ライフサイエンスコーパス: Phe-tRNA

1 Binding of the ternary complex [14C]Phe-tRNA-elongation factor Tu.guanyl-5'-yl imidodiphosph

2 .guanyl-5'-yl imidodiphosphate) but not [14C]Phe-tRNA.elongation factor Tu.GDP.kirromycin increased l

3 is synthesized for every approximately 7,300 Phe-tRNA(Phe), compatible with an error rate in translat

4 the presence of deacyl-tRNA(Phe) or N-acetyl-Phe-tRNA(Phe) using poly(U) or an mRNA analogue containi

5 For N-acetyl-Phe-tRNA(Phe) with either poly(U) or the mRNA analogue,

6 esence of a peptidyl tRNA analogue, N-acetyl-Phe-tRNA(Phe), in the A site, which mimicked the post-pe

7 Binding of N-acetylated Phe-tRNA(Phe), an analog of the initiator fMet-tRNA(Met)

8 d during oxidative stress, while the cognate Phe-tRNA(Phe) aminoacylation activity is unchanged.

9 some bound with ternary complexes containing Phe-tRNA(Phe), Trp-tRNA(Trp), or Leu-tRNA(LeuI).

10 formation and dissociation of the EF-Tu-GTP-Phe-tRNA(Phe) ternary complex.

11 ant has a reduced affinity for mitochondrial Phe-tRNA(Phe).

12 active in polymerization with mitochondrial Phe-tRNA(Phe), this variant has low activity in the form

13 and slow phases similar to those for natural Phe-tRNA(Phe).

14 his tRNA, but still 2-fold less than natural Phe-tRNA(Phe).

15 conserved G37, adjacent to the anticodon of Phe tRNAs.

16 conserved base pairs in the tertiary core of Phe-tRNA(Phe), 18-55 and 19-56, on rate and equilibrium

17 s on the side chain of the esterified Phe of Phe-tRNA(Phe).

18 elongation as measured by polymerization of Phe-tRNA on a poly(U) template in presence of GDP can be

19 ues within the editing site had no effect on Phe-tRNA(Phe) synthesis, but abolished hydrolysis of Tyr

20 rameric protein responsible for synthesizing Phe-tRNA(Phe) during protein synthesis.

21 og and provide the most complete view of the Phe-tRNA synthetase/tRNAPhe system to date.

22 With a single exception (tRNA(Phe)-tRNA(Glu) pair), the parallelism is especially impr

23 rce in complexes carrying an aminoacyl tRNA, Phe-tRNA(Phe), in the A site, indicating that the SD int

24 We report structures of M. tuberculosis Phe-tRNA synthetase complexed with an unmodified tRNAPhe

25 upture force as compared to the complex with Phe-tRNA(Phe), and the resultant force was the same for

26 e affinities of the mutant proteins to yeast Phe-tRNA(Phe) determined.

27 do]triphosphate (EF-Tu.GDPNP) bound to yeast Phe-tRNA(Phe) reveals that EF-Tu interacts with the tRNA