1988
DOI: 10.1038/334362a0
|View full text |Cite
|
Sign up to set email alerts
|

Interaction of elongation factors EF-G and EF-Tu with a conserved loop in 23S RNA

Abstract: The elongation factors EF-Tu and EF-G interact with ribosomes during protein synthesis: EF-Tu presents incoming aminoacyl transfer RNA to the programmed ribosome as an EF-Tu-GTP-tRNA ternary complex and EF-G promotes translocation of peptidyl-tRNA and its associated messenger RNA from the A to the P site after peptidyl transfer. Both events are accompanied by ribosome-dependent GTP hydrolysis. Here we use chemical probes to investigate the possible interaction of these factors with ribosomal RNA in E. coli rib… Show more

Help me understand this report

Search citation statements

Order By: Relevance

Paper Sections

Select...
2
1

Citation Types

20
349
0
3

Year Published

1997
1997
2014
2014

Publication Types

Select...
4
3

Relationship

0
7

Authors

Journals

citations
Cited by 489 publications
(372 citation statements)
references
References 26 publications
20
349
0
3
Order By: Relevance
“…Fig. 1B), are protected from chemical modification by the binding of EF-G to 70S ribosomes (11) and are presumptive RNA identity elements for the factor, although protection by a ligand from chemical modification does not of necessity connote a direct interaction. Oligoribonucleotides having deletions, transversions, and transitions of these three purines were constructed, and the effects of the mutations on the binding of EF-G were assessed (Fig.…”
Section: Resultsmentioning
confidence: 99%
See 3 more Smart Citations
“…Fig. 1B), are protected from chemical modification by the binding of EF-G to 70S ribosomes (11) and are presumptive RNA identity elements for the factor, although protection by a ligand from chemical modification does not of necessity connote a direct interaction. Oligoribonucleotides having deletions, transversions, and transitions of these three purines were constructed, and the effects of the mutations on the binding of EF-G were assessed (Fig.…”
Section: Resultsmentioning
confidence: 99%
“…Fig. 5A) is involved in EF-G-dependent functions (5)(6)(7)(8)(9)(10)(11). Thiostrepton, an antibiotic that inhibits binding of EF-G to ribosomes (5), binds to a 23S rRNA fragment that has A1067 (26); in addition, methylation of the 2Ј-hydroxyl of A1067 confers resistance to thiostrepton in strains of Streptomyces aureus (6).…”
Section: Resultsmentioning
confidence: 99%
See 2 more Smart Citations
“…Here, it is important to consider the effect of the SRL of the 23S rRNA subunit, and, in particular the role of residue A2662 (see Fig. 33 for relative positions), whose critical role has been already pointed out elsewhere (Hausner et al 1987 ;Lancaster et al 2008 ;Moazed et al 1988). Significantly, our simulations of the EF-Tu'/ribosome complex found that the presence of the SRL loop (with its A2662 residue) was essential for the proper positioning of H84 (without any additional artificial force constraints).…”
Section: Efs and Ribosomal Activationmentioning
confidence: 99%