메뉴 건너뛰기




Volumn 38, Issue 2, 2009, Pages 548-558

GTP-dependent structural rearrangement of the eRF1:eRF3 complex and eRF3 sequence motifs essential for PABP binding

Author keywords

[No Author keywords available]

Indexed keywords

ERF1 PROTEIN; ERF2 PROTEIN; ERF3 PROTEIN; GUANOSINE DIPHOSPHATE; GUANOSINE TRIPHOSPHATASE; GUANOSINE TRIPHOSPHATE; INTERFERON REGULATORY FACTOR 1; INTERFERON REGULATORY FACTOR 3; NUCLEOTIDE; PEPTIDE; POLYADENYLIC ACID BINDING PROTEIN; PROTEIN; UNCLASSIFIED DRUG; ETF1 PROTEIN, HUMAN; PEPTIDE CHAIN RELEASE FACTOR 3; PEPTIDE-CHAIN-RELEASE FACTOR 3; TRANSLATION TERMINATION FACTOR;

EID: 77449158439     PISSN: 03051048     EISSN: 13624962     Source Type: Journal    
DOI: 10.1093/nar/gkp908     Document Type: Article
Times cited : (30)

References (48)
  • 2
    • 0029145925 scopus 로고
    • Termination of translation in eukaryotes is governed by two interacting polypeptide chain release factors, eRF1 and eRF3
    • Zhouravleva, G., Frolova, L., Le Goff, X., Le Guellec, R., Inge-Vechtomov, S., Kisselev, L. and Philippe, M. (1995) Termination of translation in eukaryotes is governed by two interacting polypeptide chain release factors, eRF1 and eRF3. EMBO J., 14, 4065-4072.
    • (1995) EMBO J. , vol.14 , pp. 4065-4072
    • Zhouravleva, G.1    Frolova, L.2    Le Goff, X.3    Le Guellec, R.4    Inge-Vechtomov, S.5    Kisselev, L.6    Philippe, M.7
  • 3
    • 33746728252 scopus 로고    scopus 로고
    • Class-1 release factor eRF1 promotes GTP binding by class-2 release factor eRF3
    • Hauryliuk, V., Zavialov, A., Kisselev, L. and Ehrenberg, M. (2006) Class-1 release factor eRF1 promotes GTP binding by class-2 release factor eRF3. Biochimie, 88, 747-757.
    • (2006) Biochimie , vol.88 , pp. 747-757
    • Hauryliuk, V.1    Zavialov, A.2    Kisselev, L.3    Ehrenberg, M.4
  • 5
    • 33748572261 scopus 로고    scopus 로고
    • Termination of translation in eukaryotes is mediated by the quaternary eRF1*eRF3*GTP*Mg2+ complex. The biological roles of eRF3 and prokaryotic RF3 are profoundly distinct
    • Mitkevich, V.A., Kononenko, A.V., Petrushanko, I.Y., Yanvarev, D.V., Makarov, A.A. and Kisselev, L.L. (2006) Termination of translation in eukaryotes is mediated by the quaternary eRF1*eRF3*GTP*Mg2+ complex. The biological roles of eRF3 and prokaryotic RF3 are profoundly distinct. Nucleic Acids Res., 34, 3947-3954.
    • (2006) Nucleic Acids Res. , vol.34 , pp. 3947-3954
    • Mitkevich, V.A.1    Kononenko, A.V.2    Petrushanko, I.Y.3    Yanvarev, D.V.4    Makarov, A.A.5    Kisselev, L.L.6
  • 6
    • 33845992204 scopus 로고    scopus 로고
    • Kinetic analysis of interaction of eukaryotic release factor 3 with guanine nucleotides
    • Pisareva, V.P., Pisarev, A.V., Hellen, C.U., Rodnina, M.V. and Pestova, T.V. (2006) Kinetic analysis of interaction of eukaryotic release factor 3 with guanine nucleotides. J. Biol. Chem., 281, 40224-40235.
    • (2006) J. Biol. Chem. , vol.281 , pp. 40224-40235
    • Pisareva, V.P.1    Pisarev, A.V.2    Hellen, C.U.3    Rodnina, M.V.4    Pestova, T.V.5
  • 7
    • 50349097986 scopus 로고    scopus 로고
    • Co-factor dependent conformational switching of GTPases
    • Hauryliuk, V., Hansson, S. and Ehrenberg, M. (2008) Co-factor dependent conformational switching of GTPases. Biophys. J., 95, 1704-1715.
    • (2008) Biophys. J. , vol.95 , pp. 1704-1715
    • Hauryliuk, V.1    Hansson, S.2    Ehrenberg, M.3
  • 8
    • 19244364778 scopus 로고    scopus 로고
    • Eukaryotic polypeptide chain release factor eRF3 is an eRF1-and ribosome-dependent guanosine triphosphatase
    • Frolova, L., Le Goff, X., Zhouravleva, G., Davydova, E., Philippe, M. and Kisselev, L. (1996) Eukaryotic polypeptide chain release factor eRF3 is an eRF1-and ribosome-dependent guanosine triphosphatase. RNA, 2, 334-341.
    • (1996) RNA , vol.2 , pp. 334-341
    • Frolova, L.1    Le Goff, X.2    Zhouravleva, G.3    Davydova, E.4    Philippe, M.5    Kisselev, L.6
  • 9
    • 33744993160 scopus 로고    scopus 로고
    • In vitro reconstitution of eukaryotic translation reveals cooperativity between release factors eRF1 and eRF3
    • Alkalaeva, E.Z., Pisarev, A.V., Frolova, L.Y., Kisselev, L.L. and Pestova, T.V. (2006) In vitro reconstitution of eukaryotic translation reveals cooperativity between release factors eRF1 and eRF3. Cell, 125, 1125-1136.
    • (2006) Cell , vol.125 , pp. 1125-1136
    • Alkalaeva, E.Z.1    Pisarev, A.V.2    Frolova, L.Y.3    Kisselev, L.L.4    Pestova, T.V.5
  • 10
    • 0036237537 scopus 로고    scopus 로고
    • Poly(A)-binding protein acts in translation termination via eukaryotic release factor 3 interaction and does not influence [PSI(+)] propagation
    • Cosson, B., Couturier, A., Chabelskaya, S., Kiktev, D., Inge-Vechtomov, S., Philippe, M. and Zhouravleva, G. (2002) Poly(A)-binding protein acts in translation termination via eukaryotic release factor 3 interaction and does not influence [PSI(+)] propagation. Mol. Cell Biol., 22, 3301-3315.
    • (2002) Mol. Cell Biol. , vol.22 , pp. 3301-3315
    • Cosson, B.1    Couturier, A.2    Chabelskaya, S.3    Kiktev, D.4    Inge-Vechtomov, S.5    Philippe, M.6    Zhouravleva, G.7
  • 11
    • 0033546405 scopus 로고    scopus 로고
    • The eukaryotic polypeptide chain releasing factor (eRF3/GSPT) carrying the translation termination signal to the 3′-Poly(A) tail of mRNA. Direct association of erf3/GSPT with polyadenylate-binding protein
    • Hoshino, S., Imai, M., Kobayashi, T., Uchida, N. and Katada, T. (1999) The eukaryotic polypeptide chain releasing factor (eRF3/GSPT) carrying the translation termination signal to the 3′-Poly(A) tail of mRNA. Direct association of erf3/GSPT with polyadenylate-binding protein. J. Biol. Chem., 274, 16677-16680.
    • (1999) J. Biol. Chem. , vol.274 , pp. 16677-16680
    • Hoshino, S.1    Imai, M.2    Kobayashi, T.3    Uchida, N.4    Katada, T.5
  • 13
    • 0037184899 scopus 로고    scopus 로고
    • A novel role of the mammalian GSPT/eRF3 associating with poly(A)-binding protein in Cap/Poly(A)-dependent translation
    • Uchida, N., Hoshino, S., Imataka, H., Sonenberg, N. and Katada, T. (2002) A novel role of the mammalian GSPT/eRF3 associating with poly(A)-binding protein in Cap/Poly(A)-dependent translation. J. Biol. Chem., 277, 50286-50292.
    • (2002) J. Biol. Chem. , vol.277 , pp. 50286-50292
    • Uchida, N.1    Hoshino, S.2    Imataka, H.3    Sonenberg, N.4    Katada, T.5
  • 14
    • 0141866883 scopus 로고    scopus 로고
    • Translation termination factor eRF3 mediates mRNA decay through the regulation of deadenylation
    • Hosoda, N., Kobayashi, T., Uchida, N., Funakoshi, Y., Kikuchi, Y., Hoshino, S. and Katada, T. (2003) Translation termination factor eRF3 mediates mRNA decay through the regulation of deadenylation. J. Biol. Chem., 278, 38287-38291.
    • (2003) J. Biol. Chem. , vol.278 , pp. 38287-38291
    • Hosoda, N.1    Kobayashi, T.2    Uchida, N.3    Funakoshi, Y.4    Kikuchi, Y.5    Hoshino, S.6    Katada, T.7
  • 15
    • 8544231439 scopus 로고    scopus 로고
    • The GTP-binding release factor eRF3 as a key mediator coupling translation termination to mRNA decay
    • Kobayashi, T., Funakoshi, Y., Hoshino, S. and Katada, T. (2004) The GTP-binding release factor eRF3 as a key mediator coupling translation termination to mRNA decay. J. Biol. Chem., 279, 45693-45700.
    • (2004) J. Biol. Chem. , vol.279 , pp. 45693-45700
    • Kobayashi, T.1    Funakoshi, Y.2    Hoshino, S.3    Katada, T.4
  • 16
    • 46249091565 scopus 로고    scopus 로고
    • Translation factors promote the formation of two states of the closed-loop mRNP
    • Amrani, N., Ghosh, S., Mangus, D.A. and Jacobson, A. (2008) Translation factors promote the formation of two states of the closed-loop mRNP. Nature, 453, 1276-1280.
    • (2008) Nature , vol.453 , pp. 1276-1280
    • Amrani, N.1    Ghosh, S.2    Mangus, D.A.3    Jacobson, A.4
  • 17
    • 58149178746 scopus 로고    scopus 로고
    • Evolution of nonstop, no-go and nonsense-mediated mRNA decay and their termination factor-derived components
    • Atkinson, G.C., Baldauf, S.L. and Hauryliuk, V. (2008) Evolution of nonstop, no-go and nonsense-mediated mRNA decay and their termination factor-derived components. BMC Evol. Biol., 8, 290.
    • (2008) BMC Evol. Biol. , vol.8 , pp. 290
    • Atkinson, G.C.1    Baldauf, S.L.2    Hauryliuk, V.3
  • 19
    • 0242317676 scopus 로고    scopus 로고
    • Assessing functional divergence in EF-1alpha and its paralogs in eukaryotes and archaebacteria
    • Inagaki, Y., Blouin, C., Susko, E. and Roger, A.J. (2003) Assessing functional divergence in EF-1alpha and its paralogs in eukaryotes and archaebacteria. Nucleic Acids Res., 31, 4227-4237.
    • (2003) Nucleic Acids Res. , vol.31 , pp. 4227-4237
    • Inagaki, Y.1    Blouin, C.2    Susko, E.3    Roger, A.J.4
  • 20
    • 0034039808 scopus 로고    scopus 로고
    • Evolution of the eukaryotic translation termination system: origins of release factors
    • Inagaki, Y. and Doolittle, W.F. (2000) Evolution of the eukaryotic translation termination system: origins of release factors. Mol. Biol. Evol., 17, 882-889.
    • (2000) Mol. Biol. Evol. , vol.17 , pp. 882-889
    • Inagaki, Y.1    Doolittle, W.F.2
  • 21
    • 0032832981 scopus 로고    scopus 로고
    • Genetic study of interactions between the cytoskeletal assembly protein Sla1 and prion-forming domain of the release factor Sup35 (eRF3) in Saccharomyces cerevisiae
    • Bailleul, P.A., Newnam, G.P., Steenbergen, J.N. and Chernoff, Y.O. (1999) Genetic study of interactions between the cytoskeletal assembly protein Sla1 and prion-forming domain of the release factor Sup35 (eRF3) in Saccharomyces cerevisiae. Genetics, 153, 81-94.
    • (1999) Genetics , vol.153 , pp. 81-94
    • Bailleul, P.A.1    Newnam, G.P.2    Steenbergen, J.N.3    Chernoff, Y.O.4
  • 23
    • 10744227206 scopus 로고    scopus 로고
    • Structural basis of ligand recognition by PABC, a highly specific peptide-binding domain found in poly(A)-binding protein and a HECT ubiquitin ligase
    • Kozlov, G., De Crescenzo, G., Lim, N.S., Siddiqui, N., Fantus, D., Kahvejian, A., Trempe, J.F., Elias, D., Ekiel, I., Sonenberg, N. et al. (2004) Structural basis of ligand recognition by PABC, a highly specific peptide-binding domain found in poly(A)-binding protein and a HECT ubiquitin ligase. EMBO J., 23, 272-281.
    • (2004) EMBO J. , vol.23 , pp. 272-281
    • Kozlov, G.1    De Crescenzo, G.2    Lim, N.S.3    Siddiqui, N.4    Fantus, D.5    Kahvejian, A.6    Trempe, J.F.7    Elias, D.8    Ekiel, I.9    Sonenberg, N.10
  • 25
    • 1942470550 scopus 로고    scopus 로고
    • Crystal structure and functional analysis of the eukaryotic class II release factor eRF3 from S. pombe
    • Kong, C., Ito, K., Walsh, M.A., Wada, M., Liu, Y., Kumar, S., Barford, D., Nakamura, Y. and Song, H. (2004) Crystal structure and functional analysis of the eukaryotic class II release factor eRF3 from S. pombe. Mol. Cell, 14, 233-245.
    • (2004) Mol. Cell , vol.14 , pp. 233-245
    • Kong, C.1    Ito, K.2    Walsh, M.A.3    Wada, M.4    Liu, Y.5    Kumar, S.6    Barford, D.7    Nakamura, Y.8    Song, H.9
  • 26
    • 34249675662 scopus 로고    scopus 로고
    • The role of N-terminal domain of translational release factor eRF3 for the control of functionality and stability in S. cerevisiae
    • Kodama, H., Ito, K. and Nakamura, Y. (2007) The role of N-terminal domain of translational release factor eRF3 for the control of functionality and stability in S. cerevisiae. Genes Cells, 12, 639-650.
    • (2007) Genes Cells , vol.12 , pp. 639-650
    • Kodama, H.1    Ito, K.2    Nakamura, Y.3
  • 28
    • 43249084802 scopus 로고    scopus 로고
    • A competition between stimulators and antagonists of Upf complex recruitment governs human nonsense-mediated mRNA decay
    • Singh, G., Rebbapragada, I. and Lykke-Andersen, J. (2008) A competition between stimulators and antagonists of Upf complex recruitment governs human nonsense-mediated mRNA decay. Plos Biol., 6, 860-871.
    • (2008) Plos Biol. , vol.6 , pp. 860-871
    • Singh, G.1    Rebbapragada, I.2    Lykke-Andersen, J.3
  • 29
    • 57149092343 scopus 로고    scopus 로고
    • Chen, B.-Y. and Janes, H.W. (eds). 2nd edn. Humana Press, Totowa, NJ
    • Chen, B.-Y. and Janes, H.W. (2002) (eds), PCR cloning protocols, 2nd edn. Humana Press, Totowa, NJ.
    • (2002) PCR cloning protocols
  • 30
    • 13744252890 scopus 로고    scopus 로고
    • MAFFT version 5: improvement in accuracy of multiple sequence alignment
    • Katoh, K., Kuma, K., Toh, H. and Miyata, T. (2005) MAFFT version 5: improvement in accuracy of multiple sequence alignment. Nucleic Acids Res., 33, 511-518.
    • (2005) Nucleic Acids Res. , vol.33 , pp. 511-518
    • Katoh, K.1    Kuma, K.2    Toh, H.3    Miyata, T.4
  • 32
    • 29244442950 scopus 로고    scopus 로고
    • Simplified screening for the detection of soluble fusion constructs expressed in E. coli using a modular set of vectors
    • Dummler, A., Lawrence, A.M. and de Marco, A. (2005) Simplified screening for the detection of soluble fusion constructs expressed in E. coli using a modular set of vectors. Microb. Cell Fact., 4, 34.
    • (2005) Microb. Cell Fact. , vol.4 , pp. 34
    • Dummler, A.1    Lawrence, A.M.2    de Marco, A.3
  • 33
    • 0021093448 scopus 로고
    • Enthalpy-entropy compensation and heat capacity changes for protein-ligand interactions: general thermodynamic models and data for the binding of nucleotides to ribonuclease A
    • Eftink, M.R., Anusiem, A.C. and Biltonen, R.L. (1983) Enthalpy-entropy compensation and heat capacity changes for protein-ligand interactions: general thermodynamic models and data for the binding of nucleotides to ribonuclease A. Biochemistry, 22, 3884-3896.
    • (1983) Biochemistry , vol.22 , pp. 3884-3896
    • Eftink, M.R.1    Anusiem, A.C.2    Biltonen, R.L.3
  • 35
    • 0032901515 scopus 로고    scopus 로고
    • Isothermal titration calorimetry and differential scanning calorimetry as complementary tools to investigate the energetics of biomolecular recognition
    • Jelesarov, I. and Bosshard, H.R. (1999) Isothermal titration calorimetry and differential scanning calorimetry as complementary tools to investigate the energetics of biomolecular recognition. J. Mol. Recogn., 12, 3-18.
    • (1999) J. Mol. Recogn. , vol.12 , pp. 3-18
    • Jelesarov, I.1    Bosshard, H.R.2
  • 36
    • 0026651279 scopus 로고
    • Heat capacity changes and hydrophobic interactions in the binding of FK506 and rapamycin to the FK506 binding protein
    • Connelly, P.R. and Thomson, J.A. (1992) Heat capacity changes and hydrophobic interactions in the binding of FK506 and rapamycin to the FK506 binding protein. Proc. Natl Acad. Sci. USA, 89, 4781-4785.
    • (1992) Proc. Natl Acad. Sci. USA , vol.89 , pp. 4781-4785
    • Connelly, P.R.1    Thomson, J.A.2
  • 38
    • 0034603210 scopus 로고    scopus 로고
    • The crystal structure of human eukaryotic release factor eRF1-mechanism of stop codon recognition and peptidyl-tRNA hydrolysis
    • Song, H., Mugnier, P., Das, A.K., Webb, H.M., Evans, D.R., Tuite, M.F., Hemmings, B.A. and Barford, D. (2000) The crystal structure of human eukaryotic release factor eRF1-mechanism of stop codon recognition and peptidyl-tRNA hydrolysis. Cell, 100, 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
  • 39
    • 3242886767 scopus 로고    scopus 로고
    • Molecular morphology of eukaryotic class I translation termination factor eRF1 in solution
    • Kononenko, A.V., Dembo, K.A., Kiselev, L.L. and Volkov, V.V. (2004) Molecular morphology of eukaryotic class I translation termination factor eRF1 in solution. Mol. Biol. (Mosk), 38, 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
  • 42
    • 0030920782 scopus 로고    scopus 로고
    • G protein mechanisms: insights from structural analysis
    • Sprang, S.R. (1997) G protein mechanisms: insights from structural analysis. Annu. Rev. Biochem., 66, 639-678.
    • (1997) Annu. Rev. Biochem. , vol.66 , pp. 639-678
    • Sprang, S.R.1
  • 44
    • 0032575550 scopus 로고    scopus 로고
    • Molecular cloning of a novel member of the eukaryotic polypeptide chain-releasing factors (eRF). Its identification as eRF3 interacting with eRF1
    • Hoshino, S., Imai, M., Mizutani, M., Kikuchi, Y., Hanaoka, F., Ui, M. and Katada, T. (1998) Molecular cloning of a novel member of the eukaryotic polypeptide chain-releasing factors (eRF). Its identification as eRF3 interacting with eRF1. J. Biol. Chem., 273, 22254-22259.
    • (1998) J. Biol. Chem. , vol.273 , pp. 22254-22259
    • Hoshino, S.1    Imai, M.2    Mizutani, M.3    Kikuchi, Y.4    Hanaoka, F.5    Ui, M.6    Katada, T.7
  • 45
    • 0035408928 scopus 로고    scopus 로고
    • Identification of a novel termination release factor eRF3b expressing the eRF3 activity in vitro and in vivo
    • Jakobsen, C.G., Segaard, T.M., Jean-Jean, O., Frolova, L. and Justesen, J. (2001) Identification of a novel termination release factor eRF3b expressing the eRF3 activity in vitro and in vivo. Mol. Biol., 35, 672-681.
    • (2001) Mol. Biol. , vol.35 , pp. 672-681
    • Jakobsen, C.G.1    Segaard, T.M.2    Jean-Jean, O.3    Frolova, L.4    Justesen, J.5
  • 46
    • 21744448013 scopus 로고    scopus 로고
    • Involvement of human release factors eRF3a and eRF3b in translation termination and regulation of the termination complex formation
    • Chauvin, C., Salhi, S., Le Goff, C., Viranaicken, W., Diop, D. and Jean-Jean, O. (2005) Involvement of human release factors eRF3a and eRF3b in translation termination and regulation of the termination complex formation. Mol. Cell Biol., 25, 5801-5811.
    • (2005) Mol. Cell Biol. , vol.25 , pp. 5801-5811
    • Chauvin, C.1    Salhi, S.2    Le Goff, C.3    Viranaicken, W.4    Diop, D.5    Jean-Jean, O.6
  • 47
    • 45449118785 scopus 로고    scopus 로고
    • Recognition of nonsense mRNA: towards a unified model
    • Muhlemann, O. (2008) Recognition of nonsense mRNA: towards a unified model. Biochem. Soc. Trans., 36, 497-501.
    • (2008) Biochem. Soc. Trans. , vol.36 , pp. 497-501
    • Muhlemann, O.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.