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Volumn 63, Issue 4, 1999, Pages 666-671

Expression of elongation factor 1β′ in escherichia coli and its interaction with elongation factor 1α from silk gland

Author keywords

Bombyx mori; Elongation factor 1 ; Elongation factor 1 ; Glutathione S transferase (GST) fusion protein; Subunit interaction

Indexed keywords

COMPLEMENTARY DNA; ELONGATION FACTOR; ELONGATION FACTOR 1; GUANINE NUCLEOTIDE;

EID: 0033111657     PISSN: 09168451     EISSN: 13476947     Source Type: Journal    
DOI: 10.1271/bbb.63.666     Document Type: Article
Times cited : (5)

References (18)
  • 1
    • 0018269922 scopus 로고
    • Exchangeability of silk gland elongation factor lß and pig liver elongation factor β in polypeptide chain elongation
    • Ejiri, S., Naoki, Y., Murakami, K., and Katsumata, T., Exchangeability of silk gland elongation factor lß and pig liver elongation factor β in polypeptide chain elongation. FEBS Lett., 95, 277-280 (1978).
    • (1978) FEBS Lett. , vol.95 , pp. 277-280
    • Ejiri, S.1    Naoki, Y.2    Murakami, K.3    Katsumata, T.4
  • 3
    • 0030771126 scopus 로고    scopus 로고
    • The PROSITE database, its status in 1997
    • Bairoch, A., Bucher, P., Hofman, K., The PROSITE database, its status in 1997. Nucleic Acids Res., 25, 217-221 (1997).
    • (1997) Nucleic Acids Res. , vol.25 , pp. 217-221
    • Bairoch, A.1    Bucher, P.2    Hofman, K.3
  • 4
    • 0025158139 scopus 로고
    • Elongation factor 1β of Artemia: Localization of functional sites and homology to elongation factor IS. Biochim. Biophys
    • van Damme, H. T. F., Amons, R., Karssies, R., Timmers, C. J., Janssen, G. M. C., and Möller, W., Elongation factor 1β of Artemia: localization of functional sites and homology to elongation factor IS. Biochim. Biophys. Acta, 1050, 241-247 (1990).
    • (1990) Acta , vol.1050 , pp. 241-247
    • Van Damme, H.T.F.1    Amons, R.2    Karssies, R.3    Timmers, C.J.4    Janssen, G.M.C.5    Möller, W.6
  • 5
    • 0025805898 scopus 로고
    • Mapping the functional domains of the eukaryotic elongation factor 1 β
    • van Damme, H. T. F., Amons, R., Janssen, G. M. C., and Möller, W., Mapping the functional domains of the eukaryotic elongation factor 1 β. Eur. J. Biochem., 197, 505-511 (1991).
    • (1991) Eur. J. Biochem. , vol.197 , pp. 505-511
    • Van Damme, H.T.F.1    Amons, R.2    Janssen, G.M.C.3    Möller, W.4
  • 6
    • 0028314690 scopus 로고
    • Interactions among four subunits of elongation factor 1 from rice embryo
    • Ejiri, S., Kawamura, R., and Katsumata, T., Interactions among four subunits of elongation factor 1 from rice embryo. Biochim. Biophys. Acta, 1217, 266-272 (1994).
    • (1994) Biochim. Biophys. Acta , vol.1217 , pp. 266-272
    • Ejiri, S.1    Kawamura, R.2    Katsumata, T.3
  • 7
    • 0031467125 scopus 로고    scopus 로고
    • Recombinant Subunits of Mammalian elongation factor 1 expressed in Escherichia coli
    • Sheu, S., and Traugh, J. A., Recombinant Subunits of Mammalian elongation factor 1 expressed in Escherichia coli. J. Biol. Chem., 272, 33290-33297 (1997).
    • (1997) J. Biol. Chem. , vol.272 , pp. 33290-33297
    • Sheu, S.1    Traugh, J.A.2
  • 8
    • 0026691915 scopus 로고
    • Identification of the sites in the eukaryotic elongation factor la involved in the binding of elongation factor iß and aminoacyl-tRNA
    • van Damme, H. T. F., Amons, R., and Möller, W., Identification of the sites in the eukaryotic elongation factor la involved in the binding of elongation factor iß and aminoacyl-tRNA. Eur. J. Biochem., 207, 1025-1034 (1992).
    • (1992) Eur. J. Biochem. , vol.207 , pp. 1025-1034
    • Van Damme, H.T.F.1    Amons, R.2    Möller, W.3
  • 9
    • 0028142290 scopus 로고
    • The leucine-zipper in elongation factor EF-1δ, a guanine-nucleotide exchange protein, is conserved in Artemia and Xenopus
    • Amons, R., Guerrucci, M. A., Karssies, R. H., Morales, J., Cormier, P., Möller, W., and Belle, R., The leucine-zipper in elongation factor EF-1δ, a guanine-nucleotide exchange protein, is conserved in Artemia and Xenopus. Biochim. Biophys. Acta, 1218, 346-350 (1994).
    • (1994) Biochim. Biophys. Acta , vol.1218 , pp. 346-350
    • Amons, R.1    Guerrucci, M.A.2    Karssies, R.H.3    Morales, J.4    Cormier, P.5    Möller, W.6    Belle, R.7
  • 12
    • 14744279005 scopus 로고
    • Protocols for cloning and analysis of blunt-ended PCR-generated DNA fragment. PCR methods and Applications
    • Costa, G. L., and Weiner, M. P., Protocols for cloning and analysis of blunt-ended PCR-generated DNA fragment. PCR methods and Applications, Manual Supplement, S95-S106 (1994).
    • (1994) Manual Supplement , pp. S95-S106
    • Costa, G.L.1    Weiner, M.P.2
  • 13
    • 0023806075 scopus 로고
    • Single-step purification of polypeptides expressed in Escherichia coli as fusions with glutathione S-transferase
    • Smith, D. B., and Johnson, K. S., Single-step purification of polypeptides expressed in Escherichia coli as fusions with glutathione S-transferase. Gene, 67, 31-40 (1988).
    • (1988) Gene , vol.67 , pp. 31-40
    • Smith, D.B.1    Johnson, K.S.2
  • 14
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K., Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature, 227, 680-685 (1970).
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 15
    • 0002751371 scopus 로고
    • Purification and characterization of polypeptide chain elongation factor 1 from plants
    • Ejiri, S., Purification and characterization of polypeptide chain elongation factor 1 from plants. Methods in Enzymology, 118, 140-153 (1986).
    • (1986) Methods in Enzymology , vol.118 , pp. 140-153
    • Ejiri, S.1
  • 16
    • 0017688569 scopus 로고
    • Purification and properties of polypeptide chain elongation factor-1/Iy from pig liver
    • Motoyoshi, K., Iwasaki, K., and Kaziro, Y., Purification and properties of polypeptide chain elongation factor-1/Iy from pig liver. J Biochem., 82, 145-155 (1977).
    • (1977) J Biochem. , vol.82 , pp. 145-155
    • Motoyoshi, K.1    Iwasaki, K.2    Kaziro, Y.3
  • 17
    • 0030025671 scopus 로고    scopus 로고
    • The structure of the Escherichia coli EF-Tu-EF-Ts complex at 2.5 A resolution
    • Kawashima, T., Berthet Colominas, C., Wulff, M., Cusack, S., and Leberman, R., The structure of the Escherichia coli EF-Tu-EF-Ts complex at 2.5 A resolution. Nature, 379, 511-518 (1996).
    • (1996) Nature , vol.379 , pp. 511-518
    • Kawashima, T.1    Berthet Colominas, C.2    Wulff, M.3    Cusack, S.4    Leberman, R.5
  • 18
    • 0032549076 scopus 로고    scopus 로고
    • Mutational analysis of the roles of residues in Escherichia coli elongation factor Ts in the interaction with elongation factor Tu
    • Zhang, Y., Yu, N., and Spremulli, L. L., Mutational analysis of the roles of residues in Escherichia coli elongation factor Ts in the interaction with elongation factor Tu. J. Biol. Chem., 273, 4556-4562 (1998).
    • (1998) J. Biol. Chem. , vol.273 , pp. 4556-4562
    • Zhang, Y.1    Yu, N.2    Spremulli, L.L.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.