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1 ) and cysteinyl-tRNA synthetase (forming Cys-tRNA(Cys)).
2 by a transformation of serine misacylated to tRNACys.
3 rand replication, and secondary structure of tRNACys.
4 rm14, which generates m(2)G at position 6 in tRNA(Cys).
5 mportant for aminoacylation of H. influenzae tRNA(Cys).
6 o highly sensitive to the A37G transition in tRNA(Cys).
7 n the ability of the cysteine enzyme to bind tRNA(Cys).
8 replication partially overlaps the adjacent tRNA(Cys).
9 overcomes the cross-species barrier in human tRNA(Cys).
10 A(Cys) and subsequently converting it to Cys-tRNA(Cys).
11 iring alanine onto nonalanyl-tRNAs including tRNA(Cys).
12 rom a defect in kcat, rather than the Km for tRNA(Cys).
13 ment of proline to tRNA(Pro) and cysteine to tRNA(Cys).
14 ors to facilitate the synthesis of cysteinyl-tRNA(Cys).
15 n one other tRNA, the Haemophilus influenzae tRNA(Cys).
16 portant element in aminoacylation of E. coli tRNA(Cys), a better understanding of its structure in th
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
26 Methanocaldococcus jannaschii indicated that tRNA(Cys) becomes acylated with O-phosphoserine (Sep) bu
27 us enables a global long-range channeling of tRNA(Cys) between SepRS and SepCysS distant active sites
31 ylated intermediate is then converted to Cys-tRNA(Cys) by Sep-tRNA:Cys-tRNA synthase (SepCysS) via a
33 show here that the attachment of cysteine to tRNA(Cys) by the class I cysteinyl-tRNA synthetase (CysR
34 cs of the EF-Tu.guanosine 5'-triphosphate.aa-tRNA(Cys) complex and the roles played by Mg2+ ions and
35 ructures of Saccharomyces cerevisiae DMATase-tRNA(Cys) complex in four distinct forms, which provide
37 ious work has shown that CysRS aminoacylates tRNA(Cys) core regions containing G15-G48 with much bett
39 ound O-phosphoserine (Sep) to form cysteinyl-tRNA(Cys) (Cys-tRNA(Cys)) in methanogens that lack the c
40 ethanogenic archaea synthesize the cysteinyl-tRNA(Cys) (Cys-tRNA(Cys)) needed for protein synthesis u
41 to also catalyze the synthesis of cysteinyl-tRNA(Cys) (Cys-tRNA(Cys)) to make up for the absence of
43 on of a mismatching O-phosphoserine (Sep) to tRNA(Cys) followed by the conversion of tRNA-bounded Sep
44 nce of covalent continuity of both CysRS and tRNA(Cys) for efficient tRNA aminoacylation, and highlig
51 an alternate pathway for indirectly charging tRNA(Cys) has stimulated a re-examination of the evoluti
55 A number of archaeal organisms generate Cys-tRNA(Cys) in a two-step pathway, first charging phosphos
59 ty elements of Methanocaldococcus jannaschii tRNA(Cys) in the aminoacylation reaction for the two Met
60 erine (Sep) to form cysteinyl-tRNA(Cys) (Cys-tRNA(Cys)) in methanogens that lack the canonical cystei
61 not efficiently recognize the yeast or human tRNACys, indicating the evolution of determinants for tR
65 that the stronger affinity of the 10-mer to tRNA(Cys) is due to a significantly slower rate of disso
66 haea proceeds by a two-step pathway in which tRNA(Cys) is first aminoacylated with phosphoserine by p
70 indirect route, phosphoseryl-tRNA(Cys) (Sep-tRNA(Cys)) is first synthesized by phosphoseryl-tRNA syn
73 ome of M. mazei also features three distinct tRNA(Cys) isoacceptors, further indicating the unusual a
74 e that changes to the secondary structure of tRNACys may destroy function of the origin for light-str
76 haea synthesize the cysteinyl-tRNA(Cys) (Cys-tRNA(Cys)) needed for protein synthesis using both a can
77 promoter, and C192F cannot transcribe either tRNA(Cys) or the variant COX2 promoter from linear DNA t
79 Y54F is incapable of transcribing the weak tRNA(Cys) promoter, and C192F cannot transcribe either t
83 ins of SepCysE each bind SepRS, SepCysS, and tRNA(Cys), respectively, which mediates the dynamic arch
85 lysis of archaeal, bacterial, and eukaryotic tRNA(Cys) sequences predicted additional SepRS-specific
86 airing at this position (G15-C48), while the tRNA(Cys) species from this organism instead features an
87 est that both metabolic routes and all three tRNA(Cys) species in M. mazei play important roles in th
88 ntly compared to that observed in the native tRNA(Cys) structure bound to EF-Tu, further implicating
90 of the D loop in the tRNA core with that of tRNA(Cys) suppresses mis-charging with cysteine without
91 ions of the two-step indirect pathway of Cys-tRNA(Cys) synthesis (tRNA-dependent cysteine biosynthesi
95 sequence differences in the tertiary core of tRNA(Cys), the fused eukaryotic domain redirects the spe
96 Escherichia coli CysRS cannot acylate human tRNA(Cys), the fusion of a eukaryote-specific domain of
97 enzyme SepCysS, which converts phosphoseryl-tRNA(Cys) to cysteinyl-tRNA(Cys) in nearly all methanoge
98 S), which catalyze attachment of cysteine to tRNA(Cys) to generate the essential cysteinyl-tRNA(Cys)
100 y successively modifying the yeast and human tRNACys to ones that are efficiently aminoacylated by th
101 ze the synthesis of cysteinyl-tRNA(Cys) (Cys-tRNA(Cys)) to make up for the absence of the canonical c
103 ere Escherichia coli cysteine-specific tRNA (tRNA(cys)) was transcribed and aminoacylated in a single
104 ther the conserved elements in H. influenzae tRNA(Cys)were also important for aminoacylation of H. in
105 ample is the core region of Escherichia coli tRNA(Cys), which has been shown by biochemical studies t
107 o aminoacylate purified mature M. jannaschii tRNA(Cys) with cysteine in contrast to facile aminoacyla
109 n binding free energies upon misacylation of tRNA(Cys) with d-cysteine or O-phosphoserine and upon ch
111 hway, O-phosphoseryl-tRNA synthetase charges tRNA(Cys) with O-phosphoserine (Sep), a precursor of the
112 eryl-tRNA synthetase (SepRS), which acylates tRNA(Cys) with phosphoserine (Sep), and the well known c
114 iary interactions involving 9, 21, and 59 in tRNA(Cys) with those in tRNA(Gln) did not construct a fu
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