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1 extended FemABX family as novel nonribosomal peptidyltransferases.
6 ent of anisomycin resistance and a decreased peptidyltransferase activity and increased frameshifting
7 Escherichia coli numbering) is implicated in peptidyltransferase activity and represents one of the t
9 78 N-terminal residues, retained measurable peptidyltransferase activity and wild type substrate spe
10 ld interfere with PTC function by inhibiting peptidyltransferase activity and/or by restricting PTC A
11 es were shown to have essentially unimpaired peptidyltransferase activity at saturating substrate con
13 hat various oxazolidinones inhibit ribosomal peptidyltransferase activity in the simple reaction of 7
14 is that alterations affecting the ribosome's peptidyltransferase activity lead to changes in frameshi
22 though genetic data pointed to the ribosomal peptidyltransferase as the primary site of drug action,
25 re of an L/F-transferase and revealed that a peptidyltransferase catalyst may be constructed from app
29 pport the hypothesis that alterations in the peptidyltransferase center affect programmed -1 ribosoma
30 n folds into a compact conformation near the peptidyltransferase center and remains folded as the seq
31 omoting Sec-tRNA(Sec) accommodation into the peptidyltransferase center and/or by stimulating the rib
33 e alpha-sarcin loop has been placed near the peptidyltransferase center in Escherichia coli ribosomes
37 amphenicol, suggesting that Tcin targets the peptidyltransferase center of mitochondrial ribosomes.
39 others have shown that residue A2451 in the peptidyltransferase center of the Escherichia coli 50S r
40 n process, wherein aminoacyl-tRNA enters the peptidyltransferase center of the large ribosomal subuni
41 ow alpha-helix formation directly within the peptidyltransferase center of the ribosome interferes wi
44 3, a highly conserved protein located at the peptidyltransferase center of the ribosomes, is involved
46 otein seems capable of contacting either the peptidyltransferase center or the decoding center, so it
47 s an essential RNA component of the ribosome peptidyltransferase center that directly interacts with
49 protein L27, whose N terminus may reach the peptidyltransferase center, and LepA, a protein homologo
50 approximately 38 residues from the ribosome peptidyltransferase center, and TM2-Sec61alpha photoaddu
51 large ribosomal subunit RNA belonging to the peptidyltransferase center, are encoded in all extensive
52 the elongation factor binding region and the peptidyltransferase center, facilitating coordination of
53 formation after moving 6-7 residues from the peptidyltransferase center, irrespective of loop size.
54 e structure of the active site in the E.coli peptidyltransferase center, its lack of conservation mak
55 h encodes a ribosomal protein located at the peptidyltransferase center, promote approximately three-
56 es in 25S rRNA that link the B1a bridge, the peptidyltransferase center, the GTPase-associated center
70 the L/F-transferase is not a homolog of the peptidyltransferase enzymes involved in cell wall peptid
71 e bond formation, catalyzed by the ribosomal peptidyltransferase, has long been known to be sensitive
72 ing initiation, susceptibility/resistance to peptidyltransferase inhibitors, and the ability of ribos
73 bition is substrate-independent and that the peptidyltransferase itself is the oxazolidinone target.
74 ant of yeast, harboring the mak8-1 allele of peptidyltransferase-linked ribosomal protein L3 (RPL3),
75 ine to atom N6 of an adenine base within the peptidyltransferase loop of 23 S rRNA, thus conferring a
76 initiator fMet-tRNA(i)(Met) to the ribosomal peptidyltransferase P-site, which is vacant only prior t
79 he essential residues required to catalyze a peptidyltransferase reaction and revealed that <20% of t
80 ansferase) from Escherichia coli catalyzes a peptidyltransferase reaction that results in the N-termi
81 rapid equilibrium, ordered mechanism of the peptidyltransferase reaction, wherein binding of the A-s
83 Taken together, these results implicate the peptidyltransferase site as a regulator of both JNK/p38
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