Aminoacyl-tRNA synthetases

Current Opinion in Structural Biology

Volumn 7, Issue 6, 1997, Pages 881-889

  Cusack, Stephen ^a  

^a EUROPEAN MOLECULAR BIOLOGY LABORATORY   (France)

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATE; AMINO ACID; AMINO ACID TRANSFER RNA LIGASE; AMINOACYL TRANSFER RNA; HISTIDINE; HISTIDINE TRANSFER RNA LIGASE; PHENYLALANINE TRANSFER RNA LIGASE; SERINE TRANSFER RNA LIGASE; TRANSFER RNA;

AMINOACYLATION; CRYSTAL STRUCTURE; DATA BASE; ENZYME ACTIVITY; ENZYME STRUCTURE; ENZYME SUBSTRATE COMPLEX; MOLECULAR RECOGNITION; PRIORITY JOURNAL; PROTEIN RNA BINDING; REVIEW;

EID: 0031456444     PISSN: 0959440X     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0959-440X(97)80161-3     Document Type: Article

References (34)

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12. Åberg A, Yaremchuk A, Tukulo iv1, Rasmussen B, Cusack S. Crystal structure analysis of activation of histidine by T. thermophilus histidyl-tRNA synthetase. of outstanding interest Biochemistry. 36:1997;3084-3094 The crystal structure of T. thermophilus HisRS complexed with histidine at 2.7Å resolution reveals for the first time the fold of the insertion domain, disordered in the E. coli HisRS structure. Soaking the binary complex crystals with ATP results in the activation reaction occurring in situ and the structure of the histidyl-adenylate complex to be determined.
13. ser and a seryl-adenylate analogue reveals a conformational switch in the active site. of outstanding interest EMBO J. 15:1996;2834-2842 The presence of the seryl-adenylate analogue improves the order of the enzyme active site and allows the visualisation of how the motif 2 loop interacts within the major groove of the tRNA acceptor stem down to the fifth base pair. In the active site without tRNA (there is only one tRNA bound to the synthetase dimer), the motif 2 loop adopts an alternative conformation which is also found in the presence of ATP. The motif 2 loop thus switches conformation during the aminoacylation reaction.
14. Airas KR. Differences in the magnesium dependences of the class I and class II aminoacyl-tRNA synthetases from E. coli. of special interest Eur J Biochem. 240:1996;223-231 The magnesium dependence of the ATP/PPi exchange and aminoacylation reaction of three class I and three class II E. coli aminoacyl-tRNA synthetases are measured and the data analysed using curve fitting of rate equations. The conclusion is that the magnesium dependence of class I and class II synthetases is distinct, one magnesium being required for class I and three for the class II enzymes.
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16. 2U or C can be accommodated. The specific recognition of the other anticodon bases, U-35 and U-36, which are both major identity elements in the lysine system, is also described. Additional crystallographic data on a ternary complex with a lysyl-adenylate analogue shows that binding of the intermediate induces significant conformational changes in the active site of the enzyme.
17. ile. This paper shows that a particular insertion domain (connecting peptide 1) in each enzyme is responsible for this specific activity.
18. Saks ME, Sampson JR, Abelson JN. The transfer RNA identity problem: a search for rules. Science. 263:1994;191-197.
19. Cusack S, Yaremchuk A, Tukalo M. tRNA recognition by aminoacyl-tRNA synthetases. Eggleston DS. The Many Faces of RNA. 1997;55-64 Academic Press, London.
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22. Asp recognition by its class II aminoacyl-tRNA synthetase. Nature. 362:1993;181-184.
23. ser. Science. 263:1994;1404-1410.
24. Borel F, Vincent C, Leberman R, Härtlein M. Seryl-tRNA synthetase from E. coli: implication of its N-terminal domain in aminoacylation activity and specificity. Nucleic Acids Res. 22:1994;2963-2969.
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26. ser by its characteristic tertiary structure. J Mol Biol. 236:1994;738-748.
27. ser is analysed by the systematic mutation of each base pair in the acceptor stem. The major recognition elements are located in the range of base-pairs 2-71 and 4-69 in agreement with the results of crystal structure analysis [13]. In particular, a preference for a purine-pyrimidine base pair at position 4-69 correlated with the observed contact between the ring of Phe262 of the motif 2 loop and the hydrophobic edge (C5-C6 positions) of Cy169.
28. Mosyak L, Reshetnikova L, Goldgur Y, Delarue M, Safro MG. Structure of phenylalanyl-tRNA synthetase from T. thermophilus. Nat Struct Biol. 2:1995;537-547.
29. 2 subunit structure that is a functional dimer and binds two tRNAs. One tRNA contact all four subunits. The binding of tRNA orders the N-terminal domain of the α subunit which appears as a long coiled coil, similar to that found in seryl-tRNA synthetase. Anticodon recognition is performed by the U1A-like RNP domain at the C-terminal end of the β subunit.
30. Sanni A, Walter P, Boulanger Y, Ebel J-P, Fasiolo F. Evolution of aminoacyl-tRNA synthetase quarternary structure and activity: S. cerevisiae mitochondrial phenylalanyl-tRNA synthetase. Proc Natl Acad Sci USA. 88:1991;8387-8391.
31. phe recognition nucleotides and initial aminoacylation site. Biochemistry. 35:1996;117-123.
32. gln(asn). More surprisingly, there is no obvious candidate for cysteinyl-tRNA synthetase and the seryl-tRNA synthetase is barely recognisable as such, being much less well-conserved than any other know seryl-tRNA synthetase sequence. There is one class II synthetase of unknown specificity but resembling phenylalanyl-tRNA synthetase. Most strikingly, inital searches could not identify a lysyl-tRNA synthetase (See also [33]).
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34. Kraulis PJ. MOLSCRIPT: a program to produce both detailed and schematic plots and protein structure. J Appl Crystallogr. 24:1991;946-950.