ライフサイエンスコーパス: tRNA(Lys)

1 These undermodified tRNALys,3 anticodon loops are distinctly different from

2 anticodon recognition and for utilization of tRNALys,3 by HIV-1 as the native reverse transcriptase p

3 Viral Pol proteins influenced tRNAlys,3 packaging but had little influence on virion p

4 ication and the additional A+-C base-pair on tRNALys,3 structure.

5 cleotides comprising the anticodon domain of tRNALys,3.

6 t from those for viral genomic RNA or primer tRNAlys,3.

7 All mutants showed reduced affinity for tRNALys-3 and supported significantly less (-)-strand DN

8 sis that mutant PBS reversion is a result of tRNALys-3 annealing onto and extension from a PBS that s

9 of HIV-1 RT supports an interaction with the tRNALys-3 anticodon loop critical for efficient (-)-stra

10 V type 1 (HIV-1) specifically uses host cell tRNALys-3 as a primer for reverse transcription.

11 Structural features of binary RT.tRNALys-3 complexes were examined by in situ footprintin

12 We have developed a mutant tRNALys-3 derivative with mutations in the PBS-binding r

13 tRNALys-3 interacts directly with HIV-1 reverse transcri

14 rast, NC promotes specific annealing of only tRNALys-3 onto an RNA template (HXB2) whose PBS sequence

15 ements outside the acceptor-TPsiC domains of tRNALys-3 play an important role in preferential primer

16 Cellular tRNALys-3 serves as the primer for reverse transcription

17 Recently, tRNALys-3 was cross-linked via its anticodon loop to hum

18 uences quickly revert to be complementary to tRNALys-3.

19 as that the G2.U71 wobble pair of spirochete tRNALys acts as antideterminant for class II LysRS but d

20 EF-G-catalyzed translocation step of the two tRNALys and the slippery codons from the A- and P- sites

21 e unfolding process of charged and uncharged tRNALys and tRNALeu(UUR) has revealed that the separatio

22 Purified Arg-tRNALys, Thr-tRNALys, and Met-tRNALys were essentially not deacylated

23 f structure-based sequence alignments, seven tRNALys anticodon variants and seven LysRS1 anticodon bi

24 lass I LysRSs recognize the same elements in tRNALys as their class II counterparts, namely the discr

25 cific recognition of the same nucleotides in tRNALys by the two unrelated types of enzyme suggests th

26 uggest that specificity for the anticodon of tRNALys could have been acquired through relatively few

27 Refinement of the LysRS1-tRNALys docking model based upon these data suggested th

28 analysis of the Pyrococcus horikoshii LysRS1-tRNALys docking model.

29 nzyme whose major function is to provide Lys-tRNALys for protein synthesis, also catalyzes aminoacyla

30 rtions have been identified in the T loop of tRNALys from Didymium and tRNAGlu from Physarum.

31 of nucleotide (nt) 8344 in the mitochondrial tRNALys gene, were examined for the proportion of mutant

32 egion containing avrPphB was inserted into a tRNALYS gene, which was re-formed at the right junction

33 This observation indicates that the tRNALys initiation step plays an important role in the d

34 ng length variation analysis of the COII and tRNALYS intergenic region, nucleotide sequence analysis

35 sRS), are required for specific packaging of tRNALys into virions.

36 that suggest the importance of the ratio of tRNALys isoacceptors in Type-2 diabetes.

37 two unrelated types of enzyme suggests that tRNALys predates at least one of the LysRSs in the evolu

38 inary complex does not occur when a chimeric tRNALys/Pro containing proline-specific D and anticodon

39 To examine the specificity of tRNALys selection, E. coli tRNA3Lys was modified to tRNA

40 ass I-type enzyme to aminoacylate particular tRNALys species and provides a molecular basis for the o

41 Purified Arg-tRNALys, Thr-tRNALys, and Met-tRNALys were essentially n

42 transfer (smFRET) between (Cy5)EF-G and (Cy3)tRNALys, we studied the translational elongation dynamic

43 Purified Arg-tRNALys, Thr-tRNALys, and Met-tRNALys were essentially not deacylated by LysRS, indica

44 synthesis, also catalyzes aminoacylation of tRNALys with arginine, threonine, methionine, leucine, a

45 trand contains the UUU anticodon sequence of tRNALys with flanking GCs to increase duplex stability.

46 ing mechanism which prevents misacylation of tRNALys with ornithine.