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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
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
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
14 t indicates that His343 is not essential for peptidyl transferase activity in yeast mitochondria.
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
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
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
33 ribosomal subunit association as well as its peptidyl-transferase activity) caused accumulation of mR
35 scribed rRNAs exhibited high activity in the peptidyl transferase assay and in a poly(U)-dependent ce
37 that of assisting the assembly of ribosomal peptidyl transferase by correctly positioning functional
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
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
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
52 tion axes for both subunits pass through the peptidyl transferase center (PTC), indicating a tendency
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
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
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
74 bosomal subunits and the conformation of the peptidyl transferase center in the context of the intact
77 s to block assembly at a late stage when the peptidyl transferase center is formed, indicating a poss
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
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
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
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
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.
109 omain V (which is known to be a component of peptidyl transferase center) and a loop of the helix 35
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
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
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
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
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
178 nd is believed to interact directly with the peptidyl-transferase centre (PTC) of the 50S ribosomal s
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
189 ledge on the fundamental mechanisms by which peptidyl transferase inhibitors modulate the catalytic a
191 lls harboring this mutation are resistant to peptidyl-transferase inhibitors (e.g., anisomycin).
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
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
205 tion inhibitor anisomycin, which affects the peptidyl transferase reaction in translation elongation,
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.
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
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
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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