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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
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
17 for protein synthesis using both a canonical cysteinyl-tRNA synthetase (CysRS) as well as a set of tw
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
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
28 synthetase (proS [mhp397]) (P = 0.009), and cysteinyl-tRNA synthetase (cysS [mhp661]) (P < 0.001) we
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
34 on factor 2, cell division protein FtsZ, and cysteinyl-tRNA synthetase as immunoreactive proteins.
36 he cysS2 gene was thought to encode a second cysteinyl-tRNA synthetase in addition to cysS but the pr
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
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
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