메뉴 건너뛰기




Volumn 365, Issue 4, 2008, Pages 718-723

Lysyl-tRNA synthetase interacts with EF1α, aspartyl-tRNA synthetase and p38 in vitro

Author keywords

Amino terminal extensions; Aminoacylation; EF1 ; Enzyme interactions; Lysyl tRNA synthetase; Multi enzyme complex; p38; Supramolecular assembly

Indexed keywords

AMINO ACID TRANSFER RNA LIGASE; ASPARTIC ACID TRANSFER RNA; CYTOKINE; ELONGATION FACTOR 1ALPHA; GUANOSINE TRIPHOSPHATE; LYSINE TRANSFER RNA; LYSINE TRANSFER RNA LIGASE; PARKIN; SCAFFOLD PROTEIN; SYNAPTOPHYSIN; SYNTHETASE;

EID: 36849031896     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2007.11.028     Document Type: Article
Times cited : (13)

References (24)
  • 1
    • 34247131410 scopus 로고    scopus 로고
    • Macromolecular complexes as depots for releasable regulatory proteins
    • Ray P.S., Arif A., and Fox P.L. Macromolecular complexes as depots for releasable regulatory proteins. Trends Biochem. Sci. 32 (2007) 158-164
    • (2007) Trends Biochem. Sci. , vol.32 , pp. 158-164
    • Ray, P.S.1    Arif, A.2    Fox, P.L.3
  • 3
    • 0020359763 scopus 로고
    • Macromolecular complexes from sheep and rabbit containing seven aminoacyl-tRNA synthetases
    • Mirande M., Kellermann O., and Waller J.P. Macromolecular complexes from sheep and rabbit containing seven aminoacyl-tRNA synthetases. J. Biol. Chem. 257 (1982) 11049-11055
    • (1982) J. Biol. Chem. , vol.257 , pp. 11049-11055
    • Mirande, M.1    Kellermann, O.2    Waller, J.P.3
  • 4
    • 0000983324 scopus 로고    scopus 로고
    • Interaction between human tRNA synthetases involves repeated sequence elements
    • Rho S.B., Lee K.H., Kim J.W., Shiba K., Jo Y.J., and Kim S. Interaction between human tRNA synthetases involves repeated sequence elements. Proc. Natl. Acad. Sci. USA 93 (1996) 10128-10133
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 10128-10133
    • Rho, S.B.1    Lee, K.H.2    Kim, J.W.3    Shiba, K.4    Jo, Y.J.5    Kim, S.6
  • 5
    • 0034671360 scopus 로고    scopus 로고
    • Macromolecular assemblage of aminoacyl-tRNA synthetases
    • Robinson J.C., Kerjan P., and Mirande M. Macromolecular assemblage of aminoacyl-tRNA synthetases. J. Mol. Biol. 304 (2000) 983-994
    • (2000) J. Mol. Biol. , vol.304 , pp. 983-994
    • Robinson, J.C.1    Kerjan, P.2    Mirande, M.3
  • 6
    • 33644668804 scopus 로고    scopus 로고
    • A three-dimensional working model of the multienzyme complex of aminoacyl-tRNA synthetases based on electron microscopic placements of tRNA and proteins
    • 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
    • (2005) J. Biol. Chem. , vol.280 , pp. 38870-38878
    • Wolfe, C.L.1    Warrington, J.A.2    Treadwell, L.3    Norcum, M.T.4
  • 7
    • 0023664710 scopus 로고
    • A basic NH2-terminal extension of rat liver arginyl-tRNA synthetase required for its association with high molecular weight complexes
    • Vellekamp G., and Deutscher M.P. A basic NH2-terminal extension of rat liver arginyl-tRNA synthetase required for its association with high molecular weight complexes. J. Biol. Chem. 262 (1987) 9927-9930
    • (1987) J. Biol. Chem. , vol.262 , pp. 9927-9930
    • Vellekamp, G.1    Deutscher, M.P.2
  • 8
    • 46549102174 scopus 로고
    • A model for the structural organization of aminoacyl-tRNA synthetases in mammalian cells
    • Cirakoglu B., Mirande M., and Waller J.P. A model for the structural organization of aminoacyl-tRNA synthetases in mammalian cells. FEBS Lett. 183 (1985) 185-190
    • (1985) FEBS Lett. , vol.183 , pp. 185-190
    • Cirakoglu, B.1    Mirande, M.2    Waller, J.P.3
  • 9
    • 0024463581 scopus 로고
    • cDNA sequence, predicted primary structure, and evolving amphiphilic helix of human aspartyl-tRNA synthetase
    • Jacobo-Molina A., Peterson R., and Yang D.C. cDNA sequence, predicted primary structure, and evolving amphiphilic helix of human aspartyl-tRNA synthetase. J. Biol. Chem. 264 (1989) 16608-16612
    • (1989) J. Biol. Chem. , vol.264 , pp. 16608-16612
    • Jacobo-Molina, A.1    Peterson, R.2    Yang, D.C.3
  • 10
    • 0030921858 scopus 로고    scopus 로고
    • Human lysyl-tRNA synthetase accepts nucleotide 73 variants and rescues Escherichia coli double-defective mutant
    • Shiba K., Stello T., Motegi H., Noda T., Musier-Forsyth K., and Schimmel P. Human lysyl-tRNA synthetase accepts nucleotide 73 variants and rescues Escherichia coli double-defective mutant. J. Biol. Chem. 272 (1997) 22809-22816
    • (1997) J. Biol. Chem. , vol.272 , pp. 22809-22816
    • Shiba, K.1    Stello, T.2    Motegi, H.3    Noda, T.4    Musier-Forsyth, K.5    Schimmel, P.6
  • 11
    • 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., Kang Y.S., Lee J.W., Kim H.J., Ahn Y.H., Park H., Ko Y.G., and Kim S. p38 is essential for the assembly and stability of macromolecular tRNA synthetase complex: implications for its physiological significance. Proc. Natl. Acad. Sci. USA 99 (2002) 7912-7916
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 7912-7916
    • Kim, J.Y.1    Kang, Y.S.2    Lee, J.W.3    Kim, H.J.4    Ahn, Y.H.5    Park, H.6    Ko, Y.G.7    Kim, S.8
  • 12
    • 0031464187 scopus 로고    scopus 로고
    • The p43 component of the mammalian multi-synthetase complex is likely to be the precursor of the endothelial monocyte-activating polypeptide II cytokine
    • Quevillon S., Agou F., Robinson J.C., and Mirande M. 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 (1997) 32573-32579
    • (1997) J. Biol. Chem. , vol.272 , pp. 32573-32579
    • Quevillon, S.1    Agou, F.2    Robinson, J.C.3    Mirande, M.4
  • 13
    • 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., Park B.J., Kang Y.S., Kim H.J., Park J.H., Kang J.W., Lee S.W., Han J.M., Lee H.W., and Kim S. Downregulation of FUSE-binding protein and c-myc by tRNA synthetase cofactor p38 is required for lung cell differentiation. Nat. Genet. 34 (2003) 330-336
    • (2003) Nat. Genet. , vol.34 , pp. 330-336
    • Kim, M.J.1    Park, B.J.2    Kang, Y.S.3    Kim, H.J.4    Park, J.H.5    Kang, J.W.6    Lee, S.W.7    Han, J.M.8    Lee, H.W.9    Kim, S.10
  • 15
    • 0018801031 scopus 로고
    • Disassembly and gross structure of particulate aminoacyl-tRNA synthetases from rat liver
    • Dang C.V., and Yang D.C.H. Disassembly and gross structure of particulate aminoacyl-tRNA synthetases from rat liver. J. Biol. Chem. 254 (1979) 5350-5356
    • (1979) J. Biol. Chem. , vol.254 , pp. 5350-5356
    • Dang, C.V.1    Yang, D.C.H.2
  • 16
    • 0037127205 scopus 로고    scopus 로고
    • The N-terminal domain of mammalian Lysyl-tRNA synthetase is a functional tRNA-binding domain
    • 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
    • (2002) J. Biol. Chem. , vol.277 , pp. 1762-1769
    • Francin, M.1    Kaminska, M.2    Kerjan, P.3    Mirande, M.4
  • 17
    • 33747467582 scopus 로고    scopus 로고
    • Identity elements for specific aminoacylation of a tRNA by mammalian lysyl-tRNA synthetase bearing a non-specific tRNA-interacting factor
    • Francin M., and Mirande M. Identity elements for specific aminoacylation of a tRNA by mammalian lysyl-tRNA synthetase bearing a non-specific tRNA-interacting factor. Biochemistry 45 (2006) 10153-10160
    • (2006) Biochemistry , vol.45 , pp. 10153-10160
    • Francin, M.1    Mirande, M.2
  • 18
    • 0028589301 scopus 로고
    • Mechanisms of the transfer of aminoacyl-tRNA from aminoacyl-tRNA synthetase to the elongation factor 1α
    • Reed V.S., Wastney M., and Yang D.C.H. Mechanisms of the transfer of aminoacyl-tRNA from aminoacyl-tRNA synthetase to the elongation factor 1α. J. Biol. Chem. 269 (1994) 32932-32936
    • (1994) J. Biol. Chem. , vol.269 , pp. 32932-32936
    • Reed, V.S.1    Wastney, M.2    Yang, D.C.H.3
  • 19
    • 0031019325 scopus 로고    scopus 로고
    • Aspartyl-tRNA synthetase from rat: in vitro functional analysis of its assembly into the multisynthetase complex
    • 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
    • (1997) Eur. J. Biochem. , vol.243 , pp. 259-267
    • Agou, F.1    Mirande, M.2
  • 21
    • 34247324364 scopus 로고    scopus 로고
    • Systematic analysis of fusion and affinity tags using human aspartyl-tRNA synthetase expressed in E. coli
    • Guzzo C.M., and Yang D.C. Systematic analysis of fusion and affinity tags using human aspartyl-tRNA synthetase expressed in E. coli. Protein Expr. Purif. 54 (2007) 166-175
    • (2007) Protein Expr. Purif. , vol.54 , pp. 166-175
    • Guzzo, C.M.1    Yang, D.C.2
  • 22
    • 0027516716 scopus 로고
    • Expression of human aspartyl-tRNA synthetase in Escherichia coli: functional analysis of the N-terminal putative amphiphilic helix
    • Escalante C., and Yang D.C. Expression of human aspartyl-tRNA synthetase in Escherichia coli: functional analysis of the N-terminal putative amphiphilic helix. J. Biol. Chem. 268 (1993) 6014-6023
    • (1993) J. Biol. Chem. , vol.268 , pp. 6014-6023
    • Escalante, C.1    Yang, D.C.2
  • 23
    • 0025754306 scopus 로고
    • Protein kinase C phosphorylates glutamyl-tRNA synthetase in rabbit reticulocytes stimulated by tumor promoting phorbol esters
    • Venema R.C., and Traugh J.A. Protein kinase C phosphorylates glutamyl-tRNA synthetase in rabbit reticulocytes stimulated by tumor promoting phorbol esters. J. Biol. Chem. 266 (1991) 5298-5302
    • (1991) J. Biol. Chem. , vol.266 , pp. 5298-5302
    • Venema, R.C.1    Traugh, J.A.2
  • 24
    • 0022178606 scopus 로고
    • Alteration of aminoacyl-tRNA synthetase activities by phosphorylation with casein kinase I
    • Pendergast A.M., and Traugh J. Alteration of aminoacyl-tRNA synthetase activities by phosphorylation with casein kinase I. J. Biol. Chem. 260 (1985) 11769-11774
    • (1985) J. Biol. Chem. , vol.260 , pp. 11769-11774
    • Pendergast, A.M.1    Traugh, J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.