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Volumn 20, Issue 6, 2005, Pages 929-938

The SAXS solution structure of RF1 differs from its crystal structure and is similar to its ribosome bound cryo-EM structure

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL PROTEIN; PEPTIDYLTRANSFERASE; PROTEIN DERIVATIVE; RELEASE FACTOR 1 PROTEIN; RELEASE FACTOR 2 PROTEIN; TRANSLATION TERMINATION FACTOR; UNCLASSIFIED DRUG;

EID: 29144499347     PISSN: 10972765     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.molcel.2005.11.022     Document Type: Article
Times cited : (84)

References (50)
  • 1
    • 12944333197 scopus 로고    scopus 로고
    • The protein content in crystals and packing coefficients in different space groups
    • K.M. Andersson, and S. Hovmoller The protein content in crystals and packing coefficients in different space groups Acta Crystallogr. D Biol. Crystallogr. 56 2000 789 790
    • (2000) Acta Crystallogr. D Biol. Crystallogr. , vol.56 , pp. 789-790
    • Andersson, K.M.1    Hovmoller, S.2
  • 2
    • 0015028434 scopus 로고
    • Mammalian peptide chain termination. II. Codon specificity and GTPase activity of release factor
    • A.L. Beaudet, and C.T. Caskey Mammalian peptide chain termination. II. Codon specificity and GTPase activity of release factor Proc. Natl. Acad. Sci. USA 68 1971 619 624
    • (1971) Proc. Natl. Acad. Sci. USA , vol.68 , pp. 619-624
    • Beaudet, A.L.1    Caskey, C.T.2
  • 6
    • 0034672060 scopus 로고    scopus 로고
    • A post-translational modification in the GGQ motif of RF2 from Escherichia coli stimulates termination of translation
    • V. Dincbas-Renqvist, A. Engstrom, L. Mora, V. Heurgue-Hamard, R. Buckingham, and M. Ehrenberg A post-translational modification in the GGQ motif of RF2 from Escherichia coli stimulates termination of translation EMBO J. 19 2000 6900 6907
    • (2000) EMBO J. , vol.19 , pp. 6900-6907
    • Dincbas-Renqvist, V.1    Engstrom, A.2    Mora, L.3    Heurgue-Hamard, V.4    Buckingham, R.5    Ehrenberg, M.6
  • 7
    • 0021370660 scopus 로고
    • Costs of accuracy determined by a maximal growth rate constraint
    • M. Ehrenberg, and C.G. Kurland Costs of accuracy determined by a maximal growth rate constraint Q. Rev. Biophys. 17 1984 45 82
    • (1984) Q. Rev. Biophys. , vol.17 , pp. 45-82
    • Ehrenberg, M.1    Kurland, C.G.2
  • 9
    • 0030949960 scopus 로고    scopus 로고
    • Release factor RF3 in E. coli accelerates the dissociation of release factors RF1 and RF2 from the ribosome in a GTP-dependent manner
    • D.V. Freistroffer, M.Y. Pavlov, J. MacDougall, R.H. Buckingham, and M. Ehrenberg Release factor RF3 in E. coli accelerates the dissociation of release factors RF1 and RF2 from the ribosome in a GTP-dependent manner EMBO J. 16 1997 4126 4133
    • (1997) EMBO J. , vol.16 , pp. 4126-4133
    • Freistroffer, D.V.1    Pavlov, M.Y.2    MacDougall, J.3    Buckingham, R.H.4    Ehrenberg, M.5
  • 11
    • 0032840382 scopus 로고    scopus 로고
    • Mutations in the highly conserved GGQ motif of class 1 polypeptide release factors abolish ability of human eRF1 to trigger peptidyl-tRNA hydrolysis
    • L.Y. Frolova, R.Y. Tsivkovskii, G.F. Sivolobova, N.Y. Oparina, O.I. Serpinsky, V.M. Blinov, S.I. Tatkov, and L.L. Kisselev Mutations in the highly conserved GGQ motif of class 1 polypeptide release factors abolish ability of human eRF1 to trigger peptidyl-tRNA hydrolysis RNA 5 1999 1014 1020
    • (1999) RNA , vol.5 , pp. 1014-1020
    • Frolova, L.Y.1    Tsivkovskii, R.Y.2    Sivolobova, G.F.3    Oparina, N.Y.4    Serpinsky, O.I.5    Blinov, V.M.6    Tatkov, S.I.7    Kisselev, L.L.8
  • 12
    • 0036216442 scopus 로고    scopus 로고
    • Highly conserved NIKS tetrapeptide is functionally essential in eukaryotic translation termination factor eRF1
    • L. Frolova, A. Seit-Nebi, and L. Kisselev Highly conserved NIKS tetrapeptide is functionally essential in eukaryotic translation termination factor eRF1 RNA 8 2002 129 136
    • (2002) RNA , vol.8 , pp. 129-136
    • Frolova, L.1    Seit-Nebi, A.2    Kisselev, L.3
  • 15
    • 0037084101 scopus 로고    scopus 로고
    • The hemK gene in Escherichia coli encodes the N(5)-glutamine methyltransferase that modifies peptide release factors
    • V. Heurgue-Hamard, S. Champ, A. Engstrom, M. Ehrenberg, and R.H. Buckingham The hemK gene in Escherichia coli encodes the N(5)-glutamine methyltransferase that modifies peptide release factors EMBO J. 21 2002 769 778
    • (2002) EMBO J. , vol.21 , pp. 769-778
    • Heurgue-Hamard, V.1    Champ, S.2    Engstrom, A.3    Ehrenberg, M.4    Buckingham, R.H.5
  • 16
    • 13244259475 scopus 로고    scopus 로고
    • The glutamine residue of the conserved GGQ motif in Saccharomyces cerevisiae release factor eRF1 is methylated by the product of the YDR140w gene
    • V. Heurgue-Hamard, S. Champ, L. Mora, T. Merkulova-Rainon, L.L. Kisselev, and R.H. Buckingham The glutamine residue of the conserved GGQ motif in Saccharomyces cerevisiae release factor eRF1 is methylated by the product of the YDR140w gene J. Biol. Chem. 280 2005 2439 2445
    • (2005) J. Biol. Chem. , vol.280 , pp. 2439-2445
    • Heurgue-Hamard, V.1    Champ, S.2    Mora, L.3    Merkulova-Rainon, T.4    Kisselev, L.L.5    Buckingham, R.H.6
  • 17
    • 0034628438 scopus 로고    scopus 로고
    • A tripeptide 'anticodon' deciphers stop codons in messenger RNA
    • K. Ito, M. Uno, and Y. Nakamura A tripeptide 'anticodon' deciphers stop codons in messenger RNA Nature 403 2000 680 684
    • (2000) Nature , vol.403 , pp. 680-684
    • Ito, K.1    Uno, M.2    Nakamura, Y.3
  • 18
    • 0030841587 scopus 로고    scopus 로고
    • Electron-density map interpretation
    • T.A. Jones, and M. Kjeldgaard Electron-density map interpretation Methods Enzymol. 277 1997 173 208
    • (1997) Methods Enzymol. , vol.277 , pp. 173-208
    • Jones, T.A.1    Kjeldgaard, M.2
  • 20
    • 0037439231 scopus 로고    scopus 로고
    • Termination of translation: Interplay of mRNA, rRNAs and release factors?
    • L. Kisselev, M. Ehrenberg, and L. Frolova Termination of translation: interplay of mRNA, rRNAs and release factors? EMBO J. 22 2003 175 182
    • (2003) EMBO J. , vol.22 , pp. 175-182
    • Kisselev, L.1    Ehrenberg, M.2    Frolova, L.3
  • 21
    • 0037249466 scopus 로고    scopus 로고
    • The unfolding story of polypeptide release factors
    • M. Kjeldgaard The unfolding story of polypeptide release factors Mol. Cell 11 2003 8 10
    • (2003) Mol. Cell , vol.11 , pp. 8-10
    • Kjeldgaard, M.1
  • 23
    • 0020114103 scopus 로고
    • X-ray diffraction and scattering on disordered systems using synchrotron radiation
    • M.H.J. Koch, and J. Bordas X-ray diffraction and scattering on disordered systems using synchrotron radiation Nucl. Instrum. Methods Phys. Res. A 208 1983 461 469
    • (1983) Nucl. Instrum. Methods Phys. Res. a , vol.208 , pp. 461-469
    • Koch, M.H.J.1    Bordas, J.2
  • 24
    • 0345169163 scopus 로고    scopus 로고
    • Small-angle scattering: A view on the properties, structures and structural changes of biological macromolecules in solution
    • M.H. Koch, P. Vachette, and D.I. Svergun Small-angle scattering: a view on the properties, structures and structural changes of biological macromolecules in solution Q. Rev. Biophys. 36 2003 147 227
    • (2003) Q. Rev. Biophys. , vol.36 , pp. 147-227
    • Koch, M.H.1    Vachette, P.2    Svergun, D.I.3
  • 26
    • 3242886767 scopus 로고    scopus 로고
    • Molecular morphology of eukaryotic class I translation termination factor eRF1 in solution
    • A.V. Kononenko, K.A. Dembo, L.L. Kiselev, and V.V. Volkov Molecular morphology of eukaryotic class I translation termination factor eRF1 in solution Mol. Biol. (Mosk.) 38 2004 303 311
    • (2004) Mol. Biol. (Mosk.) , vol.38 , pp. 303-311
    • Kononenko, A.V.1    Dembo, K.A.2    Kiselev, L.L.3    Volkov, V.V.4
  • 27
    • 0035124442 scopus 로고    scopus 로고
    • Automated matching of high- and low-resolution structural models
    • M.B. Kozin, and D.I. Svergun Automated matching of high- and low-resolution structural models J. Appl. Crystallogr. 34 2001 33 41
    • (2001) J. Appl. Crystallogr. , vol.34 , pp. 33-41
    • Kozin, M.B.1    Svergun, D.I.2
  • 29
    • 11144223549 scopus 로고    scopus 로고
    • Release factors eRF1 and RF2: A universal mechanism controls the large conformational changes
    • B. Ma, and R. Nussinov Release factors eRF1 and RF2: a universal mechanism controls the large conformational changes J. Biol. Chem. 279 2004 53875 53885
    • (2004) J. Biol. Chem. , vol.279 , pp. 53875-53885
    • Ma, B.1    Nussinov, R.2
  • 30
    • 0037223622 scopus 로고    scopus 로고
    • The essential role of the invariant GGQ motif in the function and stability in vivo of bacterial release factors RF1 and RF2
    • L. Mora, V. Heurgue-Hamard, S. Champ, M. Ehrenberg, L.L. Kisselev, and R.H. Buckingham The essential role of the invariant GGQ motif in the function and stability in vivo of bacterial release factors RF1 and RF2 Mol. Microbiol. 47 2003 267 275
    • (2003) Mol. Microbiol. , vol.47 , pp. 267-275
    • Mora, L.1    Heurgue-Hamard, V.2    Champ, S.3    Ehrenberg, M.4    Kisselev, L.L.5    Buckingham, R.H.6
  • 31
    • 0347517767 scopus 로고    scopus 로고
    • Stop codon recognition and interactions with peptide release factor RF3 of truncated and chimeric RF1 and RF2 from Escherichia coli
    • L. Mora, A. Zavialov, M. Ehrenberg, and R.H. Buckingham Stop codon recognition and interactions with peptide release factor RF3 of truncated and chimeric RF1 and RF2 from Escherichia coli Mol. Microbiol. 50 2003 1467 1476
    • (2003) Mol. Microbiol. , vol.50 , pp. 1467-1476
    • Mora, L.1    Zavialov, A.2    Ehrenberg, M.3    Buckingham, R.H.4
  • 32
    • 0016200132 scopus 로고
    • A semi-quantitative treatment of missense and nonsense suppression in the strA and ram ribosomal mutants of Escherichia coli. Evaluation of some molecular parameters of translation in vivo
    • J. Ninio A semi-quantitative treatment of missense and nonsense suppression in the strA and ram ribosomal mutants of Escherichia coli. Evaluation of some molecular parameters of translation in vivo J. Mol. Biol. 84 1974 297 313
    • (1974) J. Mol. Biol. , vol.84 , pp. 297-313
    • Ninio, J.1
  • 33
    • 11844261550 scopus 로고    scopus 로고
    • The N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase PrmC/HemK in Chlamydia trachomatis methylates class 1 release factors
    • Y. Pannekoek, V. Heurgue-Hamard, A.A. Langerak, D. Speijer, R.H. Buckingham, and A. van der Ende The N5-glutamine S-adenosyl-L-methionine- dependent methyltransferase PrmC/HemK in Chlamydia trachomatis methylates class 1 release factors J. Bacteriol. 187 2005 507 511
    • (2005) J. Bacteriol. , vol.187 , pp. 507-511
    • Pannekoek, Y.1    Heurgue-Hamard, V.2    Langerak, A.A.3    Speijer, D.4    Buckingham, R.H.5    Van Der Ende, A.6
  • 34
    • 23244455562 scopus 로고    scopus 로고
    • Global rigid body modeling of macromolecular complexes against small-angle scattering data
    • M.V. Petoukhov, and D.I. Svergun Global rigid body modeling of macromolecular complexes against small-angle scattering data Biophys. J. 89 2005 1237 1250
    • (2005) Biophys. J. , vol.89 , pp. 1237-1250
    • Petoukhov, M.V.1    Svergun, D.I.2
  • 37
    • 0034266465 scopus 로고    scopus 로고
    • Mutation of a glutamine residue in the universal tripeptide GGQ in human eRF1 termination factor does not cause complete loss of its activity
    • A. Seit Nebi, L. Frolova, N. Ivanova, A. Poltaraus, and L. Kiselev Mutation of a glutamine residue in the universal tripeptide GGQ in human eRF1 termination factor does not cause complete loss of its activity Mol. Biol. (Mosk.) 34 2000 899 900
    • (2000) Mol. Biol. (Mosk.) , vol.34 , pp. 899-900
    • Seit Nebi, A.1    Frolova, L.2    Ivanova, N.3    Poltaraus, A.4    Kiselev, L.5
  • 38
    • 0036747332 scopus 로고    scopus 로고
    • Conversion of omnipotent translation termination factor eRF1 into ciliate-like UGA-only unipotent eRF1
    • A. Seit-Nebi, L. Frolova, and L. Kisselev Conversion of omnipotent translation termination factor eRF1 into ciliate-like UGA-only unipotent eRF1 EMBO Rep. 3 2002 881 886
    • (2002) EMBO Rep. , vol.3 , pp. 881-886
    • Seit-Nebi, A.1    Frolova, L.2    Kisselev, L.3
  • 39
    • 4143064788 scopus 로고    scopus 로고
    • Structural analyses of peptide release factor 1 from Thermotoga maritima reveal domain flexibility required for its interaction with the ribosome
    • D.H. Shin, J. Brandsen, J. Jancarik, H. Yokota, R. Kim, and S.H. Kim Structural analyses of peptide release factor 1 from Thermotoga maritima reveal domain flexibility required for its interaction with the ribosome J. Mol. Biol. 341 2004 227 239
    • (2004) J. Mol. Biol. , vol.341 , pp. 227-239
    • Shin, D.H.1    Brandsen, J.2    Jancarik, J.3    Yokota, H.4    Kim, R.5    Kim, S.H.6
  • 40
    • 0034603210 scopus 로고    scopus 로고
    • The crystal structure of human eukaryotic release factor eRF1 - Mechanism of stop codon recognition and peptidyl-tRNA hydrolysis
    • H. Song, P. Mugnier, A.K. Das, H.M. Webb, D.R. Evans, M.F. Tuite, B.A. Hemmings, and D. Barford The crystal structure of human eukaryotic release factor eRF1 - mechanism of stop codon recognition and peptidyl-tRNA hydrolysis Cell 100 2000 311 321
    • (2000) Cell , vol.100 , pp. 311-321
    • Song, H.1    Mugnier, P.2    Das, A.K.3    Webb, H.M.4    Evans, D.R.5    Tuite, M.F.6    Hemmings, B.A.7    Barford, D.8
  • 41
    • 0016044321 scopus 로고
    • Three-dimensional structure of yeast phenylalanine transfer RNA at 3.0 angstroms resolution
    • F.L. Suddath, G.J. Quigley, A. McPherson, D. Sneden, J.J. Kim, S.H. Kim, and A. Rich Three-dimensional structure of yeast phenylalanine transfer RNA at 3.0 angstroms resolution Nature 248 1974 20 24
    • (1974) Nature , vol.248 , pp. 20-24
    • Suddath, F.L.1    Quigley, G.J.2    McPherson, A.3    Sneden, D.4    Kim, J.J.5    Kim, S.H.6    Rich, A.7
  • 42
    • 0026910457 scopus 로고
    • Determination of the regularization parameter in indirect-transform methods using perceptual criteria
    • D.I. Svergun Determination of the regularization parameter in indirect-transform methods using perceptual criteria J. Appl. Crystallogr. 25 1992 495 503
    • (1992) J. Appl. Crystallogr. , vol.25 , pp. 495-503
    • Svergun, D.I.1
  • 43
    • 0033001996 scopus 로고    scopus 로고
    • Restoring low resolution structure of biological macromolecules from solution scattering using simulated annealing
    • D.I. Svergun Restoring low resolution structure of biological macromolecules from solution scattering using simulated annealing Biophys. J. 76 1999 2879 2886
    • (1999) Biophys. J. , vol.76 , pp. 2879-2886
    • Svergun, D.I.1
  • 44
    • 84944815124 scopus 로고
    • Small-angle-scattering-data treatment by the regularization method
    • D.I. Svergun, A.V. Semenyuk, and L.A. Feigin Small-angle-scattering-data treatment by the regularization method Acta. Cryst. 44 1988 244 250
    • (1988) Acta. Cryst. , vol.44 , pp. 244-250
    • Svergun, D.I.1    Semenyuk, A.V.2    Feigin, L.A.3
  • 45
    • 0029185933 scopus 로고
    • CRYSOL - A program to evaluate X-ray solution scattering of biological macromolecules from atomic coordinates
    • D. Svergun, C. Barberato, and M.H.J. Koch CRYSOL - A program to evaluate X-ray solution scattering of biological macromolecules from atomic coordinates J. Appl. Crystallogr. 28 1995 768 773
    • (1995) J. Appl. Crystallogr. , vol.28 , pp. 768-773
    • Svergun, D.1    Barberato, C.2    Koch, M.H.J.3
  • 49
    • 0035812714 scopus 로고    scopus 로고
    • A posttermination ribosomal complex is the guanine nucleotide exchange factor for peptide release factor RF3
    • A.V. Zavialov, R.H. Buckingham, and M. Ehrenberg A posttermination ribosomal complex is the guanine nucleotide exchange factor for peptide release factor RF3 Cell 107 2001 115 124
    • (2001) Cell , vol.107 , pp. 115-124
    • Zavialov, A.V.1    Buckingham, R.H.2    Ehrenberg, M.3
  • 50
    • 0036810254 scopus 로고    scopus 로고
    • Release of peptide promoted by the GGQ motif of class 1 release factors regulates the GTPase activity of RF3
    • A.V. Zavialov, L. Mora, R.H. Buckingham, and M. Ehrenberg Release of peptide promoted by the GGQ motif of class 1 release factors regulates the GTPase activity of RF3 Mol. Cell 10 2002 789 798
    • (2002) Mol. Cell , vol.10 , pp. 789-798
    • Zavialov, A.V.1    Mora, L.2    Buckingham, R.H.3    Ehrenberg, M.4


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