ライフサイエンスコーパス: alanyl-tRNA

1 al neuropathy, demonstrating that defects of alanyl-tRNA charging can result in a wide spectrum of di

2 Ps in the coding regions of two human mRNAs: alanyl tRNA synthetase and replication protein A, 70-kDa

3 s that bacterial GlyRS is closely related to alanyl tRNA synthetase, which led us to define a new sub

4 e relatively easily altered to be charged by alanyl tRNA synthetase.

5 identified mutations in the nuclear-encoded alanyl-tRNA synthetase (AARS) in these two unrelated fam

6 ntly recognized by A. gossypii mitochondrial alanyl-tRNA synthetase (AgAlaRS).

7 tion of alanine-specific tRNA (tRNA(Ala)) by alanyl-tRNA synthetase (AlaRS) gave rise to the concept

8 Here we show that the class II alanyl-tRNA synthetase (AlaRS) has a specialized interna

9 Throughout evolution, tRNA(Ala) selection by alanyl-tRNA synthetase (AlaRS) has depended predominantl

10 Transfer of alanine from Escherichia coli alanyl-tRNA synthetase (AlaRS) to RNA minihelices that m

11 machinery provides MurM, quality control by alanyl-tRNA synthetase (AlaRS) was investigated.

12 ) that are associated with aminoacylation by alanyl-tRNA synthetase (AlaRS) were investigated in vivo

13 ypomorphic mutation in the editing domain of alanyl-tRNA synthetase (AlaRS), resulted in accumulation

14 major determinants for recognition by Dm mt alanyl-tRNA synthetase (AlaRS).

15 Paradoxically, although alanyl-tRNA synthetase activates glycine as well as alan

16 es of an active fragment of Aquifex aeolicus alanyl-tRNA synthetase complexed, separately, with Mg2+-

17 minihelix) lacked determinants for editing, alanyl-tRNA synthetase effectively cleared a mischarged

18 Alanyl-tRNA synthetase efficiently aminoacylates tRNAAla

19 Data on alanyl-tRNA synthetase from an early eukaryote and other

20 ssense mutation in the editing domain of the alanyl-tRNA synthetase gene that compromises the proofre

21 d, a small defect in the editing activity of alanyl-tRNA synthetase is causally linked to neurodegene

22 he AlaXp redundancy of the editing domain of alanyl-tRNA synthetase is thought to reflect an unusual

23 y was within 1-2 kcal.mol(-1) of a truncated alanyl-tRNA synthetase that has aminoacylation activity

24 Here we identify a two-helix pair in alanyl-tRNA synthetase that is required for RNA microhel

25 he transfer of alanine from Escherichia coli alanyl-tRNA synthetase to a cognate RNA minihelix involv

26 e contacts between tRNA and Escherichia coli alanyl-tRNA synthetase, an enzyme previously shown to in

27 ponents, such as the alpha-subunit of phenyl-alanyl-tRNA synthetase, and several metabolic enzymes.

28 Here we show that the editing site of alanyl-tRNA synthetase, as an artificial recombinant fra

29 te that prevents aminoacylation by the dicot alanyl-tRNA synthetase, indicating that features identif

30 When applied to Escherichia coli alanyl-tRNA synthetase, the assay allowed accurate measu

31 d by a strain harboring an editing-defective alanyl-tRNA synthetase, was rescued by an AlaXp-encoding

32 agenesis of the homologous editing pocket of alanyl-tRNA synthetase, where even a mild defect in edit

33 , we examined a fragment of Escherichia coli alanyl-tRNA synthetase, which catalyzes aminoacyl adenyl

34 Similarly, autonomous alanyl-tRNA synthetase-editing domain homologues (AlaX p

35 (G3.U70) marks a tRNA for aminoacylation by alanyl-tRNA synthetase.

36 for clearance of errors of aminoacylation by alanyl-tRNA synthetase.

37 We report that CDC64 encodes Ala1p, an alanyl-tRNA synthetase.

38 not to be a substrate for (re)activation by alanyl-tRNA synthetase.Application of the optimized syst

39 sing from confusion of serine for alanine by alanyl-tRNA synthetases (AlaRSs) has profound functional

40 evented in part by the editing activities of alanyl-tRNA synthetases (AlaRSs), which remove serine fr

41 rative aminoacylation and editing domains of alanyl-tRNA synthetases (AlaRSs).

42 n bacterial and eukaryotic threonyl- and all alanyl-tRNA synthetases is missing from archaebacterial

43 G. lamblia's archaeal-type prolyl- and alanyl-tRNA synthetases refine our understanding of the

44 nine, is activated by both human prolyl- and alanyl-tRNA synthetases.

45 ome-encoded homolog of the editing domain of alanyl-tRNA synthetases.

46 yzes the transfer of the alanyl residue from alanyl-tRNA to the N terminus of the tetrapeptide interm