Crystallization of the seryl-tRNA synthetase-tRNASer complex from Thermus thermophilus

Yaremchuk, A.; Tukalo, M. A.; Krikliviy, I. A.; Mel'nik, V.N.; Berthet-Colominas, C.; Cusack, Stephen; Leberman, Reuben

doi:10.1016/0022-2836(92)91014-g

Cited by 10 publications

(4 citation statements)

References 22 publications

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“…The choice of a thermophilic organism was also determined by the ability of its proteins to crystallize readily (GiegC et al, 1994) and to be easily purified when expressed in E. coli. Indeed, several thermophilic synthetases have been crystallized in free form or complexed with their ligands during the past years: Asp-tRNA synthetase (Poterszman et al, 1993), Glu-tRNA synthetase (Nureki et al, 1992(Nureki et al, , 1995, His-tRNA sythetase (Yaremchuk et al, 1995a), Lys-tRNA synthetase (Yaremchuk et al, 1995b), MettRNA synthetase (Nureki et al, 1991), Phe-tRNA synthetase (Keller et al, 1992;Kreutzer et al, 1992;Reshetnikova et al, 1992: Mosyak et al, 1995, Ser-tRNA synthetase (Yaremchuk et al, 1992) and Thr-tRNA synthetase (Zheltonosova et al, 1994).…”

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confidence: 99%

An Example of Non‐Conservation of Oligomeric Structure in Prokaryotic Aminoacyl‐tRNA Synthetases

Mazauric

Reinbolt

Lorber

et al. 1996

European Journal of Biochemistry

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Glycyl-tRNA synthetase (Gly-tRNA synthetase) from Thermus thermoplzilus was purified to homogeneity and with high yield using a five-step purification procedure in amounts sufficient to solve its crystallographic structure [Logan, D. Heat-stability measurements show that this synthetase keeps its ATP-PP, exchange and aminoacylation activities up to 70°C. Glycyladenylate strongly protects the enzyme against thermal inactivation at higher temperatures. Unexpectedly, tRNACly does not induce protection.Cross-aminoacylations reveal that the thermophilic Gly-tRNA synthetase charges heterologous E. coli tRNA"l~'G'C'~ and tRNA"lscCCC) and yeast tRNAG1y("C"' as efficiently as 7: thermophilus tRNA"IY. All these aminoacylation reactions are characterized by similar activation energies as deduced from Arrhenius plots. Therefore, contrary to the E. coli and H. sapiens Gly-tRNA synthetases, the prokaryotic thermophilic enzyme does not possess a strict species specificity.The results are discussed in the context of the three-dimensional structure of the synthetase and in the view of the particular evolution of the glycinylation systems.

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confidence: 99%

An Example of Non‐Conservation of Oligomeric Structure in Prokaryotic Aminoacyl‐tRNA Synthetases

Mazauric

Reinbolt

Lorber

et al. 1996

European Journal of Biochemistry

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“…In order to study the structure of tRNA Ser and the molecular basis of its recognition by the synthetase, we have obtained four crystal forms of the complex between SerRS and its cognate tRNA from the T. thermophilus [28,29]. Of these, two (denoted by Form III and Form IV) have tetragonal crystal forms and both diffract to about 6 C resolution [28]. Form III crystals diffract to about 3.5 C and contain two synthetase dimmers with two tRNA molecules each.…”

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confidence: 99%

“…Form III crystals diffract to about 3.5 C and contain two synthetase dimmers with two tRNA molecules each. On the other hand, Form IV crystals, which diffract to 2.8 C resolution, contain only one tRNA molecule bound to the synthetase dimer [28]. Using Form IV crystals the structure of T. thermophilus SerRS complexed with tRNA Ser molecule was solved at 2.9 C resolution [18].…”

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confidence: 99%

Recognition of tRNAs with a long variable arm by aminoacyl-tRNA synthetases

et al. 2013

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In prokaryotic cells three tRNA species, tRNASer, tRNALeu and tRNATyr, possess a long variable arm of 11–20 nucleotides (type 2 tRNA) rather than usual 4 or 5 nucleotides (type 1 tRNA). In this review we have summarized the results of our research on the structural basis for recognition and discrimination of type 2 tRNAs by Thermus thermophilus seryl-, tyrosyl- and leucyl-tRNA synthetases (SerRS, TyrRS and LeuRS) obtained by X-ray crystallography and chemical probing tRNA in solution. Crystal structures are now known of all three aminoacyl-tRNA synthetases complexed with type 2 tRNAs and the different modes of tRNA recognition represented by these structures will be discussed. In particular, emphasis will be given to the results on recognition of characteristic shape of type 2 tRNAs by cognate synthetases. In tRNASer, tRNATyr and tRNALeu the orientation of the long variable arm with respect to the body of the tRNA is different and is controlled by different packing of the core. In the case of SerRS the N-terminal domain and in the case of TyrRS, the C-terminal domain, bind to the characteristic long variable arm of the cognate RNA, thus recognizing the unique shape of the tRNA. The core of T. thermophilus tRNALeu has several layers of unusual base-pairs, which are revealed by the crystal structure of tRNALeu complexed with T. thermophilus LeuRS and by probing a ligand-free tRNA by specific chemical reagents in solution. In the crystal structure of the LeuRS-tRNALeu complex the unique D-stem structure is recognized by the C-terminal domain of LeuRS and these data are in good agreement with those obtained in solution. LeuRS has canonical class I mode of tRNA recognition, approaching the tRNA acceptor stem from the D-stem and minor groove of the acceptor stem side. SerRS also has canonical class II mode of tRNA recognition and approaches tRNASer from opposite, variable stem and major groove of acceptor stem site. And finally, TyrRS in strong contrast to canonical class I system has class II mode of tRNA recognition

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“…As proteínas e estruturas de RNA envolvidas na biossíntese, direcionamento e incorporação do aminoácido Selenocisteína na cadeia polipeptídica são: [19][20][21] , pois é incapaz diferenciar a região anticódon do tRNA reconhecendo apenas suas grandes regiões do braço variável (maiores de 10 nucleotídeos em comparação aos 4-5 encontrados nos demais tRNAs) 22,23 ; Selenocisteína Sintase (SELA ou SepSecS) -proteína homodecamérica (506 kDa) em eubactérias 24,25 , homodimérica (84 kDa) em arqueobactéria (putativa a de eubactéria) 25,26 e homotetramérica (220 kDa) em arqueobactérias e eucariotos 25 . É responsável pela conversão do resíduo Serina em Selenocisteína.…”

Section: Figura 1 3 -Sequências De Inserção Sec (Secis) Em A-secis unclassified

Determinação estrutural da proteína Selenocisteína Sintase de Escherichia coli

Cassago¹

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Crystallization of the seryl-tRNA synthetase-tRNASer complex from Thermus thermophilus

Cited by 10 publications

References 22 publications

An Example of Non‐Conservation of Oligomeric Structure in Prokaryotic Aminoacyl‐tRNA Synthetases

An Example of Non‐Conservation of Oligomeric Structure in Prokaryotic Aminoacyl‐tRNA Synthetases

Recognition of tRNAs with a long variable arm by aminoacyl-tRNA synthetases

Determinação estrutural da proteína Selenocisteína Sintase de Escherichia coli

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