The "allosteric three-site model" of elongation cannot be confirmed in a well-defined ribosome system from Escherichia coli
about
Deacylated tRNA is released from the E site upon A site occupation but before GTP is hydrolyzed by EF-Tu.Function of the ribosomal E-site: a mutagenesis study.Kinetics of initiating polypeptide elongation in an IRES-dependent systemRPS25 is essential for translation initiation by the Dicistroviridae and hepatitis C viral IRESsThe role of L1 stalk-tRNA interaction in the ribosome elongation cycleBinding interaction between Tet(M) and the ribosome: requirements for binding.Photolabile anticodon stem-loop analogs of tRNAPhe as probes of ribosomal structure and structural fluctuation at the decoding center.Role of a tRNA base modification and its precursors in frameshifting in eukaryotes.Mechanism of elongation factor G function in tRNA translocation on the ribosome.Allosteric vs. spontaneous exit-site (E-site) tRNA dissociation early in protein synthesisProtein Synthesis in E. coli: Dependence of Codon-Specific Elongation on tRNA Concentration and Codon Usage.Further in vitro exploration fails to support the allosteric three-site model.Genetic analysis of the E site during RF2 programmed frameshifting.Are the current three-site models valid descriptions of the ribosomal elongation cycle?Real-time assay for testing components of protein synthesis.The elongation, termination, and recycling phases of translation in eukaryotes.The integrity of the G2421-C2395 base pair in the ribosomal E-site is crucial for protein synthesisRibosomal frameshifting used in influenza A virus expression occurs within the sequence UCC_UUU_CGU and is in the +1 direction.A new kinetic model reveals the synergistic effect of E-, P- and A-sites on +1 ribosomal frameshifting.Destabilization of the P site codon-anticodon helix results from movement of tRNA into the P/E hybrid state within the ribosome.Following movement of the L1 stalk between three functional states in single ribosomes.Allosteric collaboration between elongation factor G and the ribosomal L1 stalk directs tRNA movements during translationFidelity at the molecular level: lessons from protein synthesis.Coordinated conformational and compositional dynamics drive ribosome translocation.A structural view on the mechanism of the ribosome-catalyzed peptide bond formation.Synchronous tRNA movements during translocation on the ribosome are orchestrated by elongation factor G and GTP hydrolysis.Models of the elongation cycle: an evaluation.GTP hydrolysis by EF-G synchronizes tRNA movement on small and large ribosomal subunits.Elongation factor G stabilizes the hybrid-state conformation of the 70S ribosome.Real-time tRNA transit on single translating ribosomes at codon resolution.A role for the 30S subunit E site in maintenance of the translational reading frame.Reverse translocation of tRNA in the ribosome.Functional importance of the 3'-terminal adenosine of tRNA in ribosomal translation.Three tRNAs on the ribosome slow translation elongation.Ribosomal tRNA binding sites: three-site models of translation.Spontaneous reverse movement of mRNA-bound tRNA through the ribosome.
P2860
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P2860
The "allosteric three-site model" of elongation cannot be confirmed in a well-defined ribosome system from Escherichia coli
description
article científic
@ca
article scientifique
@fr
articolo scientifico
@it
artigo científico
@pt
bilimsel makale
@tr
scientific article published on October 1996
@en
vedecký článok
@sk
vetenskaplig artikel
@sv
videnskabelig artikel
@da
vědecký článek
@cs
name
The "allosteric three-site mod ...... e system from Escherichia coli
@en
The "allosteric three-site mod ...... system from Escherichia coli.
@nl
type
label
The "allosteric three-site mod ...... e system from Escherichia coli
@en
The "allosteric three-site mod ...... system from Escherichia coli.
@nl
prefLabel
The "allosteric three-site mod ...... e system from Escherichia coli
@en
The "allosteric three-site mod ...... system from Escherichia coli.
@nl
P2860
P356
P1476
The "allosteric three-site mod ...... e system from Escherichia coli
@en
P2093
W Wintermeyer
Y P Semenkov
P2860
P304
12183-12188
P356
10.1073/PNAS.93.22.12183
P407
P577
1996-10-01T00:00:00Z