ライフサイエンスコーパス: cysteinyl-tRNA

1 Cysteinyl-tRNA (Cys-tRNA) is essential for protein synth

2 rately forms both prolyl-tRNA (Pro-tRNA) and cysteinyl-tRNA (Cys-tRNA) suitable for in vivo translati

3 of tRNA-bound O-phosphoserine (Sep) to form cysteinyl-tRNA(Cys) (Cys-tRNA(Cys)) in methanogens that

4 ubset of methanogenic archaea synthesize the cysteinyl-tRNA(Cys) (Cys-tRNA(Cys)) needed for protein s

5 y reported to also catalyze the synthesis of cysteinyl-tRNA(Cys) (Cys-tRNA(Cys)) to make up for the a

6 f prolyl-tRNA synthetase can synthesize both cysteinyl-tRNA(Cys) and prolyl-tRNA(Pro).

7 Synthesis of cysteinyl-tRNA(Cys) by cysteine-tRNA synthetase is requi

8 ggests a direct pathway for the synthesis of cysteinyl-tRNA(Cys) during protein synthesis.

9 Synthesis of cysteinyl-tRNA(Cys) in methanogenic archaea proceeds by

10 sS, which converts phosphoseryl-tRNA(Cys) to cysteinyl-tRNA(Cys) in nearly all methanogens.

11 teine to tRNA(Cys) to generate the essential cysteinyl-tRNA(Cys) required for protein synthesis.

12 r RNA factors to facilitate the synthesis of cysteinyl-tRNA(Cys).

13 ave been characterized, and the mechanism of cysteinyl-tRNA formation in Methanococcus jannaschii and

14 tion, the absence of a recognizable gene for cysteinyl tRNA synthetase in the genomes of Archae such

15 Escherichia coli cysteinyl-tRNA synthetase (CysRS) achieves a high level

16 Escherichia coli cysteinyl-tRNA synthetase (CysRS) achieves high amino ac

17 for protein synthesis using both a canonical cysteinyl-tRNA synthetase (CysRS) as well as a set of tw

18 Human cysteinyl-tRNA synthetase (CysRS) does not associate wit

19 nd were used to identify a putative class II cysteinyl-tRNA synthetase (CysRS) in several archaea tha

20 ment of cysteine to tRNA(Cys) by the class I cysteinyl-tRNA synthetase (CysRS) is flexible; the enzym

21 Cysteinyl-tRNA synthetase (CysRS) is highly specific for

22 t aminoacylation of tRNA by Escherichia coli cysteinyl-tRNA synthetase (CysRS) requires both domains,

23 that possess a canonical single-specificity cysteinyl-tRNA synthetase (CysRS), raising the question

24 for protein synthesis, through the action of cysteinyl-tRNA synthetase (CysRS).

25 Cys)) in methanogens that lack the canonical cysteinyl-tRNA synthetase (CysRS).

26 responsible for the formation of Cys-tRNA is cysteinyl-tRNA synthetase (CysRS).

27 n open reading frame (ORF) for the canonical cysteinyl-tRNA synthetase (CysRS).

28 synthetase (proS [mhp397]) (P = 0.009), and cysteinyl-tRNA synthetase (cysS [mhp661]) (P < 0.001) we

29 ynthetases SepRS (forming Sep-tRNA(Cys)) and cysteinyl-tRNA synthetase (forming Cys-tRNA(Cys)).

30 To date this dual-specificity prolyl-cysteinyl-tRNA synthetase (ProCysRS) is only known to ex

31 nnaschii possesses the unusual enzyme prolyl-cysteinyl-tRNA synthetase (ProCysRS), a single enzyme th

32 s are synthesized with comparable rates, the cysteinyl-tRNA synthetase activity being only 4.5-fold l

33 However, a single cysteinyl-tRNA synthetase activity was detected and puri

34 on factor 2, cell division protein FtsZ, and cysteinyl-tRNA synthetase as immunoreactive proteins.

35 Here we describe a different cysteinyl-tRNA synthetase from M. jannaschii and Deinoco

36 he cysS2 gene was thought to encode a second cysteinyl-tRNA synthetase in addition to cysS but the pr

37 to make up for the absence of the canonical cysteinyl-tRNA synthetase in this organism.

38 Cysteinyl-tRNA synthetase is an essential enzyme require

39 association was also identified at the CARS (cysteinyl-tRNA synthetase) locus (OR = 1.36, P = 3.1 x 1

40 ions to the transit peptides of histidyl- or cysteinyl-tRNA synthetase, which are dual-targeted to ch

41 with phosphoserine (Sep), and the well known cysteinyl-tRNA synthetase, which charges the same tRNA w

42 tertiary fold of MshC is similar to that of cysteinyl-tRNA synthetase, with a Rossmann fold catalyti

43 A with cysteine by Methanococcus maripaludis cysteinyl-tRNA synthetase.

44 ction catalyzed by prokaryotic and mammalian cysteinyl-tRNA synthetases (CARSs).

45 that is unique to several halophile archaeal cysteinyl-tRNA synthetases (CysRS), which catalyze attac

46 uggests similarities and differences between cysteinyl-tRNA synthetases and MshC in recognition of th

47 hat, although the Escherichia coli and human cysteinyl-tRNA synthetases both recognize the same bases

48 d evaluated as substrates for glutaminyl and cysteinyl-tRNA synthetases.