Structural and functional mapping of the archaeal multi-aminoacyl-tRNA synthetase complex

FEBS Letters

Volumn 582, Issue 15, 2008, Pages 2178-2182

  Hausmann, Corinne D ^a   Ibba, Michael ^a  

^a OHIO STATE UNIVERSITY   (United States)

Author keywords

Amino acid; Aminoacyl tRNA synthetase; Translation

Indexed keywords

AMINO ACID TRANSFER RNA LIGASE; BACTERIAL PROTEIN; CORE PROTEIN; ELONGATION FACTOR 1ALPHA; PROTEIN LEURS; PROTEIN LYSRS; PROTEIN PRORS;

AMINO ACID SEQUENCE; AMINO TERMINAL SEQUENCE; ARCHAEBACTERIUM; ARTICLE; CARBOXY TERMINAL SEQUENCE; METHANOTHERMOBACTER THERMAUTOTROPHICUS; PEPTIDE MAPPING; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN DOMAIN; PROTEIN FUNCTION; PROTEIN PROTEIN INTERACTION; RNA EDITING;

AMINO ACYL-TRNA SYNTHETASES; ARCHAEAL PROTEINS; LEUCINE-TRNA LIGASE; LYSINE-TRNA LIGASE; METHANOBACTERIACEAE; MULTIENZYME COMPLEXES; PEPTIDE ELONGATION FACTOR 1; PROTEIN CONFORMATION;

ARCHAEA; METHANOTHERMOBACTER THERMAUTOTROPHICUS;

EID: 44749086081     PISSN: 00145793     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.febslet.2008.05.043     Document Type: Article

References (18)

1. Mirande M. Aminoacyl-tRNA synthetase family from prokaryotes and eukaryotes: structural domains and their implications. Prog. Nucl. Acid Res. Mol. Biol. 40 (1991) 95-142
2. Ling C., Yao Y.N., Zheng Y.G., Wei H., Wang L., Wu X.F., and Wang E.D. The C-terminal appended domain of human cytosolic leucyl-tRNA synthetase is indispensable in its interaction with arginyl-tRNA synthetase in the multi-tRNA synthetase complex. J. Biol. Chem. 280 (2005) 34755-34763
3. Cahuzac B., Berthonneau E., Birlirakis N., Guittet E., and Mirande M. A recurrent RNA-binding domain is appended to eukaryotic aminoacyl-tRNA synthetases. EMBO J. 19 (2000) 445-452
4. Guigou L., Shalak V., and Mirande M. The tRNA-interacting factor p43 associates with mammalian arginyl-tRNA synthetase but does not modify its tRNA aminoacylation properties. Biochemistry 43 (2004) 4592-4600
5. Robinson J.C., Kerjan P., and Mirande M. Macromolecular assemblage of aminoacyl-tRNA synthetases: quantitative analysis of protein-protein interactions and mechanism of complex assembly. J. Mol. Biol. 304 (2000) 983-994
6. Agou F., and Mirande M. Aspartyl-tRNA synthetase from rat: in vitro functional analysis of its assembly into the multisynthetase complex. Eur. J. Biochem. 243 (1997) 259-267
7. 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
8. Praetorius-Ibba M., Hausmann C.D., Paras M., Rogers T.E., and Ibba M. Functional association between three archaeal aminoacyl-tRNA synthetases. J. Biol. Chem. 282 (2007) 3680-3687
9. Hausmann C.D., Praetorius-Ibba M., and Ibba M. An aminoacyl-tRNA synthetase:elongation factor complex for substrate channeling in archaeal translation. Nucl. Acid Res. 35 (2007) 6094-6102
10. Fersht A.R., Ashford J.S., Bruton C.J., Jakes R., Koch G.L., and Hartley B.S. Active site titration and aminoacyl adenylate binding stoichiometry of aminoacyl-tRNA synthetases. Biochemistry 14 (1975) 1-4
11. Pro editing by Haemophilus influenzae YbaK via a novel synthetase YbaK · tRNA ternary complex. J. Biol. Chem. 280 (2005) 34465-34472
12. Wolfe C.L., Warrington J.A., Treadwell L., and Norcum M.T. A three-dimensional working model of the multienzyme complex of aminoacyl-tRNA synthetases based on electron microscopic placements of tRNA and proteins. J. Biol. Chem. 280 (2005) 38870-38878
13. Negrutskii B.S., Shalak V.F., Kerjan P., El'skaya A.V., and Mirande M. Functional interaction of mammalian valyl-tRNA synthetase with elongation factor EF-1alpha in the complex with EF-1H. J. Biol. Chem. 274 (1999) 4545-4550
14. Zhang C.M., Perona J.J., Ryu K., Francklyn C., and Hou Y.M. Distinct kinetic mechanisms of the two classes of aminoacyl-tRNA synthetases. J. Mol. Biol. 361 (2006) 300-311
15. Tukalo M., Yaremchuk A., Fukunaga R., Yokoyama S., and Cusack S. The crystal structure of leucyl-tRNA synthetase complexed with tRNALeu in the post-transfer-editing conformation. Nat. Struct. Mol. Biol. 12 (2005) 923-930
16. Leu reveal two modes of discriminator-base recognition. Nat. Struct. Mol. Biol. 12 (2005) 915-922
17. Ile. Biochemistry 46 (2007) 4985-4996
18. Nomanbhoy T.K., Hendrickson T.L., and Schimmel P. Transfer RNA-dependent translocation of misactivated amino acids to prevent errors in protein synthesis. Mol. Cell 4 (1999) 519-528