Aminoacyl-tRNA Synthetase Complexes: Molecular Multitasking Revealed

Overview

Journal FEMS Microbiol Rev

Publisher Oxford University Press

Specialty Microbiology

Date 2008 Jun 5

PMID 18522650

Citations 50

Authors

Corinne D Hausmann

Michael Ibba

Affiliations

Soon will be listed here.

Abstract

The accurate synthesis of proteins, dictated by the corresponding nucleotide sequence encoded in mRNA, is essential for cell growth and survival. Central to this process are the aminoacyl-tRNA synthetases (aaRSs), which provide amino acid substrates for the growing polypeptide chain in the form of aminoacyl-tRNAs. The aaRSs are essential for coupling the correct amino acid and tRNA molecules, but are also known to associate in higher order complexes with proteins involved in processes beyond translation. Multiprotein complexes containing aaRSs are found in all three domains of life playing roles in splicing, apoptosis, viral assembly, and regulation of transcription and translation. An overview of the complexes aaRSs form in all domains of life is presented, demonstrating the extensive network of connections between the translational machinery and cellular components involved in a myriad of essential processes beyond protein synthesis.

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References

Motorin YuA , Wolfson A, Orlovsky A, GLADILIN K . Mammalian valyl-tRNA synthetase forms a complex with the first elongation factor. FEBS Lett. 1988; 238(2):262-4. DOI: 10.1016/0014-5793(88)80492-7. View

Lopez-Huertas E, Charlton W, Johnson B, Graham I, Baker A . Stress induces peroxisome biogenesis genes. EMBO J. 2000; 19(24):6770-7. PMC: 305880. DOI: 10.1093/emboj/19.24.6770. View

Ahel I, Korencic D, Ibba M, Soll D . Trans-editing of mischarged tRNAs. Proc Natl Acad Sci U S A. 2003; 100(26):15422-7. PMC: 307583. DOI: 10.1073/pnas.2136934100. View

Eldred E, Schimmel P . Rapid deacylation by isoleucyl transfer ribonucleic acid synthetase of isoleucine-specific transfer ribonucleic acid aminoacylated with valine. J Biol Chem. 1972; 247(9):2961-4. View

Norcum M . Ultrastructure of the eukaryotic aminoacyl-tRNA synthetase complex derived from two dimensional averaging and classification of negatively stained electron microscopic images. FEBS Lett. 1999; 447(2-3):217-22. DOI: 10.1016/s0014-5793(99)00287-2. View

Kim T, Park S, Kim J, Seol W, Ko Y, Kim S . Catalytic peptide of human glutaminyl-tRNA synthetase is essential for its assembly to the aminoacyl-tRNA synthetase complex. J Biol Chem. 2000; 275(28):21768-72. DOI: 10.1074/jbc.M002404200. View

Dobard C, Briones M, Chow S . Molecular mechanisms by which human immunodeficiency virus type 1 integrase stimulates the early steps of reverse transcription. J Virol. 2007; 81(18):10037-46. PMC: 2045400. DOI: 10.1128/JVI.00519-07. View

Lee S, Cho B, Park S, Kim S . Aminoacyl-tRNA synthetase complexes: beyond translation. J Cell Sci. 2004; 117(Pt 17):3725-34. DOI: 10.1242/jcs.01342. View

Roy H, Ling J, Irnov M, Ibba M . Post-transfer editing in vitro and in vivo by the beta subunit of phenylalanyl-tRNA synthetase. EMBO J. 2004; 23(23):4639-48. PMC: 533057. DOI: 10.1038/sj.emboj.7600474. View

10.

Schon A, Kannangara C, Gough S, Soll D . Protein biosynthesis in organelles requires misaminoacylation of tRNA. Nature. 1988; 331(6152):187-90. DOI: 10.1038/331187a0. View

11.

Graindorge J, Senger B, Tritch D, Simos G, Fasiolo F . Role of Arc1p in the modulation of yeast glutamyl-tRNA synthetase activity. Biochemistry. 2005; 44(4):1344-52. DOI: 10.1021/bi049024z. View

12.

An S, Musier-Forsyth K . Cys-tRNA(Pro) editing by Haemophilus influenzae YbaK via a novel synthetase.YbaK.tRNA ternary complex. J Biol Chem. 2005; 280(41):34465-72. DOI: 10.1074/jbc.M507550200. View

13.

Howard O, Dong H, Yang D, Raben N, Nagaraju K, Rosen A . Histidyl-tRNA synthetase and asparaginyl-tRNA synthetase, autoantigens in myositis, activate chemokine receptors on T lymphocytes and immature dendritic cells. J Exp Med. 2002; 196(6):781-91. PMC: 2194054. DOI: 10.1084/jem.20020186. View

14.

Mirande M, Lazard M, Martinez R, Latreille M . Engineering mammalian aspartyl-tRNA synthetase to probe structural features mediating its association with the multisynthetase complex. Eur J Biochem. 1992; 203(3):459-66. DOI: 10.1111/j.1432-1033.1992.tb16570.x. View

15.

Buddha M, Crane B . Structure and activity of an aminoacyl-tRNA synthetase that charges tRNA with nitro-tryptophan. Nat Struct Mol Biol. 2005; 12(3):274-5. DOI: 10.1038/nsmb907. View

16.

Kaminska M, Shalak V, Mirande M . The appended C-domain of human methionyl-tRNA synthetase has a tRNA-sequestering function. Biochemistry. 2001; 40(47):14309-16. DOI: 10.1021/bi015670b. View

17.

Sang Lee J, Park S, Park H, Seol W, Lee S, Kim S . Interaction network of human aminoacyl-tRNA synthetases and subunits of elongation factor 1 complex. Biochem Biophys Res Commun. 2002; 291(1):158-64. DOI: 10.1006/bbrc.2002.6398. View

18.

Fersht A, Dingwall C . Evidence for the double-sieve editing mechanism in protein synthesis. Steric exclusion of isoleucine by valyl-tRNA synthetases. Biochemistry. 1979; 18(12):2627-31. DOI: 10.1021/bi00579a030. View

19.

Cen S, Khorchid A, Javanbakht H, GABOR J, Stello T, Shiba K . Incorporation of lysyl-tRNA synthetase into human immunodeficiency virus type 1. J Virol. 2001; 75(11):5043-8. PMC: 114908. DOI: 10.1128/JVI.75.11.5043-5048.2001. View

20.

Bandyopadhyay A, Deutscher M . Complex of aminoacyl-transfer RNA synthetases. J Mol Biol. 1971; 60(1):113-22. DOI: 10.1016/0022-2836(71)90451-7. View