Disease relevance of tsf

• The putative chlamydial tsf gene was expressed in E. coli as a nonfusion protein and as a 6x His-tagged fusion protein [1].
• The present study shows that the Escherichia coli mutant GRd.tsf lacking the coiled-coil motif of EF-Ts is completely resistant to phage Qbeta and that Qbeta-polymerase complex formation is not observed [2].
• Structure and importance of the dimerization domain in elongation factor Ts from Thermus thermophilus [3].
• Cloning and partial characterization of the gene encoding the putative elongation factor Ts of Streptococcus suis serotype 2 [4].
• Elongation factor Ts of Chlamydia trachomatis: structure of the gene and properties of the protein [1].

High impact information on tsf

• Inhibition of RNA polymerase activity by the Escherichia coli protein biosynthesis elongation factor Ts [5].
• The synthesized L12 can be bound to L12-depleted ribosomes and the synthesized elongation factor Tu can form complexes with both elongation factor Ts and GDP [6].
• We have studied the effects of specific amino acid replacements in EF-Tu upon the protein's interactions with guanine nucleotides and elongation factor Ts (EFTs) [7].
• However, this activity showed different sensitivities to heat and N-ethylmaleimide compared to the EF-Ts activity [8].
• Inactivation of Escherichia coli elongation factor Ts by the arginine-specific reagent butanedione [9].

Biological context of tsf

• The putative tsf gene seems to be transcribed from a promoter located within the cloned DNA fragment, as its expression is not dependent on insertional orientation within the plasmid [4].
• One copy of the tsf gene was detected in the chromosome of S. suis by Southern blot analysis [4].
• The end of an open reading frame preceding the atp genes shows remarkable homology to elongation factor TS from Escherichia coli [10].
• The loss of Mg(2+) alone, without EF-Ts, accounts for a 150-300-fold acceleration of GDP dissociation from EF-Tu.GDP, suggesting that the disruption of the Mg(2+) binding site alone does not explain the EF-Ts effect [11].
• In this study, the sequence encoding the coiled-coil motif in EF-Ts was deleted from the genome in Escherichia coli by gene replacement [12].

Anatomical context of tsf

• The cDNA for a homologue of elongation factor Ts which probably functions in mitochondria has been sequenced from a nematode Caenorhabditis elegans [13].

Associations of tsf with chemical compounds

• The role of cysteinyl residues in the activity of bacterial elongation factor Ts, a guanosine nucleotide dissociation protein [14].
• Replacement of Cys-22 by Ser or Gly only partially impairs the binding or catalytic properties of EF-Ts while it completely protects EF-Ts from the inactivation by NEM [14].
• The present results also indicate that the deletion alters the competition between EF-Ts and kirromycin for the binding to EF-Tu [12].

Regulatory relationships of tsf

• The effects are attributed to the interference of the mutations with the EF-Ts-induced movements of the P-loop of EF-Tu and changes at the domain 1/3 interface, leading to the release of the beta-phosphate group of GTP/GDP [15].

Other interactions of tsf

• The kinetic results suggest that the initial contact of EF-Ts with helix D of EF-Tu weakens binding interactions around the guanine base, whereas contacts of EF-Ts with the phosphate binding side that promotes the release of the phosphate moiety of GDP appear to take place later [16].

Analytical, diagnostic and therapeutic context of tsf

• Interestingly, the elongation factor Ts expressed by all reference strains of all S. suis serotypes were antigenically similar, as determined by Western blot [4].

References