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Volumn 38, Issue 5, 2013, Pages 222-228

Citric acid cycle and the origin of MARS

Author keywords

Citric acid cycle; Evolution; Multi aminoacyl tRNA synthetase complex; TRNA synthetase

Indexed keywords

2 OXOGLUTARIC ACID; AMINO ACID DERIVATIVE; AMINO ACID TRANSFER RNA LIGASE; CITRIC ACID; GLYOXYLIC ACID; OXALOACETIC ACID; PROTEIN AIMP1; PROTEIN AIMP2; PROTEIN AIMP3; PROTEIN MARS; SCAFFOLD PROTEIN; UNCLASSIFIED DRUG;

EID: 84876739557     PISSN: 09680004     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.tibs.2013.01.005     Document Type: Review
Times cited : (16)

References (50)
  • 1
    • 33645453254 scopus 로고    scopus 로고
    • Global landscape of protein complexes in the yeast Saccharomyces cerevisiae
    • Krogan N.J., et al. Global landscape of protein complexes in the yeast Saccharomyces cerevisiae. Nature 2006, 440:637-643.
    • (2006) Nature , vol.440 , pp. 637-643
    • Krogan, N.J.1
  • 2
    • 0022033589 scopus 로고
    • A complex from cultured Chinese hamster ovary cells containing nine aminoacyl-tRNA synthetases. Thermolabile leucyl-tRNA synthetase from the tsH1 mutant cell line is an integral component of this complex
    • Mirande M., et al. A complex from cultured Chinese hamster ovary cells containing nine aminoacyl-tRNA synthetases. Thermolabile leucyl-tRNA synthetase from the tsH1 mutant cell line is an integral component of this complex. Eur. J. Biochem. 1985, 147:281-289.
    • (1985) Eur. J. Biochem. , vol.147 , pp. 281-289
    • Mirande, M.1
  • 3
    • 0028273032 scopus 로고
    • The multienzyme complex containing nine aminoacyl-tRNA synthetases is ubiquitous from Drosophila to mammals
    • Kerjan P., et al. The multienzyme complex containing nine aminoacyl-tRNA synthetases is ubiquitous from Drosophila to mammals. Biochim. Biophys. Acta 1994, 1199:293-297.
    • (1994) Biochim. Biophys. Acta , vol.1199 , pp. 293-297
    • Kerjan, P.1
  • 4
    • 33846016966 scopus 로고    scopus 로고
    • Hierarchical network between the components of the multi-tRNA synthetase complex: implications for complex formation
    • Han J.M., et al. Hierarchical network between the components of the multi-tRNA synthetase complex: implications for complex formation. J. Biol. Chem. 2006, 281:38663-38667.
    • (2006) J. Biol. Chem. , vol.281 , pp. 38663-38667
    • Han, J.M.1
  • 5
    • 0024419067 scopus 로고
    • Isolation and electron microscopic characterization of the high molecular mass aminoacyl-tRNA synthetase complex from murine erythroleukemia cells
    • Norcum M.T. Isolation and electron microscopic characterization of the high molecular mass aminoacyl-tRNA synthetase complex from murine erythroleukemia cells. J. Biol. Chem. 1989, 264:15043-15051.
    • (1989) J. Biol. Chem. , vol.264 , pp. 15043-15051
    • Norcum, M.T.1
  • 6
    • 0028264012 scopus 로고
    • Evidence for similar structural organization of the multienzyme aminoacyl-tRNA synthetase complex in vivo and in vitro
    • Filonenko V.V., Deutscher M.P. Evidence for similar structural organization of the multienzyme aminoacyl-tRNA synthetase complex in vivo and in vitro. J. Biol. Chem. 1994, 269:17375-17378.
    • (1994) J. Biol. Chem. , vol.269 , pp. 17375-17378
    • Filonenko, V.V.1    Deutscher, M.P.2
  • 7
    • 0025876244 scopus 로고
    • Channeling of aminoacyl-tRNA for protein synthesis in vivo
    • Negrutskii B.S., Deutscher M.P. Channeling of aminoacyl-tRNA for protein synthesis in vivo. Proc. Natl. Acad. Sci. U.S.A. 1991, 88:4991-4995.
    • (1991) Proc. Natl. Acad. Sci. U.S.A. , vol.88 , pp. 4991-4995
    • Negrutskii, B.S.1    Deutscher, M.P.2
  • 8
    • 34247131410 scopus 로고    scopus 로고
    • Macromolecular complexes as depots for releasable regulatory proteins
    • Ray P.S., et al. Macromolecular complexes as depots for releasable regulatory proteins. Trends Biochem. Sci. 2007, 32:158-164.
    • (2007) Trends Biochem. Sci. , vol.32 , pp. 158-164
    • Ray, P.S.1
  • 9
    • 0034644704 scopus 로고    scopus 로고
    • Active aminoacyl-tRNA synthetases are present in nuclei as a high molecular weight multienzyme complex
    • Nathanson L., Deutscher M.P. Active aminoacyl-tRNA synthetases are present in nuclei as a high molecular weight multienzyme complex. J. Biol. Chem. 2000, 275:31559-31562.
    • (2000) J. Biol. Chem. , vol.275 , pp. 31559-31562
    • Nathanson, L.1    Deutscher, M.P.2
  • 10
    • 0037062472 scopus 로고    scopus 로고
    • P38 is essential for the assembly and stability of macromolecular tRNA synthetase complex: implications for its physiological significance
    • Kim J.Y., et al. p38 is essential for the assembly and stability of macromolecular tRNA synthetase complex: implications for its physiological significance. Proc. Natl. Acad. Sci. U.S.A. 2002, 99:7912-7916.
    • (2002) Proc. Natl. Acad. Sci. U.S.A. , vol.99 , pp. 7912-7916
    • Kim, J.Y.1
  • 11
    • 0037743658 scopus 로고    scopus 로고
    • Downregulation of FUSE-binding protein and c-myc by tRNA synthetase cofactor p38 is required for lung cell differentiation
    • Kim M.J., et al. Downregulation of FUSE-binding protein and c-myc by tRNA synthetase cofactor p38 is required for lung cell differentiation. Nat. Genet. 2003, 34:330-336.
    • (2003) Nat. Genet. , vol.34 , pp. 330-336
    • Kim, M.J.1
  • 12
    • 0033582434 scopus 로고    scopus 로고
    • Functional interaction of mammalian valyl-tRNA synthetase with elongation factor EF-1alpha in the complex with EF-1H
    • Negrutskii B.S., et al. Functional interaction of mammalian valyl-tRNA synthetase with elongation factor EF-1alpha in the complex with EF-1H. J. Biol. Chem. 1999, 274:4545-4550.
    • (1999) J. Biol. Chem. , vol.274 , pp. 4545-4550
    • Negrutskii, B.S.1
  • 13
    • 0031610693 scopus 로고    scopus 로고
    • A conserved domain within Arc1p delivers tRNA to aminoacyl-tRNA synthetases
    • Simos G., et al. A conserved domain within Arc1p delivers tRNA to aminoacyl-tRNA synthetases. Mol. Cell 1998, 1:235-242.
    • (1998) Mol. Cell , vol.1 , pp. 235-242
    • Simos, G.1
  • 14
    • 0029790980 scopus 로고    scopus 로고
    • The yeast protein Arc1p binds to tRNA and functions as a cofactor for the methionyl- and glutamyl-tRNA synthetases
    • Simos G., et al. The yeast protein Arc1p binds to tRNA and functions as a cofactor for the methionyl- and glutamyl-tRNA synthetases. EMBO J. 1996, 15:5437-5448.
    • (1996) EMBO J. , vol.15 , pp. 5437-5448
    • Simos, G.1
  • 15
    • 33947522226 scopus 로고    scopus 로고
    • Functional association between three archaeal aminoacyl-tRNA synthetases
    • Praetorius-Ibba M., et al. Functional association between three archaeal aminoacyl-tRNA synthetases. J. Biol. Chem. 2007, 282:3680-3687.
    • (2007) J. Biol. Chem. , vol.282 , pp. 3680-3687
    • Praetorius-Ibba, M.1
  • 16
    • 39549104965 scopus 로고    scopus 로고
    • An important role for the multienzyme aminoacyl-tRNA synthetase complex in mammalian translation and cell growth
    • Kyriacou S.V., Deutscher M.P. An important role for the multienzyme aminoacyl-tRNA synthetase complex in mammalian translation and cell growth. Mol. Cell 2008, 29:419-427.
    • (2008) Mol. Cell , vol.29 , pp. 419-427
    • Kyriacou, S.V.1    Deutscher, M.P.2
  • 17
    • 21244436047 scopus 로고    scopus 로고
    • Occurrence of the aminoacyl-tRNA synthetases in high-molecular weight complexes correlates with the size of substrate amino acids
    • Wolfson A., Knight R. Occurrence of the aminoacyl-tRNA synthetases in high-molecular weight complexes correlates with the size of substrate amino acids. FEBS Lett. 2005, 579:3467-3472.
    • (2005) FEBS Lett. , vol.579 , pp. 3467-3472
    • Wolfson, A.1    Knight, R.2
  • 19
    • 0030998704 scopus 로고    scopus 로고
    • Structure and regulation of expression of the Bacillus subtilis valyl-tRNA synthetase gene
    • Luo D., et al. Structure and regulation of expression of the Bacillus subtilis valyl-tRNA synthetase gene. J. Bacteriol. 1997, 179:2472-2478.
    • (1997) J. Bacteriol. , vol.179 , pp. 2472-2478
    • Luo, D.1
  • 20
    • 0023664434 scopus 로고
    • Overexpression of mammalian phenylalanyl-tRNA synthetase upon phenylalanine restriction
    • Lazard M., et al. Overexpression of mammalian phenylalanyl-tRNA synthetase upon phenylalanine restriction. FEBS Lett. 1987, 216:27-30.
    • (1987) FEBS Lett. , vol.216 , pp. 27-30
    • Lazard, M.1
  • 21
    • 0021112011 scopus 로고
    • Structure and expression of two aminoacyl-tRNA synthetase genes from Saccharomyces cerevisiae
    • Meussdoerffer F., Fink G.R. Structure and expression of two aminoacyl-tRNA synthetase genes from Saccharomyces cerevisiae. J. Biol. Chem. 1983, 258:6293-6299.
    • (1983) J. Biol. Chem. , vol.258 , pp. 6293-6299
    • Meussdoerffer, F.1    Fink, G.R.2
  • 22
    • 0030015489 scopus 로고    scopus 로고
    • Processing of the leader mRNA plays a major role in the induction of thrS expression following threonine starvation in Bacillus subtilis
    • Condon C., et al. Processing of the leader mRNA plays a major role in the induction of thrS expression following threonine starvation in Bacillus subtilis. Proc. Natl. Acad. Sci. U.S.A. 1996, 93:6992-6997.
    • (1996) Proc. Natl. Acad. Sci. U.S.A. , vol.93 , pp. 6992-6997
    • Condon, C.1
  • 23
    • 0018398193 scopus 로고
    • Relationship between histidyl-tRNA level and protein synthesis rate in wild-type and mutant Chinese hamster ovary cells
    • Lofgren D.J., Thompson L.H. Relationship between histidyl-tRNA level and protein synthesis rate in wild-type and mutant Chinese hamster ovary cells. J. Cell. Physiol. 1979, 99:303-312.
    • (1979) J. Cell. Physiol. , vol.99 , pp. 303-312
    • Lofgren, D.J.1    Thompson, L.H.2
  • 24
    • 84864282902 scopus 로고    scopus 로고
    • Association of a multi-synthetase complex with translating ribosomes in the archaeon Thermococcus kodakarensis
    • Raina M., et al. Association of a multi-synthetase complex with translating ribosomes in the archaeon Thermococcus kodakarensis. FEBS Lett. 2012, 586:2232-2238.
    • (2012) FEBS Lett. , vol.586 , pp. 2232-2238
    • Raina, M.1
  • 25
    • 84866626969 scopus 로고    scopus 로고
    • Homeostatic mechanisms by alternative forms of tRNA synthetases
    • Guo M., Schimmel P. Homeostatic mechanisms by alternative forms of tRNA synthetases. Trends Biochem. Sci. 2012, 37:401-403.
    • (2012) Trends Biochem. Sci. , vol.37 , pp. 401-403
    • Guo, M.1    Schimmel, P.2
  • 26
    • 79957776598 scopus 로고    scopus 로고
    • Structural context for mobilization of a human tRNA synthetase from its cytoplasmic complex
    • Fang P., et al. Structural context for mobilization of a human tRNA synthetase from its cytoplasmic complex. Proc. Natl. Acad. Sci. U.S.A. 2011, 108:8239-8244.
    • (2011) Proc. Natl. Acad. Sci. U.S.A. , vol.108 , pp. 8239-8244
    • Fang, P.1
  • 27
    • 77956095201 scopus 로고    scopus 로고
    • New functions of aminoacyl-tRNA synthetases beyond translation
    • Guo M., et al. New functions of aminoacyl-tRNA synthetases beyond translation. Nat. Rev. Mol. Cell Biol. 2010, 11:668-674.
    • (2010) Nat. Rev. Mol. Cell Biol. , vol.11 , pp. 668-674
    • Guo, M.1
  • 28
    • 34248223568 scopus 로고    scopus 로고
    • Evolution of glyoxylate cycle enzymes in Metazoa: evidence of multiple horizontal transfer events and pseudogene formation
    • Kondrashov F.A., et al. Evolution of glyoxylate cycle enzymes in Metazoa: evidence of multiple horizontal transfer events and pseudogene formation. Biol. Direct 2006, 1:31.
    • (2006) Biol. Direct , vol.1 , pp. 31
    • Kondrashov, F.A.1
  • 29
    • 44849096180 scopus 로고    scopus 로고
    • Aminoacyl-tRNA synthetase complexes: molecular multitasking revealed
    • Hausmann C.D., Ibba M. Aminoacyl-tRNA synthetase complexes: molecular multitasking revealed. FEMS Microbiol. Rev. 2008, 32:705-721.
    • (2008) FEMS Microbiol. Rev. , vol.32 , pp. 705-721
    • Hausmann, C.D.1    Ibba, M.2
  • 30
    • 0029043987 scopus 로고
    • Bifunctional glyoxylate cycle protein of Caenorhabditis elegans: a developmentally regulated protein of intestine and muscle
    • Liu F., et al. Bifunctional glyoxylate cycle protein of Caenorhabditis elegans: a developmentally regulated protein of intestine and muscle. Dev. Biol. 1995, 169:399-414.
    • (1995) Dev. Biol. , vol.169 , pp. 399-414
    • Liu, F.1
  • 31
    • 80051503319 scopus 로고    scopus 로고
    • Caenorhabditis elegans evolves a new architecture for the multi-aminoacyl-tRNA synthetase complex
    • Havrylenko S., et al. Caenorhabditis elegans evolves a new architecture for the multi-aminoacyl-tRNA synthetase complex. J. Biol. Chem. 2011, 286:28476-28487.
    • (2011) J. Biol. Chem. , vol.286 , pp. 28476-28487
    • Havrylenko, S.1
  • 32
    • 0020491186 scopus 로고
    • Macromolecular complexes from sheep and rabbit containing seven aminoacyl-tRNA synthetases. I. Species specificity of the polypeptide composition
    • Kellermann O., et al. Macromolecular complexes from sheep and rabbit containing seven aminoacyl-tRNA synthetases. I. Species specificity of the polypeptide composition. J. Biol. Chem. 1982, 257:11041-11048.
    • (1982) J. Biol. Chem. , vol.257 , pp. 11041-11048
    • Kellermann, O.1
  • 33
    • 39149110563 scopus 로고    scopus 로고
    • The genome of the choanoflagellate Monosiga brevicollis and the origin of metazoans
    • King N., et al. The genome of the choanoflagellate Monosiga brevicollis and the origin of metazoans. Nature 2008, 451:783-788.
    • (2008) Nature , vol.451 , pp. 783-788
    • King, N.1
  • 34
    • 0042761742 scopus 로고    scopus 로고
    • Evolution of the coordinate regulation of glycolytic enzyme genes by hypoxia
    • Webster K.A. Evolution of the coordinate regulation of glycolytic enzyme genes by hypoxia. J. Exp. Biol. 2003, 206:2911-2922.
    • (2003) J. Exp. Biol. , vol.206 , pp. 2911-2922
    • Webster, K.A.1
  • 35
    • 0031781593 scopus 로고    scopus 로고
    • Anaerobic regulation of Bacillus subtilis Krebs cycle genes
    • Nakano M.M., et al. Anaerobic regulation of Bacillus subtilis Krebs cycle genes. J. Bacteriol. 1998, 180:3304-3311.
    • (1998) J. Bacteriol. , vol.180 , pp. 3304-3311
    • Nakano, M.M.1
  • 36
    • 80052613870 scopus 로고    scopus 로고
    • Analysis of hypoxia and hypoxia-like states through metabolite profiling
    • Gleason J.E., et al. Analysis of hypoxia and hypoxia-like states through metabolite profiling. PLoS ONE 2011, 6:e24741.
    • (2011) PLoS ONE , vol.6
    • Gleason, J.E.1
  • 37
    • 65249123553 scopus 로고    scopus 로고
    • Dissection of the structural organization of the aminoacyl-tRNA synthetase complex
    • Kaminska M., et al. Dissection of the structural organization of the aminoacyl-tRNA synthetase complex. J. Biol. Chem. 2009, 284:6053-6060.
    • (2009) J. Biol. Chem. , vol.284 , pp. 6053-6060
    • Kaminska, M.1
  • 38
    • 77957201669 scopus 로고    scopus 로고
    • Nucleating the assembly of macromolecular complexes
    • Peterson-Kaufman K.J., et al. Nucleating the assembly of macromolecular complexes. Chembiochem 2010, 11:1955-1962.
    • (2010) Chembiochem , vol.11 , pp. 1955-1962
    • Peterson-Kaufman, K.J.1
  • 39
    • 0035968226 scopus 로고    scopus 로고
    • The EMAPII cytokine is released from the mammalian multisynthetase complex after cleavage of its p43/proEMAPII component
    • Shalak V., et al. The EMAPII cytokine is released from the mammalian multisynthetase complex after cleavage of its p43/proEMAPII component. J. Biol. Chem. 2001, 276:23769-23776.
    • (2001) J. Biol. Chem. , vol.276 , pp. 23769-23776
    • Shalak, V.1
  • 40
    • 49649116700 scopus 로고    scopus 로고
    • AIMP2/p38, the scaffold for the multi-tRNA synthetase complex, responds to genotoxic stresses via p53
    • Han J.M., et al. AIMP2/p38, the scaffold for the multi-tRNA synthetase complex, responds to genotoxic stresses via p53. Proc. Natl. Acad. Sci. U.S.A. 2008, 105:11206-11211.
    • (2008) Proc. Natl. Acad. Sci. U.S.A. , vol.105 , pp. 11206-11211
    • Han, J.M.1
  • 41
    • 78349290448 scopus 로고    scopus 로고
    • Downregulation of lamin A by tumor suppressor AIMP3/p18 leads to a progeroid phenotype in mice
    • Oh Y.S., et al. Downregulation of lamin A by tumor suppressor AIMP3/p18 leads to a progeroid phenotype in mice. Aging Cell 2010, 9:810-822.
    • (2010) Aging Cell , vol.9 , pp. 810-822
    • Oh, Y.S.1
  • 42
    • 0032770725 scopus 로고    scopus 로고
    • On the possibility of constructive neutral evolution
    • Stoltzfus A. On the possibility of constructive neutral evolution. J. Mol. Evol. 1999, 49:169-181.
    • (1999) J. Mol. Evol. , vol.49 , pp. 169-181
    • Stoltzfus, A.1
  • 43
    • 0027201750 scopus 로고
    • On the evolution of RNA editing
    • Covello P.S., Gray M.W. On the evolution of RNA editing. Trends Genet. 1993, 9:265-268.
    • (1993) Trends Genet. , vol.9 , pp. 265-268
    • Covello, P.S.1    Gray, M.W.2
  • 44
    • 78149403325 scopus 로고    scopus 로고
    • Cell biology. Irremediable complexity?
    • Gray M.W., et al. Cell biology. Irremediable complexity?. Science 2010, 330:920-921.
    • (2010) Science , vol.330 , pp. 920-921
    • Gray, M.W.1
  • 45
    • 34547396004 scopus 로고    scopus 로고
    • The frailty of adaptive hypotheses for the origins of organismal complexity
    • Lynch M. The frailty of adaptive hypotheses for the origins of organismal complexity. Proc. Natl. Acad. Sci. U.S.A. 2007, 104(Suppl. 1):8597-8604.
    • (2007) Proc. Natl. Acad. Sci. U.S.A. , vol.104 , Issue.SUPPL. 1 , pp. 8597-8604
    • Lynch, M.1
  • 46
    • 0021243715 scopus 로고
    • The eucaryotic aminoacyl-tRNA synthetase complex: suggestions for its structure and function
    • Deutscher M.P. The eucaryotic aminoacyl-tRNA synthetase complex: suggestions for its structure and function. J. Cell Biol. 1984, 99:373-377.
    • (1984) J. Cell Biol. , vol.99 , pp. 373-377
    • Deutscher, M.P.1
  • 47
    • 0015243504 scopus 로고
    • Complex of aminoacyl-transfer RNA synthetases
    • Bandyopadhyay A.K., Deutscher M.P. Complex of aminoacyl-transfer RNA synthetases. J. Mol. Biol. 1971, 60:113-122.
    • (1971) J. Mol. Biol. , vol.60 , pp. 113-122
    • Bandyopadhyay, A.K.1    Deutscher, M.P.2
  • 48
    • 67649412022 scopus 로고    scopus 로고
    • Dynamic organization of aminoacyl-tRNA synthetase complexes in the cytoplasm of human cells
    • Kaminska M., et al. Dynamic organization of aminoacyl-tRNA synthetase complexes in the cytoplasm of human cells. J. Biol. Chem. 2009, 284:13746-13754.
    • (2009) J. Biol. Chem. , vol.284 , pp. 13746-13754
    • Kaminska, M.1
  • 49
    • 0017579551 scopus 로고
    • Subcellular distribution of aminoacyl-tRNA synthetases in various eukaryotic cells
    • Ussery M.A., et al. Subcellular distribution of aminoacyl-tRNA synthetases in various eukaryotic cells. Eur. J. Biochem. 1977, 72:491-500.
    • (1977) Eur. J. Biochem. , vol.72 , pp. 491-500
    • Ussery, M.A.1
  • 50
    • 0032791864 scopus 로고    scopus 로고
    • Renaturation of rabbit liver aminoacyl-tRNA synthetases by 80S ribosomes
    • Turkovskaya H.V., et al. Renaturation of rabbit liver aminoacyl-tRNA synthetases by 80S ribosomes. Int. J. Biochem. Cell Biol. 1999, 31:759-768.
    • (1999) Int. J. Biochem. Cell Biol. , vol.31 , pp. 759-768
    • Turkovskaya, H.V.1


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