ライフサイエンスコーパス: peptidyl transferase

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 dded to the nascent chain of proteins by the peptidyl transferase activity of the ribosome and the di

23 , A2602 (Escherichia coli numbering), on the peptidyl transferase activity of the ribosome.

24 Peptidyl transferase activity of Thermus aquaticus ribos

25 lity of ribosome-bound tryptophan to inhibit peptidyl transferase activity rather than by reducing th

26 In neither case was the loss of binding or peptidyl transferase activity suppressed by mutations in

27 ing of the wild-type (CCA) tRNA fragment and peptidyl transferase activity using the wild-type tRNA f

28 Finally, 60S ribosome-associated peptidyl transferase activity, a key enzyme for peptide

29 a decrease in growth rate, an impairment in peptidyl transferase activity, and a sharp decline in th

30 air has significant deleterious effects upon peptidyl transferase activity, but because G*U mutation

31 ribosomal P-site, showed drastically reduced peptidyl transferase activity, whereas clindamycin resis

32 rase center, where bound tryptophan inhibits peptidyl transferase activity.

33 s been implicated in a direct involvement in peptidyl transferase activity.

34 ly-GR of >=20 repeats inhibit the ribosome's peptidyl-transferase activity at nanomolar concentration

35 ribosomal subunit association as well as its peptidyl-transferase activity) caused accumulation of mR

36 e tunnel, competes with poly-PR and restores peptidyl-transferase activity.

37 within 18 A from the active site, revealing peptidyl transferase as an RNA enzyme.

38 scribed rRNAs exhibited high activity in the peptidyl transferase assay and in a poly(U)-dependent ce

39 This simplified peptidyl transferase assay follows a rapid equilibrium r

40 that of assisting the assembly of ribosomal peptidyl transferase by correctly positioning functional

41 inding, including significant changes in the peptidyl-transferase catalytic site.

42 idyl-tRNA analog to form a peptide bond in a peptidyl transferase-catalyzed reaction.

43 RNAs containing deleterious mutations in the peptidyl transferase center (25S NRD).

44 ibosomes are limited by the lack of complete peptidyl transferase center (PTC) active site mutational

45 r: rotation of the 5S RNP, maturation of the peptidyl transferase center (PTC) and the nascent polype

46 e ribosomal RNA segments that constitute the peptidyl transferase center (PTC) and those that connect

47 beling, and mutational analyses revealed the peptidyl transferase center (PTC) as the focal point of

48 nucleotide rearrangements that suppress the peptidyl transferase center (PTC) catalytic activity sti

49 The ribosome's peptidyl transferase center (PTC) catalyzes peptide bond

50 its peptide-bond formation in the ribosome's peptidyl transferase center (PTC) during its own transla

51 The effect of AAP and Arg on ribosome peptidyl transferase center (PTC) function was analyzed

52 ribosomal exit tunnel and the A-site of the peptidyl transferase center (PTC) in halting translation

53 the CCA-end of the A-site tRNA away from the peptidyl transferase center (PTC) is functionally signif

54 Here we demonstrate that the ribosomal peptidyl transferase center (PTC) is supported by a fram

55 The catalytic peptidyl transferase center (PTC) is targeted by the bro

56 x RNA helicase specifically activated by the peptidyl transferase center (PTC) of 23S rRNA.

57 we visualize the formation of the conserved peptidyl transferase center (PTC) of the human mitochond

58 Peptide bond formation is catalyzed at the peptidyl transferase center (PTC) of the large ribosomal

59 es, thereby participating in structuring the peptidyl transferase center (PTC) of the large ribosomal

60 protein synthesis inhibitors that target the peptidyl transferase center (PTC) on the large subunit o

61 nding of neither nucleotide (ATP or ADP) nor peptidyl transferase center (PTC) RNA, the presumed phys

62 ribosomal RNA (rRNA) helix 89 of the nascent peptidyl transferase center (PTC) through Nsa2.

63 tion axes for both subunits pass through the peptidyl transferase center (PTC), indicating a tendency

64 cific insertion in HflX reaches far into the peptidyl transferase center (PTC), such that it would ov

65 none molecule within its binding site in the peptidyl transferase center (PTC).

66 oteins are essential for the function of the peptidyl transferase center (PTC).

67 and catalyzing peptide bond formation at the peptidyl transferase center (PTC).

68 of the large ribosomal subunit known as the peptidyl transferase center (PTC).

69 Thus, eIF5B interaction with the peptidyl transferase center A loop increases the accurac

70 All three are at or have been linked to the peptidyl transferase center according to the literature.

71 eptide exit tunnel at some distance from the peptidyl transferase center agrees with the proposed mod

72 ection between peptide bond formation at the peptidyl transferase center and chaperone-assisted de no

73 er resistance to antibiotics that target the peptidyl transferase center and exit tunnel of the ribos

74 contributes to the tertiary structure of the peptidyl transferase center and influences the conformat

75 he C-terminal domain of EF4 reaches into the peptidyl transferase center and interacts with the accep

76 alterations at every rRNA nucleotide of the peptidyl transferase center and isolating gain-of-functi

77 the protein that interacts with the ribosome peptidyl transferase center and mimics the 3'-acceptor s

78 omycin A (HygA) and macrolides, which target peptidyl transferase center and peptide exit tunnel, res

79 Both antibiotics bind at the peptidyl transferase center and sterically occlude the C

80 nterferes with eRF1's accommodation into the peptidyl transferase center and subsequent peptide relea

81 nd the subsequent expansions that shaped the peptidyl transferase center and the conserved core.

82 n of essential functional sites, such as the peptidyl transferase center and the decoding site.

83 end in tRNA interactions with the ribosomal peptidyl transferase center and the elongation factor Tu

84 ubunit along the path it follows between the peptidyl transferase center and the exit site on the dis

85 Two hydrophobic crevices, one at the peptidyl transferase center and the other at the entranc

86 a catalytic water can be coordinated in the peptidyl transferase center and, together with previous

87 Proposed catalytic mechanisms at the peptidyl transferase center are based on structures of m

88 d that the ribosome dynamics detected at the peptidyl transferase center are highly inhomogeneous.

89 The tRNAs in the peptidyl transferase center are in the A/A site and the

90 es of tRNA substrate located in the ribosome peptidyl transferase center around the 2-fold axis, we h

91 oRNA binding causes little distortion of the peptidyl transferase center but do provide suggestive ev

92 fined to the nascent peptide residues in the peptidyl transferase center but not to the peptide segme

93 e ribosome is catalyzed in the large subunit peptidyl transferase center by release factors on recogn

94 confirm the topographical separation of the peptidyl transferase center from the E site domain.

95 bosomal subunits and the conformation of the peptidyl transferase center in the context of the intact

96 Cryo-EM analysis revealed a malformed peptidyl transferase center in the misassembled 50S subu

97 Classic peptidyl transferase center inhibitor chloramphenicol (C

98 ce of these results for the structure of the peptidyl transferase center is considered.

99 s to block assembly at a late stage when the peptidyl transferase center is formed, indicating a poss

100 The ribosomal peptidyl transferase center is responsible for two funda

101 gest that the positioning of Pro-tRNA in the peptidyl transferase center is the major determinant for

102 nity for CCdApPuro comparable to that of the peptidyl transferase center itself (Kd approximately 10

103 Three additional sites were at the peptidyl transferase center itself.

104 ntly, Nog1 eviction from the pre-60S permits peptidyl transferase center maturation, and allows Yvh1

105 class I release factor (RF) protein and the peptidyl transferase center of a large subunit rRNA.

106 to interact with nucleotide residues in the peptidyl transferase center of domain V.

107 to pseudouridine (Psi) in a stem-loop at the peptidyl transferase center of Escherichia coli 23S rRNA

108 lmN and Cfr, both methylate A2503 within the peptidyl transferase center of prokaryotic ribosomes, yi

109 ance of pseudouridine formation (Psi) in the peptidyl transferase center of rRNA was examined by depl

110 These findings directly implicate the peptidyl transferase center of the 50S subunit in the me

111 on and peptidyl release are catalyzed at the peptidyl transferase center of the 50S subunit of the 70

112 on binding sites of the 30S subunit with the peptidyl transferase center of the 50S subunit via rRNA-

113 , inhibit protein synthesis by targeting the peptidyl transferase center of the bacterial ribosome.

114 has been implicated as a constituent of the peptidyl transferase center of the Escherichia coli 50 S

115 h the accommodation corridor en route to the peptidyl transferase center of the large ribosomal subun

116 (BlaS) targets translation by binding to the peptidyl transferase center of the large ribosomal subun

117 The action of the peptidyl transferase center of the large ribosomal unit

118 ffectively an unbranched tube connecting the peptidyl transferase center of the large subunit and the

119 or interaction localized in proximity to the peptidyl transferase center of the large subunit of the

120 lation of an adenosine nucleotide within the peptidyl transferase center of the ribosome mediated by

121 gyl anisomycin binds to the highly conserved peptidyl transferase center of the ribosome similar to t

122 ired for introducing specific changes in the peptidyl transferase center of the ribosome that activat

123 This nucleotide is positioned within the peptidyl transferase center of the ribosome, which is a

124 This modification is located in the peptidyl transferase center of the ribosome.

125 of domain V, which forms a major part of the peptidyl transferase center of the ribosome.

126 catalytically productive orientation in the peptidyl transferase center of the ribosome.

127 o acids are polymerized into peptides in the peptidyl transferase center of the ribosome.

128 ndividual point mutations, in either the 25S peptidyl transferase center or 18S decoding site, that a

129 aphic structures of antibiotics bound to the peptidyl transferase center or the exit tunnel of archae

130 crystallography and reveals it to occupy the peptidyl transferase center P-site of the ribosome.

131 es specific nucleotides within the ribosomal peptidyl transferase center that appear to be essential

132 , nascent polypeptide chains travel from the peptidyl transferase center through the nascent polypept

133 e essential macromolecular components of the peptidyl transferase center to 23S rRNA and ribosomal pr

134 s a hydrolytic reaction in the large subunit peptidyl transferase center to release the finished poly

135 subunit surface, connecting the tRNA in the peptidyl transferase center to the distally located nasc

136 -helices inside the ribosome tunnel near the peptidyl transferase center under specific conditions.

137 changes occur at several nucleotides in the peptidyl transferase center upon alterations in pH, temp

138 es of 8 rRNA-modifying enzymes targeting the peptidyl transferase center were individually inactivate

139 rom the back of the 50 S particle toward the peptidyl transferase center within the 50 S subunit.

140 ming the three- dimensional structure of the peptidyl transferase center within the ribosome.

141 omain V (which is known to be a component of peptidyl transferase center) and a loop of the helix 35

142 ther universally conserved nucleotide in the peptidyl transferase center, A2451.

143 itionally, a nucleotide located close to the peptidyl transferase center, A2572, which was protected

144 the A loop and P loop, respectively, of the peptidyl transferase center, and G1735A, mapping near a

145 , including the neighborhood surrounding the peptidyl transferase center, and stable association of r

146 ons of two other nucleotide positions in the peptidyl transferase center, C2471 and U2519 (C2452 and

147 S rRNA nucleotides in the 2585 region of the peptidyl transferase center, G2583A and U2584C, were obs

148 onstruct that comprises much of the 23S rRNA peptidyl transferase center, including the central loop

149 -bound tRNAs, whose 3' termini reside in the peptidyl transferase center, label primarily nucleotides

150 in 23S rRNA, which is situated close to the peptidyl transferase center, may participate in one or m

151 Such placement, near the peptidyl transferase center, provides a rationale for th

152 discovered near the decoding center and the peptidyl transferase center, respectively.

153 ethylates an adenosine nucleotide within the peptidyl transferase center, resulting in the C-8 methyl

154 mes, and their effect on conformation in the peptidyl transferase center, the GTPase-associated cente

155 erichia coli 23S rRNA, 14 are located in the peptidyl transferase center, the main antibiotic target

156 iary interactions between nucleotides in the peptidyl transferase center, the SRD, and the GTPase-ass

157 rmB is unperturbed by SrmB deletion, but the peptidyl transferase center, the uL7/12 stalk, and 30S c

158 reates a free tryptophan-binding site in the peptidyl transferase center, where bound tryptophan inhi

159 econd, their acceptor stems are bound by the peptidyl transferase center, which aligns the 3'-aminoac

160 he subunit interface, and junctions near the peptidyl transferase center.

161 r RNA 3'-CCA end is improperly docked in the peptidyl transferase center.

162 f the ribosome such as the tRNA path and the peptidyl transferase center.

163 Nucleotide A2572 is in the ribosomal peptidyl transferase center.

164 binding sites of several antibiotics in the peptidyl transferase center.

165 m to pause before allowing entrance into the peptidyl transferase center.

166 may generalize to other aaRS, as well as the peptidyl transferase center.

167 entified group thought to reside in the rRNA peptidyl transferase center.

168 the CCA end of deacyl-tRNA departs from the peptidyl transferase center.

169 to the E site but remains temporarily in the peptidyl transferase center.

170 re with another activity associated with the peptidyl transferase center.

171 n establishing the tertiary structure of the peptidyl transferase center.

172 ics on the scale of seconds at the ribosomal peptidyl transferase center.

173 is located in the immediate vicinity of the peptidyl transferase center.

174 is known to be a component of the ribosomal peptidyl transferase center.

175 ial for the successful assembly of ribosomal peptidyl transferase center.

176 via tertiary interactions to features of the peptidyl transferase center.

177 f the acceptor end of the A-site tRNA at the peptidyl transferase center.

178 within domains IV and V, which contains the peptidyl transferase center.

179 o position helices 77 and 78 relative to the peptidyl transferase center.

180 interplay between the nascent chain and the peptidyl transferase center.

181 No hydrolytic water molecule was seen in the peptidyl transferase center.

182 o the polypeptide exit tunnel (PET) near the peptidyl transferase center.

183 egion is in close proximity to the ribosomal peptidyl transferase center.

184 as a function of the distance away from the peptidyl transferase center.

185 from adopting an active conformation at the peptidyl transferase center.

186 e accommodation of decoding factors into the peptidyl transferase center.

187 the L27 N-terminus, which protrudes into the peptidyl transferase center.

188 oning the activated ends of tRNAs within the peptidyl transferase center.

189 f the A-tRNA from entering the A site of the peptidyl transferase center.

190 omal tunnel to the exit port, ~100A from the peptidyl transferase center.

191 S rRNA A-loop, an essential component of the peptidyl transferase center.

192 are elongated, one residue at a time, at the peptidyl transferase center.

193 he modern ribosome this remnant includes the peptidyl transferase center.

194 esidue was separated by 14 residues from the peptidyl transferase center.

195 l RNA (rRNA) that includes hairpin 92 of the peptidyl transferase center.

196 y conserved GGQ motif packs tightly into the peptidyl transferase center.

197 ents are normally performed in the ribosomal peptidyl transferase center.

198 23S ribosomal RNA, an important part of the peptidyl transferase center.

199 somal subunit in the cleft that contains the peptidyl transferase center.

200 the RNA-mediated catalysis of the ribosomal peptidyl transferase center.

201 3S rRNA at three sites, all located near the peptidyl transferase center.

202 inhibition of TnaC-tRNA(Pro) cleavage at the peptidyl transferase center.

203 A), especially in the catalytic active site (peptidyl transferase center; PTC), are often functionall

204 l differences are in the conformation of the peptidyl-transferase center (PTC) and the interface betw

205 the sarcin/ricin loop (SRL) and A2531 in the peptidyl-transferase center (PTC) has adverse effects on

206 e tunnel of the ribosome, extending into the peptidyl-transferase center (PTC).

207 owing a disruption of the A-site side of the peptidyl-transferase center (PTC).

208 d helix 44 of 18S rRNA, domain 4 is near the peptidyl-transferase center and its helical subdomain co

209 al subunit bL27m to provide stability to the peptidyl-transferase center during elongation.

210 nd peptidyl-D-aa-tRNA can trap the ribosomal peptidyl-transferase center in a conformation in which p

211 centers in the large subunit, including the peptidyl-transferase center, for unnatural polymer synth

212 tRNAs for binding in the A-site cleft in the peptidyl-transferase center, which is universally conser

213 s access to both the decoding center and the peptidyl-transferase center.

214 that docks the catalytic GGQ motif into the peptidyl-transferase center.

215 rnate secondary structure within the nascent peptidyl-transferase-center (PTC).

216 ment of the ribosome functional decoding and peptidyl transferase centers.

217 evolution, the catalytic site, known as the peptidyl transferase centre (PTC), is thought to be near

218 It takes place in the peptidyl transferase centre of the large (50S) ribosomal

219 nce of the appropriate A-site substrate, the peptidyl transferase centre positions the ester link of

220 wise dominantly lethal rRNA mutations in the peptidyl transferase centre that facilitate the translat

221 lk, empty transfer RNA-binding sites and the peptidyl transferase centre through carboxy-terminal dom

222 tituted peptidyl-tRNA substrate and that the peptidyl transferase centre undergoes a slow inactivatio

223 5 may be a constituent part of the ribosomal peptidyl transferase centre.

224 A UFL1 loop inserts into and remodels the peptidyl transferase centre.

225 Cs in the functional pre-attack state of the peptidyl transferase centre.

226 0S protrusions during accommodation into the peptidyl transferase centre.

227 t tunnel to relay the stalling signal to the peptidyl transferase centre.

228 f RF1 that promotes its interaction with the peptidyl transferase centre.

229 nd is believed to interact directly with the peptidyl-transferase centre (PTC) of the 50S ribosomal s

230 -containing domain of RF2 interacts with the peptidyl-transferase centre (PTC).

231 itioning the conserved C-terminus within the peptidyl-transferase centre to promote recoding.

232 the protein for interaction with rRNA in the peptidyl transferase cleft of the subunit, allowing it t

233 dApPuro, a high-affinity ligand of ribosomal peptidyl transferase designed as a transition-state anal

234 minal domain with the base of the stalk, the peptidyl transferase domain, and the head of the 30 S su

235 In this method, the ribosomal peptidyl transferase forms a peptide bond between two li

236 tivate free tryptophan binding, resulting in peptidyl transferase inhibition.

237 Here, we show that the peptidyl transferase inhibitor sparsomycin triggers accu

238 Chloramphenicol, a peptidyl transferase inhibitor, affected translational f

239 ational frameshifting in the presence of the peptidyl-transferase inhibitor puromycin.

240 ledge on the fundamental mechanisms by which peptidyl transferase inhibitors modulate the catalytic a

241 y increase the susceptibility of bacteria to peptidyl transferase inhibitors.

242 lls harboring this mutation are resistant to peptidyl-transferase inhibitors (e.g., anisomycin).

243 The effects of two peptidyl-transferase inhibitors, anisomycin and sparsomy

244 The ribosomal peptidyl transferase is a biologically essential catalys

245 both aminoacyl-transfer RNA selection and in peptidyl transferase; it may also play an important role

246 toribosomes arose from two cooperating RNAs: peptidyl transferase (large subunit) and mRNA-binder (sm

247 Binding of CCdApPuro by a peptidyl transferase-like motif in the absence of protei

248 h similarity to conserved nucleotides of the peptidyl transferase loop domain of 23S rRNA and is cons

249 erferes with protein synthesis by inhibiting peptidyl transferase or the 80S ribosomal function.

250 ssential integral component of the ribosomal peptidyl transferase, oxazolidinones do not inhibit pept

251 er of macromolecular components required for peptidyl transferase, particles obtained by extraction o

252 ymes (196 nucleotides) that perform the same peptidyl transferase reaction as the ribosome: that is,

253 es are valuable for studies of the ribosomal peptidyl transferase reaction by complete kinetic isotop

254 due with the neutral pK(a) important for the peptidyl transferase reaction cannot be fully supported

255 The ribosome-catalyzed peptidyl transferase reaction displays a complex pH prof

256 tion inhibitor anisomycin, which affects the peptidyl transferase reaction in translation elongation,

257 eature will simplify characterization of the peptidyl transferase reaction mechanism.

258 or the transition state intermediate of the peptidyl transferase reaction show that this reaction pr

259 , translocation, translational accuracy, the peptidyl transferase reaction, and ribosome recycling.

260 s important mechanistic implications for the peptidyl transferase reaction.

261 active-site residues reposition to allow the peptidyl transferase reaction.

262 te acts as an "oxyanion hole" to promote the peptidyl transferase reaction.

263 h is about the same as that reported for the peptidyl transferase reaction.

264 tent with a proton shuttle mechanism for the peptidyl transferase reaction.

265 me in which ribosomal RNA is responsible for peptidyl-transferase reaction catalysis.

266 he 50S subunit of the ribosome catalyzes the peptidyl-transferase reaction of protein synthesis.

267 and specificity to G2553 of 23S rRNA and is peptidyl transferase reactive in its cross-linked state,

268 ivity of A2451 in the center of the 23S rRNA peptidyl transferase region, ascribed to a perturbed pKa

269 nscript mimicking the local structure of the peptidyl transferase site.

270 strategically positioned near the ribosome's peptidyl transferase site.

271 Haloarcula marismortui (Hma) complexed with peptidyl transferase substrate analogues that reveal an

272 Proper placement of the peptidyl transferase substrates, peptidyl-tRNA and amino

273 all peptidoglycan and are novel nonribosomal peptidyl transferases that use aminoacyl-tRNA as the ami

274 rRNA plays an important role in function of peptidyl transferase, the catalytic center of the riboso

275 The previously studied peptidyl transferase transition state analog CC-dA-phosp

276 he G-protein superfamily, catalyzes the post-peptidyl transferase translocation of deacylated tRNA an

277 -encoded peptides are in vitro inhibitors of peptidyl transferase, which is thought to be the basis f