ライフサイエンスコーパス: histidyl-tRNA

1 The histidyl-tRNA from Escherichia coli is distinguished by

2 attenuation mechanism in which the level of histidyl-tRNA serves as a key sensor of the intracellula

3 . coli which restore histidine identity to a histidyl-tRNA suppressor carrying U73.

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

62 (Thg1) enzyme, and no examples of eukaryotic histidyl-tRNAs that lack this essential element have bee