ライフサイエンスコーパス: alanyl-tRNA synthetase

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

37 Alanyl-tRNA synthetase efficiently aminoacylates tRNAAla

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

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

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

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

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

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

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

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

46 Alanyl-tRNA synthetase retains a conserved prototype str

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

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

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

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

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

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

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

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