ライフサイエンスコーパス: tRNA(Cys

1 ) and cysteinyl-tRNA synthetase (forming Cys-tRNA(Cys)).

2 n one other tRNA, the Haemophilus influenzae tRNA(Cys).

3 mportant for aminoacylation of H. influenzae tRNA(Cys).

4 n the ability of the cysteine enzyme to bind tRNA(Cys).

5 replication partially overlaps the adjacent tRNA(Cys).

6 rm14, which generates m(2)G at position 6 in tRNA(Cys).

7 o highly sensitive to the A37G transition in tRNA(Cys).

8 overcomes the cross-species barrier in human tRNA(Cys).

9 A(Cys) and subsequently converting it to Cys-tRNA(Cys).

10 rom a defect in kcat, rather than the Km for tRNA(Cys).

11 iring alanine onto nonalanyl-tRNAs including tRNA(Cys).

12 ment of proline to tRNA(Pro) and cysteine to tRNA(Cys).

13 ors to facilitate the synthesis of cysteinyl-tRNA(Cys).

14 by a transformation of serine misacylated to tRNACys.

15 rand replication, and secondary structure of tRNACys.

16 portant element in aminoacylation of E. coli tRNA(Cys), a better understanding of its structure in th

17 Resulting from the historical study of tRNA(Cys) aminoacylation and the integrative perspective

18 Most organisms form Cys-tRNA(Cys), an essential component for protein synthesis,

19 etween the acceptor stem of Escherichia coli tRNA(Cys) and cysteine-tRNA synthetase.

20 eotides for their ability to bind to E. coli tRNA(Cys) and inhibit aminoacylation.

21 RNA synthetase can synthesize both cysteinyl-tRNA(Cys) and prolyl-tRNA(Pro).

22 way, first charging phosphoserine (Sep) onto tRNA(Cys) and subsequently converting it to Cys-tRNA(Cys

23 lthough analysis of the crystal structure of tRNA(Cys) and tRNA(Gln) implicated long-range tertiary b

24 s maripaludis synthetases SepRS (forming Sep-tRNA(Cys)) and cysteinyl-tRNA synthetase (forming Cys-tR

25 The enzyme recognizes the acceptor stem of tRNA(Cys), as micro- and minihelices, truncated versions

26 i6A37 increased the activity of tRNACys at a cognate codon and that of tRNATyr at a near

27 Methanocaldococcus jannaschii indicated that tRNA(Cys) becomes acylated with O-phosphoserine (Sep) bu

28 us enables a global long-range channeling of tRNA(Cys) between SepRS and SepCysS distant active sites

29 The trend in EF-Tu.Cys-tRNA(Cys) binding energies observed as the result of mut

30 tRNA(Cys) binding to SepRS also enhances the capacity of

31 Synthesis of cysteinyl-tRNA(Cys) by cysteine-tRNA synthetase is required for de

32 ylated intermediate is then converted to Cys-tRNA(Cys) by Sep-tRNA:Cys-tRNA synthase (SepCysS) via a

33 ep-tRNA(Cys), which is then converted to Cys-tRNA(Cys) by SepCysS.

34 show here that the attachment of cysteine to tRNA(Cys) by the class I cysteinyl-tRNA synthetase (CysR

35 cs of the EF-Tu.guanosine 5'-triphosphate.aa-tRNA(Cys) complex and the roles played by Mg2+ ions and

36 ructures of Saccharomyces cerevisiae DMATase-tRNA(Cys) complex in four distinct forms, which provide

37 Escherichia coli tRNACys contains an unusual G15.G48 tertiary base pair t

38 ious work has shown that CysRS aminoacylates tRNA(Cys) core regions containing G15-G48 with much bett

39 dentify alternative functional design of the tRNA(Cys) core that contains G15:C48.

40 ound O-phosphoserine (Sep) to form cysteinyl-tRNA(Cys) (Cys-tRNA(Cys)) in methanogens that lack the c

41 ethanogenic archaea synthesize the cysteinyl-tRNA(Cys) (Cys-tRNA(Cys)) needed for protein synthesis u

42 to also catalyze the synthesis of cysteinyl-tRNA(Cys) (Cys-tRNA(Cys)) to make up for the absence of

43 irect pathway for the synthesis of cysteinyl-tRNA(Cys) during protein synthesis.

44 on of a mismatching O-phosphoserine (Sep) to tRNA(Cys) followed by the conversion of tRNA-bounded Sep

45 nce of covalent continuity of both CysRS and tRNA(Cys) for efficient tRNA aminoacylation, and highlig

46 sRS), the essential enzyme that provides Cys-tRNA(Cys) for translation in most organisms.

47 Thus, the mechanism of Cys-tRNA(Cys) formation in M. jannaschii still remains to be

48 amination of the evolutionary history of Cys-tRNA(Cys) formation.

49 the "missing" CysRS activity for in vivo Cys-tRNA(Cys) formation.

50 ed the dominance of vertical inheritance for tRNA(Cys) from a single common ancestor.

51 dihydrouridine stemloop of Escherichia coli tRNA(Cys) has been shown to stably bind to the tRNA.

52 an alternate pathway for indirectly charging tRNA(Cys) has stimulated a re-examination of the evoluti

53 tor stem, the two hotspots for tRNA(Pro) and tRNA(Cys) identity determinants.

54 Thus, tRNA(Cys) identity is an ancient RNA record that depicts

55 Introduction of tRNA(Cys) identity nucleotides at the acceptor and antic

56 for Cys-tRNAPro and avoid deacylation of Cys-tRNACys in the cell.

57 A number of archaeal organisms generate Cys-tRNA(Cys) in a two-step pathway, first charging phosphos

58 the enzyme involved in the synthesis of Cys-tRNA(Cys) in M. jannaschii.

59 Synthesis of cysteinyl-tRNA(Cys) in methanogenic archaea proceeds by a two-step

60 converts phosphoseryl-tRNA(Cys) to cysteinyl-tRNA(Cys) in nearly all methanogens.

61 ty elements of Methanocaldococcus jannaschii tRNA(Cys) in the aminoacylation reaction for the two Met

62 erine (Sep) to form cysteinyl-tRNA(Cys) (Cys-tRNA(Cys)) in methanogens that lack the canonical cystei

63 not efficiently recognize the yeast or human tRNACys, indicating the evolution of determinants for tR

64 tructural dynamics of tRNA and the EF-Tu.Cys-tRNA(Cys) interface.

65 Previous studies show that dissection of tRNA(Cys) into acceptor and anticodon helices seriously

66 Introduction of the nucleotide U73 of tRNA(Cys) into tRNA(Val) was found to confer the flexibi

67 This indicates that Cys-tRNACys is formed by direct acylation in these organisms

68 Therefore, it is not clear if Cys-tRNACys is formed by direct aminoacylation or by a trans

69 that the stronger affinity of the 10-mer to tRNA(Cys) is due to a significantly slower rate of disso

70 haea proceeds by a two-step pathway in which tRNA(Cys) is first aminoacylated with phosphoserine by p

71 The core of Escherichia coli tRNA(Cys) is important for aminoacylation of the tRNA by

72 The core region of Escherichia coli tRNA(Cys)is important for aminoacylation of the tRNA.

73 indirect route, phosphoseryl-tRNA(Cys) (Sep-tRNA(Cys)) is first synthesized by phosphoseryl-tRNA syn

74 reveals that each enzyme prefers a distinct tRNA(Cys) isoacceptor or pair of isoacceptors.

75 ome of M. mazei also features three distinct tRNA(Cys) isoacceptors, further indicating the unusual a

76 Depletion of the pool of tRNA(Cys) led to ribosome stalling at Cys codons within

77 e that changes to the secondary structure of tRNACys may destroy function of the origin for light-str

78 templates containing the 14S rRNA, COX2, and tRNAcys mitochondrial promoters.

79 haea synthesize the cysteinyl-tRNA(Cys) (Cys-tRNA(Cys)) needed for protein synthesis using both a can

80 promoter, and C192F cannot transcribe either tRNA(Cys) or the variant COX2 promoter from linear DNA t

81 The tRNAcys promoter defect can be rescued by template super

82 Transcription of the tRNA(Cys) promoter by both mutants was significantly cor

83 Y54F is incapable of transcribing the weak tRNA(Cys) promoter, and C192F cannot transcribe either t

84 Studies with purified tRNAs indicate that tRNA(Cys) promotes cysteine activation.

85 RNA(Cys) to generate the essential cysteinyl-tRNA(Cys) required for protein synthesis.

86 ins of SepCysE each bind SepRS, SepCysS, and tRNA(Cys), respectively, which mediates the dynamic arch

87 In the indirect route, phosphoseryl-tRNA(Cys) (Sep-tRNA(Cys)) is first synthesized by phosph

88 lysis of archaeal, bacterial, and eukaryotic tRNA(Cys) sequences predicted additional SepRS-specific

89 airing at this position (G15-C48), while the tRNA(Cys) species from this organism instead features an

90 est that both metabolic routes and all three tRNA(Cys) species in M. mazei play important roles in th

91 ntly compared to that observed in the native tRNA(Cys) structure bound to EF-Tu, further implicating

92 th respect to each of the cysteine, ATP, and tRNA(Cys) substrates.

93 of the D loop in the tRNA core with that of tRNA(Cys) suppresses mis-charging with cysteine without

94 ions of the two-step indirect pathway of Cys-tRNA(Cys) synthesis (tRNA-dependent cysteine biosynthesi

95 at proS or MJ1477 gene products catalyze Cys-tRNA(Cys) synthesis in M. jannaschii.

96 cating the unusual and complex nature of Cys-tRNA(Cys) synthesis in this organism.

97 nihelices, truncated versions of full-length tRNA(Cys) that contain the acceptor stem, were also acce

98 The cys-tRNA(cys) that was synthesized and aminoacylated using t

99 sequence differences in the tertiary core of tRNA(Cys), the fused eukaryotic domain redirects the spe

100 Escherichia coli CysRS cannot acylate human tRNA(Cys), the fusion of a eukaryote-specific domain of

101 vely inactivated the sole transfer RNA(Cys) (tRNA(Cys)) through cleavage at a single site within the

102 y successively modifying the yeast and human tRNACys to ones that are efficiently aminoacylated by th

103 enzyme SepCysS, which converts phosphoseryl-tRNA(Cys) to cysteinyl-tRNA(Cys) in nearly all methanoge

104 S), which catalyze attachment of cysteine to tRNA(Cys) to generate the essential cysteinyl-tRNA(Cys)

105 coli CysRS from the A37 present in bacterial tRNA(Cys) to the G37 in mammals.

106 ze the synthesis of cysteinyl-tRNA(Cys) (Cys-tRNA(Cys)) to make up for the absence of the canonical c

107 The cys-tRNA(cys) was further modified with biotin (N-iodoacetyl

108 ere Escherichia coli cysteine-specific tRNA (tRNA(cys)) was transcribed and aminoacylated in a single

109 ther the conserved elements in H. influenzae tRNA(Cys)were also important for aminoacylation of H. in

110 ample is the core region of Escherichia coli tRNA(Cys), which has been shown by biochemical studies t

111 SepRS specifically forms Sep-tRNA(Cys), which is then converted to Cys-tRNA(Cys) by S

112 thermoautotrophicum SerRS did not mischarge tRNACys with serine.

113 o aminoacylate purified mature M. jannaschii tRNA(Cys) with cysteine in contrast to facile aminoacyla

114 etase (CARS) encodes the enzyme that charges tRNA(Cys) with cysteine in the cytoplasm.

115 synthetase also recognizes and aminoacylates tRNA(Cys) with cysteine.

116 n binding free energies upon misacylation of tRNA(Cys) with d-cysteine or O-phosphoserine and upon ch

117 These methanogens charge tRNA(Cys) with l-phosphoserine, which is also an interme

118 hway, O-phosphoseryl-tRNA synthetase charges tRNA(Cys) with O-phosphoserine (Sep), a precursor of the

119 eryl-tRNA synthetase (SepRS), which acylates tRNA(Cys) with phosphoserine (Sep), and the well known c

120 capacity to aminoacylate both tRNA(Pro) and tRNA(Cys) with their cognate amino acids.

121 iary interactions involving 9, 21, and 59 in tRNA(Cys) with those in tRNA(Gln) did not construct a fu