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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

29 Cysteinyl-tRNA synthetase is an essential enzyme require

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

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

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

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

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

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

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