Incorporation of the Arc1p tRNA-Binding Domain to the Catalytic Core of MetRS Can Functionally Replace the Yeast Arc1p-MetRS Complex

Journal of Molecular Biology

Volumn 381, Issue 3, 2008, Pages 763-771

  Karanasios, Eleftherios ^a   Boleti, Haralabia ^b   Simos, George ^a,c  

^a UNIVERSITY OF THESSALY   (Greece)

^b HELLENIC PASTEUR INSTITUTE   (Greece)

^c INSTITUTE OF HUMAN PERFORMANCE AND REHABILITATION   (Greece)

Author keywords

ARC1; GluRS; MetRS; tRNA; yeast

Indexed keywords

CHIMERIC PROTEIN; METHIONINE TRANSFER RNA LIGASE; TRANSFER RNA;

AMINOACYLATION; ARTICLE; CARBOXY TERMINAL SEQUENCE; CELL GROWTH; CONTROLLED STUDY; CYTOPLASM; ENZYME ACTIVE SITE; ENZYME ACTIVITY; IN VITRO STUDY; NONHUMAN; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN PROTEIN INTERACTION; YEAST;

EID: 47849084543     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2008.06.044     Document Type: Article

References (39)

1. Ibba M., and Soll D. Aminoacyl-tRNA synthesis. Annu. Rev. Biochem. 69 (2000) 617-650
2. Kaminska M., Deniziak M., Kerjan P., Barciszewski J., and Mirande M. A recurrent general RNA binding domain appended to plant methionyl-tRNA synthetase acts as a cis-acting cofactor for aminoacylation. EMBO J. 19 (2000) 6908-6917
3. Frugier M., Moulinier L., and Giege R. A domain in the N-terminal extension of class IIb eukaryotic aminoacyl-tRNA synthetases is important for tRNA binding. EMBO J. 19 (2000) 2371-2380
4. Francin M., Kaminska M., Kerjan P., and Mirande M. The N-terminal domain of mammalian Lysyl-tRNA synthetase is a functional tRNA-binding domain. J. Biol. Chem. 277 (2002) 1762-1769
5. Bec G., Kerjan P., and Waller J.P. Reconstitution in vitro of the valyl-tRNA synthetase-elongation factor (EF) 1 beta gamma delta complex. Essential roles of the NH2-terminal extension of valyl-tRNA synthetase and of the EF-1 delta subunit in complex formation. J. Biol. Chem. 269 (1994) 2086-2092
6. Quevillon S., Robinson J.C., Berthonneau E., Siatecka M., and Mirande M. Macromolecular assemblage of aminoacyl-tRNA synthetases: identification of protein-protein interactions and characterization of a core protein. J. Mol. Biol. 285 (1999) 183-195
7. Ahn H.C., Kim S., and Lee B.J. Solution structure and p43 binding of the p38 leucine zipper motif: coiled-coil interactions mediate the association between p38 and p43. FEBS Lett. 542 (2003) 119-124
8. Nathanson L., and Deutscher M.P. Active aminoacyl-tRNA synthetases are present in nuclei as a high molecular weight multienzyme complex. J. Biol. Chem. 275 (2000) 31559-31562
9. Lund E., and Dahlberg J.E. Proofreading and aminoacylation of tRNAs before export from the nucleus. Science 282 (1998) 2082-2085
10. Simos G., Segref A., Fasiolo F., Hellmuth K., Shevchenko A., Mann M., and Hurt E.C. The yeast protein Arc1p binds to tRNA and functions as a cofactor for the methionyl- and glutamyl-tRNA synthetases. EMBO J. 15 (1996) 5437-5448
11. Hellmuth K., Lau D.M., Bischoff F.R., Kunzler M., Hurt E., and Simos G. Yeast Los1p has properties of an exportin-like nucleocytoplasmic transport factor for tRNA. Mol. Cell. Biol. 18 (1998) 6374-6386
12. Galani K., Grosshans H., Deinert K., Hurt E.C., and Simos G. The intracellular location of two aminoacyl-tRNA synthetases depends on complex formation with Arc1p. EMBO J. 20 (2001) 6889-6898
13. Simader H., Hothorn M., Kohler C., Basquin J., Simos G., and Suck D. Structural basis of yeast aminoacyl-tRNA synthetase complex formation revealed by crystal structures of two binary sub-complexes. Nucleic Acids Res. 34 (2006) 3968-3979
14. Karanasios E., Simader H., Panayotou G., Suck D., and Simos G. Molecular determinants of the yeast Arc1p-aminoacyl-tRNA synthetase complex assembly. J. Mol. Biol. 374 (2007) 1077-1090
15. Galani K., Hurt E., and Simos G. The tRNA aminoacylation co-factor Arc1p is excluded from the nucleus by an Xpo1p-dependent mechanism. FEBS Lett. 579 (2005) 969-975
16. Simos G., Sauer A., Fasiolo F., and Hurt E.C. A conserved domain within Arc1p delivers tRNA to aminoacyl-tRNA synthetases. Mol. Cell 1 (1998) 235-242
17. Deinert K., Fasiolo F., Hurt E.C., and Simos G. Arc1p organizes the yeast aminoacyl-tRNA synthetase complex and stabilizes its interaction with the cognate tRNAs. J. Biol. Chem. 276 (2001) 6000-6008
18. Graindorge J.S., Senger B., Tritch D., Simos G., and Fasiolo F. Role of Arc1p in the modulation of yeast glutamyl-tRNA synthetase activity. Biochemistry 44 (2005) 1344-1352
19. Morales A.J., Swairjo M.A., and Schimmel P. Structure-specific tRNA-binding protein from the extreme thermophile Aquifex aeolicus. EMBO J. 18 (1999) 3475-3483
20. Deniziak M., and Barciszewski J. Methiolyl-tRNA synthetase. Acta Biochim. Pol. 48 (2001) 337-350
21. Walter P., Weygand-Durasevic I., Sanni A., Ebel J.P., and Fasiolo F. Deletion analysis in the amino-terminal extension of methionyl-tRNA synthetase from Saccharomyces cerevisiae shows that a small region is important for the activity and stability of the enzyme. J. Biol. Chem. 264 (1989) 17126-17130
22. Chihade J.W., and Schimmel P. Assembly of a catalytic unit for RNA microhelix aminoacylation using nonspecific RNA binding domains. Proc. Natl Acad. Sci. USA 96 (1999) 12316-12321
23. Renault L., Kerjan P., Pasqualato S., Menetrey J., Robinson J.C., Kawaguchi S., et al. Structure of the EMAPII domain of human aminoacyl-tRNA synthetase complex reveals evolutionary dimer mimicry. EMBO J. 20 (2001) 570-578
24. Swairjo M.A., Morales A.J., Wang C.C., Ortiz A.R., and Schimmel P. Crystal structure of Trbp111: a structure-specific tRNA-binding protein. EMBO J. 19 (2000) 6287-6298
25. Nomanbhoy T., Morales A.J., Abraham A.T., Vortler C.S., Giege R., and Schimmel P. Simultaneous binding of two proteins to opposite sides of a single transfer RNA. Nat. Struct. Biol. 8 (2001) 344-348
26. Deniziak M., Sauter C., Becker H.D., Paulus C.A., Giege R., and Kern D. Deinococcus glutaminyl-tRNA synthetase is a chimer between proteins from an ancient and the modern pathways of aminoacyl-tRNA formation. Nucleic Acids Res. 35 (2007) 1421-1431
27. Bohnsack M.T., Regener K., Schwappach B., Saffrich R., Paraskeva E., Hartmann E., and Gorlich D. Exp5 exports eEF1A via tRNA from nuclei and synergizes with other transport pathways to confine translation to the cytoplasm. EMBO J. 21 (2002) 6205-6215
28. Calado A., Treichel N., Muller E.C., Otto A., and Kutay U. Exportin-5-mediated nuclear export of eukaryotic elongation factor 1A and tRNA. EMBO J. 21 (2002) 6216-6224
29. McGuire A.T., and Mangroo D. Cex1p is a novel cytoplasmic component of the Saccharomyces cerevisiae nuclear tRNA export machinery. EMBO J. 26 (2007) 288-300
30. Feng W., and Hopper A.K. A Los1p-independent pathway for nuclear export of intronless tRNAs in Saccharomyces cerevisiae. Proc. Natl Acad. Sci. USA 99 (2002) 5412-5417
31. Sarkar S., Azad A.K., and Hopper A.K. Nuclear tRNA aminoacylation and its role in nuclear export of endogenous tRNAs in Saccharomyces cerevisiae. Proc. Natl Acad. Sci. USA 96 (1999) 14366-14371
32. Grosshans H., Hurt E., and Simos G. An aminoacylation-dependent nuclear tRNA export pathway in yeast. Genes Dev. 14 (2000) 830-840
33. Simos G., Grosshans H., and Hurt E. Nuclear export of tRNA. Results Probl. Cell Differ. 35 (2002) 115-131
34. Azad A.K., Stanford D.R., Sarkar S., and Hopper A.K. Role of nuclear pools of aminoacyl-tRNA synthetases in tRNA nuclear export. Mol. Biol. Cell 12 (2001) 1381-1392
35. Steiner-Mosonyi M., and Mangroo D. The nuclear tRNA aminoacylation-dependent pathway may be the principal route used to export tRNA from the nucleus in Saccharomyces cerevisiae. Biochem J. 378 (2004) 809-816
36. Takano A., Endo T., and Yoshihisa T. tRNA actively shuttles between the nucleus and cytosol in yeast. Science 309 (2005) 140-142
37. Shaheen H.H., and Hopper A.K. Retrograde movement of tRNAs from the cytoplasm to the nucleus in Saccharomyces cerevisiae. Proc. Natl Acad. Sci. USA 102 (2005) 11290-11295
38. Whitney M.L., Hurto R.L., Shaheen H.H., and Hopper A.K. Rapid and reversible nuclear accumulation of cytoplasmic tRNA in response to nutrient availability. Mol. Biol. Cell 18 (2007) 2678-2686
39. Mylonis I., Chachami G., Samiotaki M., Panayotou G., Paraskeva E., Kalousi A., et al. Identification of MAPK phosphorylation sites and their role in the localization and activity of hypoxia-inducible factor 1a. J. Biol. Chem. 281 (2006) 33095-33106