The tRNA-Interacting Factor p43 Associates with Mammalian Arginyl-tRNA Synthetase but Does Not Modify Its tRNA Aminoacylation Properties

Biochemistry

Volumn 43, Issue 15, 2004, Pages 4592-4600

  Guigou, Ludovic ^a   Shalak, Vyacheslav ^a   Mirande, Marc ^a  

^a CNRS   (France)

Author keywords

[No Author keywords available]

Indexed keywords

ACYLATION; AMINO ACIDS; ENZYME KINETICS; ENZYMES; POLYPEPTIDES; REACTION KINETICS; YEAST;

AMINO ACID ACTIVATION; AMINOACYLATION REACTIONS; EUKARYOTES; MULTIENZYME COMPLEXES;

RNA;

ARGININE; ARGININE TRANSFER RNA LIGASE; MULTIENZYME COMPLEX; POLYPEPTIDE; PROTEIN P43; TRANSFER RNA;

AMINO ACID SEQUENCE; AMINO TERMINAL SEQUENCE; AMINOACYLATION; ARTICLE; CARBOXY TERMINAL SEQUENCE; CATALYSIS; CATALYST; COMPLEX FORMATION; ENZYME ACTIVITY; ENZYME KINETICS; GEL; NONHUMAN; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN FUNCTION; PROTEIN PROTEIN INTERACTION; RNA BINDING; RNA TRANSLATION;

ACYLATION; ANIMALS; ARGININE-TRNA LIGASE; BASE SEQUENCE; CATALYSIS; CRICETINAE; CYTOKINES; MOLECULAR SEQUENCE DATA; NEOPLASM PROTEINS; NUCLEIC ACID CONFORMATION; PROTEIN BINDING; PROTEIN PROCESSING, POST-TRANSLATIONAL; PROTEIN SUBUNITS; RNA, TRANSFER, ARG; RNA-BINDING PROTEINS; SACCHAROMYCES CEREVISIAE PROTEINS; SEQUENCE DELETION; TRANSFER RNA AMINOACYLATION;

EUKARYOTA; MAMMALIA;

EID: 13444282697     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi036150e     Document Type: Article

References (45)

1. Ibba, M., and Söll, D. (2000) Aminoacyl-tRNA synthesis, Annu. Rev. Biochem. 69, 617-650.
2. Gln and ATP at 2.8 Å resolution, Science 246, 1135-1142.
3. Asp, Science 252, 1682-1689.
4. Lys transcript: Anticodon recognition and conformational changes upon binding of a lysyl-adenylate analogue, EMBO J. 15, 6321-6334.
5. Thr complex enlightens its repressor activity and reveals an essential zinc ion in the active site, Cell 97, 371-381.
6. Pro(CGG), EMBO J. 19, 4745-4758.
7. Sekine, S., Nureki, O., Shimada, A., Vassylyev, D. G., and Yokoyama, S. (2001) Structural basis for anticodon recognition by discriminating glutamyl-tRNA synthetase, Nat. Struct. Biol. 8, 203-206.
8. Berthonneau, E., and Mirande, M. (2000) A gene fusion event in the evolution of aminoacyl-tRNA synthetases, FEBS Lett. 470, 300-304.
9. Cahuzac, B., Berthonneau, E., Birlirakis, N., Guittet, E., and Mirande, M. (2000) A recurrent RNA-binding domain is appended to eukaryotic aminoacyl-tRNA synthetases, EMBO J. 19, 445-452.
10. Jeong, E. J., Hwang, G. S., Kim, K. H., Kim, M. J., Kim, S., and Kim, K. S. (2000) Structural analysis of multifunctional peptide motifs in human bifunctional tRNA synthetase: Identification of RNA-binding residues and functional implications for tandem repeats, Biochemistry 39, 15775-15782.
11. Kaminska, M., Shalak, V., and Mirande, M. (2001) The appended C-domain of human methionyl-tRNA synthetase has a tRNA-sequestering function, Biochemistry 40, 14309-14316.
12. Raben, N., Nichols, R., Dohlman, J., McPhie, P., Sridhar, V., Hyde, C., Leff, R., and Plotz, P. (1994) A motif in human histidyl-tRNA synthetase which is shared among several aminoacyl-tRNA synthetases is a coiled-coil that is essential for enzymatic activity and contains the major autoantigenic epitope, J. Biol. Chem. 269, 24277-24283.
13. Wu, H., Nada, S., and Dignam, J. D. (1995) Analysis of truncated forms of Bombyx mori glycyl-tRNA synthetase: function of an N-terminal structure in RNA binding, Biochemistry 34, 16327-16336.
14. Francin, M., Kaminska, M., Kerjan, P., and Mirande, M. (2002) The N-terminal domain of mammalian lysyl-tRNA synthetase is a functional tRNA-binding domain, J. Biol. Chem. 277, 1762-1769.
15. Reed, V. S., Wastney, M. E., and Yang, D. C. H. (1994) Mechanisms of the transfer of aminoacyl-tRNA from aminoacyl-tRNA synthetase to the elongation factor 1α, J. Biol. Chem. 269, 32932-32936.
16. Reed, V. S., and Yang, D. C. H. (1994) Characterization of a novel N-terminal peptide in human aspartyl-tRNA synthetase - Roles in the transfer of aminoacyl-tRNA from aminoacyl-tRNA synthetase to the elongation factor 1α, J. Biol. Chem. 269, 32937-32941.
17. Hammamieh, R., and Yang, D. C. H. (2001) Magnesium ion-mediated binding to tRNA by an amino-terminal peptide of a class II tRNA synthetase, J. Biol. Chem. 276, 428-433.
18. Francin, M., and Mirande, M. (2003) Functional dissection of the eukaryotic-specific tRNA-interacting factor of lysyl-tRNA synthetase, J. Biol. Chem. 278, 1472-1479.
19. Negrutskii, B. S., and Deutscher, M. P. (1991) Channeling of aminoacyl-tRNA for protein synthesis in vivo, Proc. Natl. Acad. Sci. U.S.A. 88, 4991-4995.
20. Simos, G., Segref, A., Fasiolo, F., Hellmuth, K., Shevchenko, A., Mann, M., and Hurt, E. C. (1996) The yeast protein Arc1p binds to tRNA and functions as a cofactor for the methionyl- and glutamyl-tRNA synthetases, EMBO J. 15, 5437-5448.
21. Simos, G., Sauer, A., Fasiolo, F., and Hurt, E. C. (1998) A conserved domain within Arc1p delivers tRNA to aminoacyl-tRNA synthetases, Mol. Cell 1, 235-242.
22. Deinert, K., Fasiolo, F., Hurt, E. C., and Simos, G. (2001) Arc1p organizes the yeast aminoacyl-tRNA synthetase complex and stabilizes its interaction with the cognate tRNAs, J. Biol. Chem. 276, 6000-6008.
23. Shalak, V., Kaminska, M., Mitnacht-Kraus, R., Vandenabeele, P., Clauss, M., and Mirande, M. (2001) The EMAPII cytokine is released from the mammalian multisynthetase complex after cleavage of its p43/proEMAPII component, J. Biol. Chem. 276, 23769-23776.
24. Kleeman, T. A., Wei, D. B., Simpson, K. L., and First, E. A. (1997) Human tyrosyl tRNA synthetase shares amino acid sequence homology with a putative cytokine, J. Biol. Chem. 272, 14420-14425.
25. Wakasugi, K., and Schimmel, P. (1999) Two distinct cytokines released from a human aminoacyl-tRNA synthetase, Science 284, 147-151.
26. Renault, L., Kerjan, P., Pasqualato, S., Menetrey, J., Robinson, J. C., Kawaguchi, S., Vassylyev, D. G., Yokoyama, S., Mirande, M., and Cherfils, J. (2001) Structure of the EMAPII domain of human aminoacyl-tRNA synthetase complex reveals evolutionary dimer mimicry, EMBO J. 20, 570-578.
27. Kao, J., Ryan, J., Brett, G., Chen, J., Shen, H., Fan, Y. G., Godman, G., Familletti, P. C., Wang, F., Pan, Y. C., Stern, D., and Clauss, M. (1992) Endothelial monocyte-activating polypeptide II. A novel tumor-derived polypeptide that activates host-response mechanisms, J. Biol. Chem. 267, 20239-20247.
28. Quevillon, S., Agou, F., Robinson, J. C., and Mirande, M. (1997) The p43 component of the mammalian multi-synthetase complex is likely to be the precursor of the endothelial monocyte-activating polypeptide II cytokine, J. Biol. Chem. 272, 32573-32579.
29. Knies, U. E., Behrensdorf, H. A., Mitchell, C. A., Deutsch, U., Risau, W., Drexler, H. C., and Clauss, M. (1998) Regulation of endothelial monocyte-activating polypeptide II release by apoptosis, Proc. Natl. Acad. Sci. U.S.A. 95, 12322-12327.
30. Ko, Y. G., Park, H., Kim, T., Lee, J. W., Park, S. G., Seol, W., Kim, J. E., Lee, W. H., Kim, S. H., Park, J. E., and Kim, S. (2001) A cofactor of tRNA synthetase, p43, is secreted to up-regulate proinflammatory genes, J. Biol. Chem. 276, 23028-23033.
31. Park, S. G., Kang, Y. S., Ahn, Y. H., Lee, S. H., Kim, K. R., Kim, K. W., Koh, G. Y., Ko, Y. G., and Kim, S. (2002) Dose-dependent biphasic activity of tRNA synthetase-associating factor, p43, in angiogenesis, J. Biol. Chem. 277, 45243-45248.
32. Norcum, M. T., and Warrington, J. A. (2000) The cytokine portion of p43 occupies a central position within the eukaryotic multi-synthetase complex, J. Biol. Chem. 275, 17921-17924.
33. Quevillon, S., Robinson, J. C., Berthonneau, E., Siatecka, M., and Mirande, M. (1999) Macromolecular assemblage of aminoacyl-tRNA synthetases: Identification of protein-protein interactions and characterization of a core protein, J. Mol. Biol. 285, 183-195.
34. Robinson, J. C., Kerjan, P., and Mirande, M. (2000) Macromolecular assemblage of aminoacyl-tRNA synthetases: Quantitative analysis of protein-protein interactions and mechanism of complex assembly, J. Mol. Biol. 304, 983-994.
35. Park, S. G., Jung, K. H., Lee, J. S., Jo, Y. J., Motegi, H., Kim, S., and Shiba, K. (1999) Precursor of pro-apoptotic cytokine modulates aminoacylation activity of tRNA synthetase, J. Biol. Chem. 274, 16673-16676.
36. Lazard, M., Kerjan, P., Agou, F., and Mirande, M. (2000) The tRNA-dependent activation of arginine by arginyl-tRNA synthetase requires inter-domain communication, J. Mol. Biol. 302, 991-1004.
37. Morales, A. J., Swairjo, M. A., and Schimmel, P. (1999) Structure-specific tRNA-binding protein from the extreme thermophile Aquifex aeolicus, EMBO J. 18, 3475-3483.
38. Mirande, M., Cirakoglu, B., and Waller, J. P. (1983) Seven mammalian aminoacyl-tRNA synthetases associated within the same complex are functionally independent, Eur. J. Biochem. 131, 163-170.
39. Rho, S. B., Kim, M. J., Lee, J. S., Seol, W. G., Motegi, H., Kim, S., and Shiba, K. (1999) Genetic dissection of protein-protein interactions in multi-tRNA synthetase complex, Proc. Natl. Acad. Sci. U.S.A. 96, 4488-4493.
40. Cirakoglu, B., and Waller, J. P. (1985) Multiple forms of arginyl- and lysyl-tRNA synthetases in rat liver: a reevaluation, Biochim. Biophys. Acta 829, 173-179.
41. Sivaram, P., and Deutscher, M. P. (1990) Existence of two forms of rat liver arginyl-tRNA synthetase suggests channeling of aminoacyl-tRNA for protein synthesis, Proc. Natl. Acad. Sci. U.S.A. 87, 3665-3669.
42. Kaminska, M., Deniziak, M., Kerjan, P., Barciszewski, J., and Mirande, M. (2000) A recurrent general RNA binding domain appended to plant methionyl-tRNA synthetase acts as a cis-acting cofactor for aminoacylation, EMBO J. 19, 6908-6917.
43. Nomanbhoy, T., Morales, A. J., Abraham, A. T., Vortler, C. S., Giegé, R., and Schimmel, P. (2001) Simultaneous binding of two proteins to opposite sides of a single transfer RNA, Nat. Struct. Biol. 8, 344-348.
44. Delagoutte, B., Moras, D., and Cavarelli, J. (2000) tRNA aminoacylation by arginyl-tRNA synthetase: induced conformations during substrates binding, EMBO J. 19, 5599-5610.
45. Swairjo, M. A., Morales, A. J., Wang, C. C., Ortiz, A. R., and Schimmel, P. (2000) Crystal structure of Trbp111: a structure-specific tRNA-binding protein, EMBO J. 19, 6287-6298.