메뉴 건너뛰기




Volumn 242, Issue 4, 1994, Pages 599-603

An alternative splicing modifies the C-terminal end of tryptophanyl-tRNA synthetase in murine embryonic stem cells

Author keywords

Alternative splicing; Aminoacyl tRNA synthetase; Mammals; Post translational processing; Protein targeting

Indexed keywords


EID: 0028075594     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1994.1608     Document Type: Article
Times cited : (21)

References (23)
  • 1
    • 0026508829 scopus 로고
    • Molecular cloning and characterization of an interferon induced human c DNA with sequence homology to a mammalian peptide chain release factor
    • Buwitt, U., Flohr, T. & Bottger, E. C. (1992). Molecular cloning and characterization of an interferon induced human c DNA with sequence homology to a mammalian peptide chain release factor. EMBO J. 11, 489-496.
    • (1992) EMBO J , vol.11 , pp. 489-496
    • Buwitt, U.1    Flohr, T.2    Bottger, E.C.3
  • 2
    • 0018639079 scopus 로고
    • Isolation of biologically active ribonucleic acids from sources enriched in ribonucleases
    • Chirgwin, J. M., Przybyla, A. E., Mac-Donald, R. J. & Rutter, W J. (1979). Isolation of biologically active ribonucleic acids from sources enriched in ribonucleases. Biochemistry, 18, 5294-5299.
    • (1979) Biochemistry , vol.18 , pp. 5294-5299
    • Chirgwin, J.M.1    Przybyla, A.E.2    Mac-Donald, R.J.3    Rutter, W.J.4
  • 3
    • 0026735063 scopus 로고
    • Protein isoprenylation and méthylation at carboxyl-terminal cysteine residues
    • Clarke, S. (1992). Protein isoprenylation and méthylation at carboxyl-terminal cysteine residues. Annu. Rev. Biochem. 61, 335-386.
    • (1992) Annu. Rev. Biochem. , vol.61 , pp. 335-386
    • Clarke, S.1
  • 4
    • 0025365655 scopus 로고
    • Does protein phosphorylation play a role in translational control by eukaryotic ami noacyl-t RN A synthetases
    • Clemens, M. J. (1990). Does protein phosphorylation play a role in translational control by eukaryotic ami noacyl-t RN A synthetases. Trends Biochem. Sci. 15, 172-175.
    • (1990) Trends Biochem. Sci. , vol.15 , pp. 172-175
    • Clemens, M.J.1
  • 5
    • 0017288293 scopus 로고
    • Limited proteolysis of tryptophanyl-t RNA synthetase from beef pancreas
    • Epely, S., Gros, C., Labouesse, J. & Lemaire, G. (1976). Limited proteolysis of tryptophanyl-t RNA synthetase from beef pancreas. Eur. J. Biochem. 61, 139-146.
    • (1976) Eur. J. Biochem. , vol.61 , pp. 139-146
    • Epely, S.1    Gros, C.2    Labouesse, J.3    Lemaire, G.4
  • 6
    • 0025158208 scopus 로고
    • Partition of t RNA synthetases into two classes based on mutually exclusive sets of sequence motifs
    • Eriani, G., Delarue, M., Poch, O., Gangloff, J. & Moras, D. (1990). Partition of t RNA synthetases into two classes based on mutually exclusive sets of sequence motifs. Nature (London) 347, 203-206.
    • (1990) Nature (London) , vol.347 , pp. 203-206
    • Eriani, G.1    Delarue, M.2    Poch, O.3    Gangloff, J.4    Moras, D.5
  • 7
    • 0026348958 scopus 로고
    • Human interferon y potently induces the synthesis of a 55-k Da protein highly homologous to rabbit peptide chain release factor and bovine tryptophanyl-t RNA synthetase
    • Fleckner, J., Rasmussen, H. H. & Justesen, J. (1991). Human interferon y potently induces the synthesis of a 55-k Da protein highly homologous to rabbit peptide chain release factor and bovine tryptophanyl-t RNA synthetase. Proc. Nat. Acad. Sci., U.S.A. 88, 11520-11524.
    • (1991) Proc. Nat. Acad. Sci., U.S.A. , vol.88 , pp. 11520-11524
    • Fleckner, J.1    Rasmussen, H.H.2    Justesen, J.3
  • 8
    • 0026351552 scopus 로고
    • Cloning and nucleotide sequence of the structural gene encoding for human tryptophanyl-t RNA synthetase
    • Frolova L. Y., Grigorieva A. Y., Sudomoina M. A., Zinovieva O. L. & Kisselev L. L. (1991). Cloning and nucleotide sequence of the structural gene encoding for human tryptophanyl-t RNA synthetase. Gene, 109, 291-296.
    • (1991) Gene , vol.109 , pp. 291-296
    • Frolova, L.Y.1    Grigorieva, A.Y.2    Sudomoina, M.A.3    Zinovieva, O.L.4    Kisselev, L.L.5
  • 9
    • 0027289072 scopus 로고
    • The human gene encoding tryptophanyl-t RNA synthetase, interferon response elements and intron-exon organisation
    • Frolova L. Y., Grigorieva A. Y., Sudomoina M. A. & Kisselev L. L. (1993). The human gene encoding tryptophanyl-t RNA synthetase, interferon response elements and intron-exon organisation. Gene, 128, 237-245.
    • (1993) Gene , vol.128 , pp. 237-245
    • Frolova, L.Y.1    Grigorieva, A.Y.2    Sudomoina, M.A.3    Kisselev, L.L.4
  • 10
    • 85027670683 scopus 로고
    • Activity patterns of ami noacyl-t RNA synthetases, t RNA methylases, arginyl tranferase and tubulin during aging
    • Gabius, H. J., Graupner, G. & Cramer, F (1983). Activity patterns of ami noacyl-t RNA synthetases, t RNA methylases, arginyl tranferase and tubulin during aging in Caenorhabditis elegans. Eur. J. Biochem. 131, 213-234.
    • (1983) Caenorhabditis Elegans. Eur. J. Biochem , vol.131 , pp. 213-234
    • Gabius, H.J.1    Graupner, G.2    Cramer, F.3
  • 12
    • 0025787954 scopus 로고
    • Biochemical mechanisms of constitutive and regulated pre-m RNA splicing
    • Green, M. R. (1991). Biochemical mechanisms of constitutive and regulated pre-m RNA splicing. Annu. Rev. Cell Biol. 7, 559-599.
    • (1991) Annu. Rev. Cell Biol. , vol.7 , pp. 559-599
    • Green, M.R.1
  • 13
    • 0025892208 scopus 로고
    • The Neurospora mitochondrial tyrosyl-t RNA synthetase is sufficient for group O intron splicing in vitro and uses the carboxy terminal t RNA binding domain along with other regions
    • Kittle, J. D., Mohr, G., Gianelos, J. A., Wang, H. & Lombowitz A. M. (1991). The Neurospora mitochondrial tyrosyl-t RNA synthetase is sufficient for group O intron splicing in vitro and uses the carboxy terminal t RNA binding domain along with other regions. Gene Develop. 5, 1009-1021.
    • (1991) Gene Develop , vol.5 , pp. 1009-1021
    • Kittle, J.D.1    Mohr, G.2    Gianelos, J.A.3    Wang, H.4    Lombowitz, A.M.5
  • 15
    • 0027471431 scopus 로고
    • Purification of glutaminyl-t RNA synthetase from Saccharomyces cerevisiae—a monomeric Aa RS with a large and dispensable NH2-terminal domain
    • 2-terminal domain. J. Biol. Chem. 268, 5519-5523.
    • (1993) J. Biol. Chem. , vol.268 , pp. 5519-5523
    • Ludmerer, S.W.1    Wright, D.J.2    Schimmel, E.3
  • 16
    • 0027284950 scopus 로고
    • Protein prenylation: A mediator of protein-protein interactions
    • Marshal, C. J. (1993). Protein prenylation: a mediator of protein-protein interactions. Science, 259, 1865-1866.
    • (1993) Science , vol.259 , pp. 1865-1866
    • Marshal, C.J.1
  • 17
    • 0026749541 scopus 로고
    • Alternative RNA splicing
    • McKeown, M. (1992). Alternative RNA splicing. Annu. Rev. Cell. Biol. 8, 133-155.
    • (1992) Annu. Rev. Cell. Biol , vol.8 , pp. 133-155
    • McKeown, M.1
  • 18
    • 0025930249 scopus 로고
    • Aminoacyl-t RNA synthetase family from prokaryotes and eukaryotes: Structural domains and their implication
    • Mirande, M. (1991). Aminoacyl-t RNA synthetase family from prokaryotes and eukaryotes: structural domains and their implication. Prog. Nucl. Acid. Res. 40, 95-124.
    • (1991) Prog. Nucl. Acid. Res. , vol.40 , pp. 95-124
    • Mirande, M.1
  • 19
    • 0026343599 scopus 로고
    • Interferon induces tryptophanyl-t RNA synthetase expression in human fibroblasts
    • Rubin, B. Y., Anderson, S. L., Xing, L., Powel, R. J. & Tate, W E (1991). Interferon induces tryptophanyl-t RNA synthetase expression in human fibroblasts. J. Biol. Chem. 266, 24245-24248.
    • (1991) J. Biol. Chem. , vol.266 , pp. 24245-24248
    • Rubin, B.Y.1    Erson, S.L.2    Xing, L.3    Powel, R.J.4    Tate, W.E.5
  • 23
    • 0028766128 scopus 로고
    • RNA: Deviants or emissaries
    • Wickens, M. & Takayama, K. (1994) RNA: deviants or emissaries. Nature (London), 367, 17-18.
    • (1994) Nature (London) , vol.367 , pp. 17-18
    • Wickens, M.1    Takayama, K.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.