메뉴 건너뛰기




Volumn 12, Issue 10, 2003, Pages 2282-2290

Isolation and characterization of human nuclear and cytosolic multisynthetase complexes and the intracellular distribution of p43/EMAPII

Author keywords

Aminoacyl tRNA synthetase complexes; Electron microscopy; Nuclear particle; Three dimensional reconstruction

Indexed keywords

AMINO ACID TRANSFER RNA LIGASE; CYTOKINE; ENDOTHELIAL MONOCYTE ACTIVATING POLYPEPTIDE II; GLUTAMINE TRANSFER RNA LIGASE; POLYPEPTIDE; PROTEIN; SYNTHETASE; URANYL ACETATE; VANADIC ACID;

EID: 0141634361     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1110/ps.03147903     Document Type: Article
Times cited : (21)

References (25)
  • 1
    • 0033867284 scopus 로고    scopus 로고
    • Endothelial monocyte-activating polypeptide II, a tumor-derived cytokine that plays an important role in inflammation, apoptosis, and angiogenesis
    • Berger, A.C., Tang, G., Alexander, H.R., and Libutti, S.K. 2000. Endothelial monocyte-activating polypeptide II, a tumor-derived cytokine that plays an important role in inflammation, apoptosis, and angiogenesis. J. Immunother. 23: 519-527.
    • (2000) J. Immunother. , vol.23 , pp. 519-527
    • Berger, A.C.1    Tang, G.2    Alexander, H.R.3    Libutti, S.K.4
  • 2
    • 0029975088 scopus 로고    scopus 로고
    • SPIDER and WEB: Processing and visualization of images in 3D electron microscopy and related fields
    • Frank, J., Radermacher, M., Penczek, P., Zhu, J., Li, Y., Ladjadj, M., and Leith, A. 1996. SPIDER and WEB: Processing and visualization of images in 3D electron microscopy and related fields. J. Struct. Biol. 116: 190-199.
    • (1996) J. Struct. Biol. , vol.116 , pp. 190-199
    • Frank, J.1    Radermacher, M.2    Penczek, P.3    Zhu, J.4    Li, Y.5    Ladjadj, M.6    Leith, A.7
  • 3
    • 0020724788 scopus 로고
    • Improved methodology for analysis and quantitation of proteins on one-dimensional silver-stained slab gels
    • Giulian, G.G., Moss, R.L., and Greaser, M. 1983. Improved methodology for analysis and quantitation of proteins on one-dimensional silver-stained slab gels. Anal. Biochem. 129: 277-287.
    • (1983) Anal. Biochem. , vol.129 , pp. 277-287
    • Giulian, G.G.1    Moss, R.L.2    Greaser, M.3
  • 4
    • 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. 2002. p38 is essential for the assembly and stability of macromolecular tRNA synthetase complex: Implications for its physiological significance. Proc. Natl. Acad. Sci. 99: 7912-7916.
    • (2002) Proc. Natl. Acad. Sci. , 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
  • 6
    • 0034192459 scopus 로고    scopus 로고
    • Nucleolar localization of human methionyl-tRNA synthetase and its role in ribosomal RNA synthesis
    • Ko, Y.-G., Kang, Y.-S., Kim, E.-K., Park, S.G., and Kim, S. 2000. Nucleolar localization of human methionyl-tRNA synthetase and its role in ribosomal RNA synthesis J. Cell Biol. 149: 567-574.
    • (2000) J. Cell Biol. , vol.149 , pp. 567-574
    • Ko, Y.-G.1    Kang, Y.-S.2    Kim, E.-K.3    Park, S.G.4    Kim, S.5
  • 8
    • 0032509304 scopus 로고    scopus 로고
    • Proofreading and aminoacylation of tRNAs before export from the nucleus
    • Lund, E. and Dahlberg, J.E. 1998. Proofreading and aminoacylation of tRNAs before export from the nucleus. Science 282: 2082-2085.
    • (1998) Science , vol.282 , pp. 2082-2085
    • Lund, E.1    Dahlberg, J.E.2
  • 9
    • 0025930249 scopus 로고
    • Aminoacyl-tRNA synthetase family from prokaryotes and eukaryotes: Structural domains and their implications
    • Mirande, M. 1991. Aminoacyl-tRNA synthetase family from prokaryotes and eukaryotes: Structural domains and their implications. Prog. Nucleic Acid Res. Mol. Biol. 40: 95-142.
    • (1991) Prog. Nucleic Acid Res. Mol. Biol. , vol.40 , pp. 95-142
    • Mirande, M.1
  • 10
    • 0034644704 scopus 로고    scopus 로고
    • Active aminoacyl-tRNA synthetases are present in nuclei as a high molecular weight multienzyme complex
    • Nathanson, L. and Deutscher, M.P. 2000. Active aminoacyl-tRNA synthetases are present in nuclei as a high molecular weight multienzyme complex. J. Biol. Chem. 275: 31559-31562.
    • (2000) J. Biol. Chem. , vol.275 , pp. 31559-31562
    • Nathanson, L.1    Deutscher, M.P.2
  • 11
    • 0024419067 scopus 로고
    • Isolation and electron microscopic characterization of the high molecular mass aminoacyl-tRNA synthetase complex from murine erythroleukemia cells
    • Norcum, M.T. 1989. Isolation and electron microscopic characterization of the high molecular mass aminoacyl-tRNA synthetase complex from murine erythroleukemia cells. J. Biol. Chem 264: 15043-15051.
    • (1989) J. Biol. Chem. , vol.264 , pp. 15043-15051
    • Norcum, M.T.1
  • 12
    • 0025883651 scopus 로고
    • Structural analysis of the high molecular mass aminoacyl-tRNA synthetase complex: Effects of neutral salts and detergents
    • -. 1991. Structural analysis of the high molecular mass aminoacyl-tRNA synthetase complex: Effects of neutral salts and detergents. J. Biol. Chem. 266: 15398-15405.
    • (1991) J. Biol. Chem. , vol.266 , pp. 15398-15405
  • 13
    • 0037070188 scopus 로고    scopus 로고
    • Three-dimensional architecture of the eukaryotic multisynthetase complex determined from negatively stained and cryoelectron micrographs
    • Norcum, M.T. and Boisset, N. 2002. Three-dimensional architecture of the eukaryotic multisynthetase complex determined from negatively stained and cryoelectron micrographs. FEBS Lett. 512: 298-302.
    • (2002) FEBS Lett. , vol.512 , pp. 298-302
    • Norcum, M.T.1    Boisset, N.2
  • 14
    • 0031939704 scopus 로고    scopus 로고
    • Structural analysis of the multienzyme aminoacyl-tRNA synthetase complex: A three domain model based on reversible crosslinking
    • Norcum, M.T. and Warrington, J.A. 1998. Structural analysis of the multienzyme aminoacyl-tRNA synthetase complex: A three domain model based on reversible crosslinking. Protein Sci. 7: 79-87.
    • (1998) Protein Sci. , vol.7 , pp. 79-87
    • Norcum, M.T.1    Warrington, J.A.2
  • 15
    • 0034674708 scopus 로고    scopus 로고
    • The cytokine portion of p43 occupies a central position within the eukaryotic multisynthetase complex
    • -. 2000. The cytokine portion of p43 occupies a central position within the eukaryotic multisynthetase complex. J. Biol. Chem. 275: 17921-17924.
    • (2000) J. Biol. Chem. , vol.275 , pp. 17921-17924
  • 17
    • 0030583549 scopus 로고    scopus 로고
    • The p18 component of the multisynthetase complex shares a protein motif with the β and γ subunits of eukaryotic elongation factor 1
    • Quevillon, S. and Mirande, M. 1996. The p18 component of the multisynthetase complex shares a protein motif with the β and γ subunits of eukaryotic elongation factor 1. FEBS Lett. 395: 63-67.
    • (1996) FEBS Lett. , vol.395 , pp. 63-67
    • Quevillon, S.1    Mirande, M.2
  • 18
    • 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. 1997. 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: 32573-32579.
    • (1997) J. Biol. Chem. , vol.272 , pp. 32573-32579
    • Quevillon, S.1    Agou, F.2    Robinson, J.-C.3    Mirande, M.4
  • 19
    • 0034671360 scopus 로고    scopus 로고
    • Macromolecular assemblage of aminoacyl-tRNA synthetases: Quantitative analysis of protein-protein interactions and mechanism of complex assembly
    • Robinson, J.-C., Kerjan, P., and Mirande, M. 2000. Macromolecular assemblage of aminoacyl-tRNA synthetases: Quantitative analysis of protein-protein interactions and mechanism of complex assembly. J. Mol. Biol. 304: 983-994.
    • (2000) J. Mol. Biol. , vol.304 , pp. 983-994
    • Robinson, J.-C.1    Kerjan, P.2    Mirande, M.3
  • 20
    • 0033613143 scopus 로고    scopus 로고
    • Caspase activation: The induced-proximity model
    • Salvesen, G.S. and Dixit, V.M. 1999. Caspase activation: The induced-proximity model Proc. Natl. Acad. Sci. 96: 10964-10967.
    • (1999) Proc. Natl. Acad. Sci. , vol.96 , pp. 10964-10967
    • Salvesen, G.S.1    Dixit, V.M.2
  • 21
    • 0032921877 scopus 로고    scopus 로고
    • Getting tRNA synthetases into the nucleus
    • Schimmel, P. and Wang, C.-C. 1999. Getting tRNA synthetases into the nucleus. Trends Biochem. Sci. 24: 127-128.
    • (1999) Trends Biochem. Sci. , vol.24 , pp. 127-128
    • Schimmel, P.1    Wang, C.-C.2
  • 22
    • 0035968226 scopus 로고    scopus 로고
    • The EMAPII cytokine is released from the mammalian multisynthetase complex after cleavage of its p43/proEMAPII component
    • Shalak, V., Kaminska, M., Mitnacht-Kraus, R., Vandenabeele, P., Clauss, M., and Mirande, M. 2001. The EMAPII cytokine is released from the mammalian multisynthetase complex after cleavage of its p43/proEMAPII component. J. Biol. Chem. 276: 23769-23776.
    • (2001) J. Biol. Chem. , vol.276 , pp. 23769-23776
    • Shalak, V.1    Kaminska, M.2    Mitnacht-Kraus, R.3    Vandenabeele, P.4    Clauss, M.5    Mirande, M.6
  • 24
    • 0032935863 scopus 로고    scopus 로고
    • The trials and travels of tRNA
    • Wolin, S.L., and Matera, A.G. 1999. The trials and travels of tRNA. Genes & Dev. 13: 1-10.
    • (1999) Genes & Dev. , vol.13 , pp. 1-10
    • Wolin, S.L.1    Matera, A.G.2
  • 25
    • 0029687712 scopus 로고    scopus 로고
    • Mammalian aminoacyl-tRNA synthetases
    • Yang, D.C.H. 1996. Mammalian aminoacyl-tRNA synthetases. Curr. Top. Cell Reg. 34: 101-136.
    • (1996) Curr. Top. Cell Reg. , vol.34 , pp. 101-136
    • Yang, D.C.H.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.