메뉴 건너뛰기




Volumn 263, Issue 3, 1999, Pages 806-816

p55-hGRF, a short natural form of the Ras-GDP exchange factor. High yield production and characterization

Author keywords

Dimerization; Guanine nucleotide exchange factor; P21 Ras; Protein protein interaction; Renaturation

Indexed keywords

DIMER; GUANINE NUCLEOTIDE EXCHANGE FACTOR; PEPTIDE FRAGMENT; PROTEIN P21; PROTEIN P39; PROTEIN P55; RAS PROTEIN; RECOMBINANT PROTEIN; UNCLASSIFIED DRUG;

EID: 0033178902     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1432-1327.1999.00558.x     Document Type: Article
Times cited : (1)

References (41)
  • 1
    • 0025010979 scopus 로고
    • The GTPase superfamily: A conserved switch for diverse cell functions
    • 1. Bourne, H.R., Sanders, D.A. & McCormick, F. (1990) The GTPase superfamily: a conserved switch for diverse cell functions. Nature (London) 348, 125-132.
    • (1990) Nature (London) , vol.348 , pp. 125-132
    • Bourne, H.R.1    Sanders, D.A.2    McCormick, F.3
  • 2
    • 0025838675 scopus 로고
    • Regulators and effectors of ras proteins
    • 2. Bollag, G. & McCormick, F. (1991) Regulators and effectors of ras proteins. Annu. Rev. Cell. Biol. 7, 601-632.
    • (1991) Annu. Rev. Cell. Biol. , vol.7 , pp. 601-632
    • Bollag, G.1    McCormick, F.2
  • 3
    • 0026063120 scopus 로고
    • GTPase domains of ras p21 oncogene protein and elongation factor Tu: Analysis of three-dimensional structures, sequence families, and functional sites
    • 3. Valencia, A., Kjeldgaard, M., Pai, E.F. & Sander, C. (1991) GTPase domains of ras p21 oncogene protein and elongation factor Tu: analysis of three-dimensional structures, sequence families, and functional sites. Proc. Natl Acad. Sci. USA 88, 5443-5447.
    • (1991) Proc. Natl Acad. Sci. USA , vol.88 , pp. 5443-5447
    • Valencia, A.1    Kjeldgaard, M.2    Pai, E.F.3    Sander, C.4
  • 5
    • 0029156702 scopus 로고
    • Molecular dynamic simulation of the solution structures of Ha-ras-p21 GDP and GTP complexes: Flexibility, possible hinges, and levers of the conformational transition
    • 5. Diaz, J.F., Wroblowski, B. & Engelborghs, Y. (1995) Molecular dynamic simulation of the solution structures of Ha-ras-p21 GDP and GTP complexes: flexibility, possible hinges, and levers of the conformational transition. Biochemistry 34, 12038-12047.
    • (1995) Biochemistry , vol.34 , pp. 12038-12047
    • Diaz, J.F.1    Wroblowski, B.2    Engelborghs, Y.3
  • 6
    • 0025117674 scopus 로고
    • Molecular switch for signal transduction: Structural differences between active and inactive forms of protooncogenic ras proteins
    • 6. Milburn, M.V., Tong, L., DeVos, A.M., Brünger, A., Yamaizumi, Z., Nishimura, S. & Kim, S.H. (1990) Molecular switch for signal transduction: structural differences between active and inactive forms of protooncogenic ras proteins. Science 247, 939-945.
    • (1990) Science , vol.247 , pp. 939-945
    • Milburn, M.V.1    Tong, L.2    DeVos, A.M.3    Brünger, A.4    Yamaizumi, Z.5    Nishimura, S.6    Kim, S.H.7
  • 7
    • 0026474955 scopus 로고
    • NMR studies of the conformational change in human N-p21 ras produced by replacement of bound GDP with the GTP analog GTPγS
    • 7. Miller, A.F., Papastavros, M.Z. & Redfield, A.G. (1992) NMR studies of the conformational change in human N-p21 ras produced by replacement of bound GDP with the GTP analog GTPγS. Biochemistry 31, 10208-10216.
    • (1992) Biochemistry , vol.31 , pp. 10208-10216
    • Miller, A.F.1    Papastavros, M.Z.2    Redfield, A.G.3
  • 9
    • 0025740753 scopus 로고
    • The structure of Ras protein: A model for a universal molecular switch
    • 9. Wittinghofer, A. & Pai, E.F. (1991) The structure of Ras protein: a model for a universal molecular switch. Trends Biochem. Sci. 16, 382-387.
    • (1991) Trends Biochem. Sci. , vol.16 , pp. 382-387
    • Wittinghofer, A.1    Pai, E.F.2
  • 10
    • 0028895654 scopus 로고
    • Modular binding domains in signal transduction proteins
    • 10. Cohen, G.B., Ren, R. & Baltimore, D. (1995) Modular binding domains in signal transduction proteins. Cell 80, 237-248.
    • (1995) Cell , vol.80 , pp. 237-248
    • Cohen, G.B.1    Ren, R.2    Baltimore, D.3
  • 11
    • 0028859279 scopus 로고
    • Protein modules and signalling networks
    • 11. Pawson, T. (1995) Protein modules and signalling networks. Nature (London) 373, 573-580.
    • (1995) Nature (London) , vol.373 , pp. 573-580
    • Pawson, T.1
  • 14
    • 0027502176 scopus 로고
    • Influence of guanine nucleotides on complex formation between Ras and CDC25 proteins
    • 14. Lai, C.C., Boguski, M., Broek, D. & Powers, S. (1993) Influence of guanine nucleotides on complex formation between Ras and CDC25 proteins. Mol. Cell. Biol. 13, 1345-1352.
    • (1993) Mol. Cell. Biol. , vol.13 , pp. 1345-1352
    • Lai, C.C.1    Boguski, M.2    Broek, D.3    Powers, S.4
  • 15
    • 0030996229 scopus 로고    scopus 로고
    • The N-terminal moiety of CDC25 (Mm), a GDP/GTP exchange factor of Ras proteins, controls the activity of the catalytic domain - Modulation by calmodulin and calpain
    • 15. Baouz, S., Jacquet, E., Bernardi, A. & Parmeggiani, A. (1997) The N-terminal moiety of CDC25 (Mm), a GDP/GTP exchange factor of Ras proteins, controls the activity of the catalytic domain -Modulation by calmodulin and calpain. J. Biol. Chem. 272, 6671-6676.
    • (1997) J. Biol. Chem. , vol.272 , pp. 6671-6676
    • Baouz, S.1    Jacquet, E.2    Bernardi, A.3    Parmeggiani, A.4
  • 17
    • 0030584674 scopus 로고    scopus 로고
    • Electrostatic control of GTP and GDP binding in the oncoprotein p21 (ras)
    • 17. Muegge, I., Schweins, T., Langen, R. & Warshel, A. (1996) Electrostatic control of GTP and GDP binding in the oncoprotein p21 (ras). Structure 4, 475-489.
    • (1996) Structure , vol.4 , pp. 475-489
    • Muegge, I.1    Schweins, T.2    Langen, R.3    Warshel, A.4
  • 19
    • 0029865523 scopus 로고    scopus 로고
    • Expression of alternative forms of Ras exchange factors GRF and SOS1 in different human tissues and cell lines
    • 19. Guerrero, C., Rojas, J.M., Chedid, M., Esteban, L.M., Zimonjic, D.B., Popescu, N.C., Demora, J.F. & Santos, E. (1996) Expression of alternative forms of Ras exchange factors GRF and SOS1 in different human tissues and cell lines. Oncogene 12, 1097-1107.
    • (1996) Oncogene , vol.12 , pp. 1097-1107
    • Guerrero, C.1    Rojas, J.M.2    Chedid, M.3    Esteban, L.M.4    Zimonjic, D.B.5    Popescu, N.C.6    Demora, J.F.7    Santos, E.8
  • 21
    • 0028564740 scopus 로고
    • GEF, which regulates the function of Ras
    • GEF, which regulates the function of Ras. Gene 151, 279-284.
    • (1994) Gene , vol.151 , pp. 279-284
    • Wei, W.1    Das, B.2    Park, W.3    Broek, D.4
  • 22
    • 0032170276 scopus 로고    scopus 로고
    • To fear or not to fear: What was the question? A potential role for Ras-GRF in memory
    • 22. Finkbeiner, S. & Dalva, M.B. (1998) To fear or not to fear: what was the question? A potential role for Ras-GRF in memory. Bioessays 20, 691-695.
    • (1998) Bioessays , vol.20 , pp. 691-695
    • Finkbeiner, S.1    Dalva, M.B.2
  • 24
    • 0009642331 scopus 로고
    • Gel electrophoresis under denaturing conditions
    • Wiley-Liss, Inc., New York
    • 24. Bollag, D.M. & Edelstein, S.J. (1992) Gel electrophoresis under denaturing conditions. In Protein Methods, pp. 95-142. Wiley-Liss, Inc., New York.
    • (1992) Protein Methods , pp. 95-142
    • Bollag, D.M.1    Edelstein, S.J.2
  • 25
    • 0028871804 scopus 로고
    • How to measure and predict the molar absorption coefficient of a protein
    • 25. Pace, C.N., Vajdos, F., Fee, L., Grimley, G. & Gray, T. (1995) How to measure and predict the molar absorption coefficient of a protein. Protein Sci. 4, 2411-2423.
    • (1995) Protein Sci. , vol.4 , pp. 2411-2423
    • Pace, C.N.1    Vajdos, F.2    Fee, L.3    Grimley, G.4    Gray, T.5
  • 26
    • 0028980920 scopus 로고
    • Characterization of mammalian C-CDC25 (Mm exchange factor and kinetic properties of the exchange reaction intermediate p21 center dot C-CDC25 (Mm)
    • 26. Jacquet, E., Baouz, S. & Parmeggiani, A. (1995) Characterization of mammalian C-CDC25 (Mm) exchange factor and kinetic properties of the exchange reaction intermediate p21 center dot C-CDC25 (Mm). Biochemistry 34, 12347-12354.
    • (1995) Biochemistry , vol.34 , pp. 12347-12354
    • Jacquet, E.1    Baouz, S.2    Parmeggiani, A.3
  • 28
    • 0026747656 scopus 로고
    • Boundary analysis in sedimentation transport expermiment: A procedure for obtaining sedimentation coefficient distributions using the time derivative of concentration profile
    • 28. Stafford, W.F. III (1992) Boundary analysis in sedimentation transport expermiment: a procedure for obtaining sedimentation coefficient distributions using the time derivative of concentration profile. Anal. Biochem. 203, 295-391.
    • (1992) Anal. Biochem. , vol.203 , pp. 295-391
    • Stafford W.F. III1
  • 30
    • 0031020114 scopus 로고    scopus 로고
    • Construction of hydrodynamic bead models from high-resolution X-ray crystallographic or nuclear magnetic resonance data
    • 30. Byron, O. (1997) Construction of hydrodynamic bead models from high-resolution X-ray crystallographic or nuclear magnetic resonance data. Biophys. J. 72, 408-415.
    • (1997) Biophys. J. , vol.72 , pp. 408-415
    • Byron, O.1
  • 31
    • 0023657949 scopus 로고
    • Hydrophobic cluster analysis: An efficient new way to compare and analyse amino acid sequences
    • 31. Gaboriaud, C., Bissery, V., Benchetrit, T. & Mornon, J.-P. (1987) Hydrophobic cluster analysis: an efficient new way to compare and analyse amino acid sequences. FEBS Lett. 224, 149-155.
    • (1987) FEBS Lett. , vol.224 , pp. 149-155
    • Gaboriaud, C.1    Bissery, V.2    Benchetrit, T.3    Mornon, J.-P.4
  • 32
    • 0027732538 scopus 로고
    • Proteins regulating Ras and its relatives
    • 32. Boguski, M.S. & McCormick, F. (1993) Proteins regulating Ras and its relatives. Nature (London) 366, 643-654.
    • (1993) Nature (London) , vol.366 , pp. 643-654
    • Boguski, M.S.1    McCormick, F.2
  • 34
    • 0016243318 scopus 로고
    • Theory of sedimentation for kinetically controlled dimerization reactions
    • 34. Cann, J.R. & Kege, G. (1974) Theory of sedimentation for kinetically controlled dimerization reactions. Biochemistry 13, 1868-1874.
    • (1974) Biochemistry , vol.13 , pp. 1868-1874
    • Cann, J.R.1    Kege, G.2
  • 35
    • 0024246956 scopus 로고
    • Surface, subunit interfaces and interior of oligomeric proteins
    • 35. Janin, J., Miller, S. & Chothia, C. (1988) Surface, subunit interfaces and interior of oligomeric proteins. J. Mol. Biol. 204, 155-164.
    • (1988) J. Mol. Biol. , vol.204 , pp. 155-164
    • Janin, J.1    Miller, S.2    Chothia, C.3
  • 36
    • 0032546533 scopus 로고    scopus 로고
    • Kinetic analysis by fluorescence of the interaction between Ras and the catalytic domain of the guanine nucleotide exchange factor Cdc25 (Mm)
    • 36. Lenzen, C., Cool, R.H., Prinz, H., Kuhlmann, J. & Wittinghofer, A. (1998) Kinetic analysis by fluorescence of the interaction between Ras and the catalytic domain of the guanine nucleotide exchange factor Cdc25 (Mm). Biochemistry 37, 7420-7430.
    • (1998) Biochemistry , vol.37 , pp. 7420-7430
    • Lenzen, C.1    Cool, R.H.2    Prinz, H.3    Kuhlmann, J.4    Wittinghofer, A.5
  • 37
    • 0030855008 scopus 로고    scopus 로고
    • Dimerization of Cdc25p, the guanine-nucleotide exchange factor for Ras from Saccharomyces cerevisiae, and its interaction with Sdc25p
    • 37. Camus, C., Geymonat, M., Garreau, H., Baudet-Nessler, S. & Jacquet, M. (1997) Dimerization of Cdc25p, the guanine-nucleotide exchange factor for Ras from Saccharomyces cerevisiae, and its interaction with Sdc25p. Eur J. Biochem. 247, 703-708.
    • (1997) Eur J. Biochem. , vol.247 , pp. 703-708
    • Camus, C.1    Geymonat, M.2    Garreau, H.3    Baudet-Nessler, S.4    Jacquet, M.5
  • 39
    • 0032538317 scopus 로고    scopus 로고
    • Structural basis for activation of ARF GTPase: Mechanisms of guanine nucleotide exchange and GTP-myristoyl switching
    • 39. Goldberg, J. (1998) Structural basis for activation of ARF GTPase: mechanisms of guanine nucleotide exchange and GTP-myristoyl switching. Cell 95, 237-248.
    • (1998) Cell , vol.95 , pp. 237-248
    • Goldberg, J.1
  • 41
    • 0030025671 scopus 로고    scopus 로고
    • The structure of the Escherichia coli EF-Tu. EF-Ts complex at 2.5Å resolution
    • 41. Kawashima, T., Berthet-Colominas, C., Wulff, M., Cusak, S. & Leberman, R. (1996) The structure of the Escherichia coli EF-Tu. EF-Ts complex at 2.5Å resolution. Nature (London) 379, 511-518.
    • (1996) Nature (London) , vol.379 , pp. 511-518
    • Kawashima, T.1    Berthet-Colominas, C.2    Wulff, M.3    Cusak, S.4    Leberman, R.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.