ライフサイエンスコーパス: alanyl-tRNA

1 ditions compromise the efficiency with which alanyl-tRNA(Ala) synthetase can avoid noncognate mischar

2 r by overexpression of the editing domain of alanyl-tRNA(Ala) synthetase that enables detoxification

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

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

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

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

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

8 d yeast assay to co-express pathogenic human alanyl-tRNA synthetase (AARS1) mutations with wild-type

9 We show that mitochondrial alanyl-tRNA synthetase (AARS2) is a protein lysine lacty

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

11 observed that BMAA is a substrate for human alanyl-tRNA synthetase (AlaRS) and can form BMAA-tRNA(Al

12 Editing defects in alanyl-tRNA synthetase (AlaRS) cause neurodegeneration a

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

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

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

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

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

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

19 f proofreading, as recently demonstrated for alanyl-tRNA synthetase (AlaRS), leads to dysregulation o

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

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

22 n AARS2 (NM_020745.2) encoding mitochondrial alanyl-tRNA synthetase (mt-AlaRS) were first described i

23 Here, we identify alanyl-tRNA synthetase 1 and methionyl-tRNA synthetase 1

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

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

26 activator of hsp90 ATPase protein 1 (Aha1), alanyl-tRNA synthetase domain containing 1 (Aarsd1), cel

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

28 Alanyl-tRNA synthetase efficiently aminoacylates tRNAAla

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

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

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

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

33 Alanyl-tRNA synthetase retains a conserved prototype str

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

49 ) that are substrates of bacterial and human alanyl-tRNA synthetase.

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

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

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

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

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

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

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

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

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