ライフサイエンスコーパス: histidyl-tRNA synthetase

1 ing of uncharged tRNA to a domain related to histidyl tRNA synthetase.

2 ation of mutants in the gene (hisS) encoding histidyl-tRNA synthetase.

3 f G(-1) to allows efficient histidylation by histidyl-tRNA synthetase.

4 equire the GCN2 regulatory domain related to histidyl tRNA synthetases.

5 four HisZ regulatory subunits that resemble histidyl-tRNA synthetases.

6 four HisZ regulatory subunits that resemble histidyl-tRNA synthetases.

7 Specifically, M88 recognizes histidyl-tRNA synthetase, an antigen known to be also ta

8 catalytic domain and a domain homologous to histidyl-tRNA synthetase and by the ability of dGCN2 to

9 necessary for the proper functioning of the histidyl-tRNA synthetase, and suggests a novel mechanism

10 as a risk factor for the development of anti-histidyl tRNA synthetase antibodies, and HLA-DRB1*11:01

11 ystal structure of the Staphylococcus aureus histidyl-tRNA synthetase apoprotein has been determined

12 required for aminoacylation of tRNA(His) by histidyl-tRNA synthetase, both in vitro and in vivo.

13 Gcn2p has a regulatory region homologous to histidyl tRNA synthetase enzymes that binds uncharged tR

14 to isolate secondary site revertants in the histidyl-tRNA synthetase from E. coli which restore hist

15 Recently, a mutation in histidyl-tRNA synthetase (HARS) was identified in a sing

16 One example from human histidyl-tRNA synthetase (HARS), termed HARS(WHEP) becau

17 ozygosity for mutations in the mitochondrial histidyl tRNA synthetase HARS2 at two highly conserved a

18 ture of the closely related Escherichia coli histidyl-tRNA synthetase (HisRS) as a guide, two mutants

19 exhibits significant sequence identity with histidyl-tRNA synthetase (HisRS) but does not aminoacyla

20 ion binds to sequences in GCN2 homologous to histidyl-tRNA synthetase (HisRS) enzymes, leading to enh

21 sociating with Gcn2p sequences homologous to histidyl-tRNA synthetase (HisRS) enzymes.

22 Crystal structures of histidyl-tRNA synthetase (HisRS) from the eukaryotic par

23 hia coli, the aminoacylation of tRNA(His) by histidyl-tRNA synthetase (HisRS) is highly dependent upo

24 ement in histidine tRNAs and residues in the histidyl-tRNA synthetase (HisRS) motif 2 loop.

25 Autoantibodies to histidyl-tRNA synthetase (HisRS) or to alanyl-, asparagi

26 GCN2 contains a regulatory domain related to histidyl-tRNA synthetase (HisRS) postulated to bind mult

27 In class II histidyl-tRNA synthetase (HisRS) the nonbridging S(p)-ox

28 This is the major recognition element for histidyl-tRNA synthetase (HisRS) to permit acylation of

29 domains of the homodimeric Escherichia coli histidyl-tRNA synthetase (HisRS) were separately express

30 In class II histidyl-tRNA synthetase (HisRS), amino acid activation

31 Gcn2 activation requires a domain related to histidyl-tRNA synthetase (HisRS), the enzyme that aminoa

32 noacyl transfer in class II Escherichia coli histidyl-tRNA synthetase (HisRS), we devised a rapid que

33 CN2, requires binding of uncharged tRNA to a histidyl-tRNA synthetase (HisRS)-like domain in GCN2.

34 rved cells on binding of uncharged tRNA to a histidyl-tRNA synthetase (HisRS)-related domain.

35 domains, including a pseudokinase domain, a histidyl-tRNA synthetase (HisRS)-related region, and a C

36 ing of uncharged tRNA to a domain related to histidyl-tRNA synthetase (HisRS).

37 d that GCN2 sequences containing homology to histidyl-tRNA synthetases (HisRS) bind uncharged tRNA th

38 ministration of bacterially expressed murine histidyl-tRNA synthetase (HRS) triggers florid muscle in

39 Moreover, the cytosolic histidyl-tRNA synthetase in A. castellanii exhibits an u

40 Thg1p-depleted cells is uncharged, although histidyl tRNA synthetase is active and the 3' end of the

41 at the level of binding by Escherichia coli histidyl-tRNA synthetase is addressed by filter binding,

42 The Gcn2p regulatory domain homologous to histidyl-tRNA synthetases is proposed to bind to uncharg

43 nst nuclear and cytoplasmic Ags that include histidyl-tRNA synthetase (Jo-1).

44 has expanded; antibodies to the autoantigen histidyl-tRNA synthetase (Jo1) being the commonest and b

45 yeast, GCN2, contains a region homologous to histidyl-tRNA synthetases juxtaposed to the kinase catal

46 substitute for the P stalk in binding to the histidyl-tRNA synthetase-like domain of Gcn2 for eIF2alp

47 mino acids by binding of uncharged tRNA to a histidyl-tRNA synthetase-like domain.

48 f mutations in HARS2, encoding mitochondrial histidyl-tRNA synthetase, mutations in CLPP expose dysfu

49 lls having a temperature-sensitive mutant of histidyl tRNA synthetase, p70(s6k) was suppressed by a t

50 tion requires binding of uncharged tRNA to a histidyl tRNA synthetase-related domain in GCN2.

51 Flanking the carboxyl terminus of the histidyl-tRNA synthetase-related domain is a region span

52 ent chemical modification experiments in the histidyl-tRNA synthetase system, emphasizes that substra

53 d sequence of tRNA(His) and at many sites in histidyl-tRNA synthetase that might be expected to affec

54 , including, in some mice, autoantibodies to histidyl-tRNA synthetase, the most common specificity fo

55 and essential for recognition by the cognate histidyl-tRNA synthetase to allow efficient His-tRNA(His

56 c interaction between MA and HO3, a putative histidyl-tRNA synthetase, was demonstrated in this syste

57 site fragments of Escherichia coli Class II histidyl-tRNA synthetase were constructed, expressed as

58 catalytic core of the contemporary class II histidyl-tRNA synthetase whose members lack aminoacylati