTC).
165 d helix 44 of 18S rRNA, domain 4 is near the peptidyl-transferase center and its helical subdomain co
166 nd peptidyl-D-aa-tRNA can trap the ribosomal peptidyl-transferase center in a conformation in which p
167  centers in the large subunit, including the peptidyl-transferase center, for unnatural polymer synth
168 tRNAs for binding in the A-site cleft in the peptidyl-transferase center, which is universally conser
169  that docks the catalytic GGQ motif into the peptidyl-transferase center.
170 s access to both the decoding center and the peptidyl-transferase center.
171                        It takes place in the peptidyl transferase centre of the large (50S) ribosomal
172 nce of the appropriate A-site substrate, the peptidyl transferase centre positions the ester link of
173 wise dominantly lethal rRNA mutations in the peptidyl transferase centre that facilitate the translat
174 tituted peptidyl-tRNA substrate and that the peptidyl transferase centre undergoes a slow inactivatio
175 5 may be a constituent part of the ribosomal peptidyl transferase centre.
176 t tunnel to relay the stalling signal to the peptidyl transferase centre.
177 f RF1 that promotes its interaction with the peptidyl transferase centre.
178 nd is believed to interact directly with the peptidyl-transferase centre (PTC) of the 50S ribosomal s
179 -containing domain of RF2 interacts with the peptidyl-transferase centre (PTC).
180 itioning the conserved C-terminus within the peptidyl-transferase centre to promote recoding.
181 the protein for interaction with rRNA in the peptidyl transferase cleft of the subunit, allowing it t
182 dApPuro, a high-affinity ligand of ribosomal peptidyl transferase designed as a transition-state anal
183 minal domain with the base of the stalk, the peptidyl transferase domain, and the head of the 30 S su
184                In this method, the ribosomal peptidyl transferase forms a peptide bond between two li
185 tivate free tryptophan binding, resulting in peptidyl transferase inhibition.
186                       Here, we show that the peptidyl transferase inhibitor sparsomycin triggers accu
187                           Chloramphenicol, a peptidyl transferase inhibitor, affected translational f
188 ational frameshifting in the presence of the peptidyl-transferase inhibitor puromycin.
189 ledge on the fundamental mechanisms by which peptidyl transferase inhibitors modulate the catalytic a
190 y increase the susceptibility of bacteria to peptidyl transferase inhibitors.
191 lls harboring this mutation are resistant to peptidyl-transferase inhibitors (e.g., anisomycin).
192                           The effects of two peptidyl-transferase inhibitors, anisomycin and sparsomy
193                                The ribosomal peptidyl transferase is a biologically essential catalys
194 both aminoacyl-transfer RNA selection and in peptidyl transferase; it may also play an important role
195 toribosomes arose from two cooperating RNAs: peptidyl transferase (large subunit) and mRNA-binder (sm
196                    Binding of CCdApPuro by a peptidyl transferase-like motif in the absence of protei
197 h similarity to conserved nucleotides of the peptidyl transferase loop domain of 23S rRNA and is cons
198 erferes with protein synthesis by inhibiting peptidyl transferase or the 80S ribosomal function.
199 ssential integral component of the ribosomal peptidyl transferase, oxazolidinones do not inhibit pept
200 er of macromolecular components required for peptidyl transferase, particles obtained by extraction o
201 ymes (196 nucleotides) that perform the same peptidyl transferase reaction as the ribosome: that is,
202 es are valuable for studies of the ribosomal peptidyl transferase reaction by complete kinetic isotop
203 due with the neutral pK(a) important for the peptidyl transferase reaction cannot be fully supported
204                       The ribosome-catalyzed peptidyl transferase reaction displays a complex pH prof
205 tion inhibitor anisomycin, which affects the peptidyl transferase reaction in translation elongation,
206 eature will simplify characterization of the peptidyl transferase reaction mechanism.
207  or the transition state intermediate of the peptidyl transferase reaction show that this reaction pr
208 , translocation, translational accuracy, the peptidyl transferase reaction, and ribosome recycling.
209 s important mechanistic implications for the peptidyl transferase reaction.
210 active-site residues reposition to allow the peptidyl transferase reaction.
211 te acts as an "oxyanion hole" to promote the peptidyl transferase reaction.
212 h is about the same as that reported for the peptidyl transferase reaction.
213 tent with a proton shuttle mechanism for the peptidyl transferase reaction.
214 me in which ribosomal RNA is responsible for peptidyl-transferase reaction catalysis.
215 he 50S subunit of the ribosome catalyzes the peptidyl-transferase reaction of protein synthesis.
216  and specificity to G2553 of 23S rRNA and is peptidyl transferase reactive in its cross-linked state,
217 ivity of A2451 in the center of the 23S rRNA peptidyl transferase region, ascribed to a perturbed pKa
218  Haloarcula marismortui (Hma) complexed with peptidyl transferase substrate analogues that reveal an
219                      Proper placement of the peptidyl transferase substrates, peptidyl-tRNA and amino
220 all peptidoglycan and are novel nonribosomal peptidyl transferases that use aminoacyl-tRNA as the ami
221  rRNA plays an important role in function of peptidyl transferase, the catalytic center of the riboso
222                       The previously studied peptidyl transferase transition state analog CC-dA-phosp
223 he G-protein superfamily, catalyzes the post-peptidyl transferase translocation of deacylated tRNA an
224 -encoded peptides are in vitro inhibitors of peptidyl transferase, which is thought to be the basis f

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