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Volumn 40, Issue 2, 2006, Pages 270-275

Influence of individual domains of the translation termination factor eRF1 on induction of the GTPase activity of the translation termination factor eRF3

Author keywords

eRF1 domains; eRF3; Eukaryotes; GTPase activity; Translation termination

Indexed keywords

EUKARYOTA;

EID: 33646496153     PISSN: 00268933     EISSN: 16083245     Source Type: Journal    
DOI: 10.1134/S0026893306020130     Document Type: Article
Times cited : (6)

References (29)
  • 1
    • 0037439231 scopus 로고    scopus 로고
    • Termination of translation: Interplay of mRNA, rRNAs and release factors?
    • Kisselev L.L., Ehrenberg M., Frolova L. Yu. 2003. Termination of translation: interplay of mRNA, rRNAs and release factors? EMBO J. 2, 175-182.
    • (2003) EMBO J. , vol.2 , pp. 175-182
    • Kisselev, L.L.1    Ehrenberg, M.2    Frolova, L.Yu.3
  • 2
    • 0037310005 scopus 로고    scopus 로고
    • Making sense of mimic in translation termination
    • Nakamura Y., Ito K. 2003. Making sense of mimic in translation termination. Trends Biochem. Sci. 28, 99-105.
    • (2003) Trends Biochem. Sci. , vol.28 , pp. 99-105
    • Nakamura, Y.1    Ito, K.2
  • 4
    • 0034603210 scopus 로고    scopus 로고
    • The crystal structure of human eukaryotic release factors eRF1: Mechanism of stop codon recognition and peptidyl-tRNA hydrolysis
    • Song H., Mugnier P., Webb H.M., Evans D.R, Tuite M.F., Hemmings B.A., Barford D. 2000. The crystal structure of human eukaryotic release factors 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    Webb, H.M.3    Evans, D.R.4    Tuite, M.F.5    Hemmings, B.A.6    Barford, D.7
  • 5
    • 0033827056 scopus 로고    scopus 로고
    • Terminating eukaryote translation: Domain 1 of release factor eRF1 functions in stop codon recognition
    • Bertram G., Bell H.A., Ritchie D.W., Fullerton G., Stansfield I. 2000. Terminating eukaryote translation: Domain 1 of release factor eRF1 functions in stop codon recognition. RNA. 6, 1236-1247.
    • (2000) RNA , vol.6 , pp. 1236-1247
    • Bertram, G.1    Bell, H.A.2    Ritchie, D.W.3    Fullerton, G.4    Stansfield, I.5
  • 6
    • 0036216442 scopus 로고    scopus 로고
    • Highly conserved NIKS tetrapeptide is functionally essential in eukaryotic translation termination factor eRF1
    • Frolova L., Seit-Nebi A., Kisselev L. 2002. Highly conserved NIKS tetrapeptide is functionally essential in eukaryotic translation termination factor eRF1. RNA. 8, 129-136.
    • (2002) RNA , vol.8 , pp. 129-136
    • Frolova, L.1    Seit-Nebi, A.2    Kisselev, L.3
  • 7
    • 0036747332 scopus 로고    scopus 로고
    • Conversion of omnipotent translation termination factor eRF1 into ciliate-like UGA-only unipotent eRF1
    • Seit-Nebi A., Frolova L., Kisselev L. 2002. Conversion of omnipotent translation termination factor eRF1 into ciliate-like UGA-only unipotent eRF1. EMBO Rep. 3, 881-886.
    • (2002) EMBO Rep. , vol.3 , pp. 881-886
    • Seit-Nebi, A.1    Frolova, L.2    Kisselev, L.3
  • 8
    • 0037173091 scopus 로고    scopus 로고
    • Omnipotent decoding potential resides in eukaryotic translation termination factor eRF1 of variant-code organisms and is modulated by the interactions of amino acid sequences within the domain 1
    • Ito K., Frolova L., Seit-Nebi A., Karamyshev A., Kisselev L., Nakamura Y. 2002. Omnipotent decoding potential resides in eukaryotic translation termination factor eRF1 of variant-code organisms and is modulated by the interactions of amino acid sequences within the domain 1. Proc. Natl. Acad. Sci. USA. 99, 8494-8499.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 8494-8499
    • Ito, K.1    Frolova, L.2    Seit-Nebi, A.3    Karamyshev, A.4    Kisselev, L.5    Nakamura, Y.6
  • 9
    • 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
    • Frolova L.Y., Tsivkovskii R.Y., Sivolobova G.F., Oparina N.Y., Serpinsky O.I., Blinov V.M., Tatkov S.I., Kisselev L.L. 1999. 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, 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
  • 10
    • 0035476654 scopus 로고    scopus 로고
    • Class-1 translation termination factors: Invariant GGQ minidomain is essential for release activity and ribosome binding but not for stop codon recognition
    • Seit-Nebi A., Frolova L., Justesen J., Kisselev L. 2001. Class-1 translation termination factors: Invariant GGQ minidomain is essential for release activity and ribosome binding but not for stop codon recognition. Nucleic Acids Res. 29, 3982-3987.
    • (2001) Nucleic Acids Res. , vol.29 , pp. 3982-3987
    • Seit-Nebi, A.1    Frolova, L.2    Justesen, J.3    Kisselev, L.4
  • 11
    • 0036810254 scopus 로고    scopus 로고
    • Release of peptide promoted by the GGQ-motif of class-1 release factors regulates the GTPase activity of RF3
    • Zavialov A.V., Mora L., Buckingham R.H., Ehrenberg M. 2002. Release of peptide promoted by the GGQ-motif of class-1 release factors regulates the GTPase activity of RF3. Mol. Cell. 10, 789-798.
    • (2002) Mol. Cell , vol.10 , pp. 789-798
    • Zavialov, A.V.1    Mora, L.2    Buckingham, R.H.3    Ehrenberg, M.4
  • 12
    • 0037223622 scopus 로고    scopus 로고
    • The essential role of the invariant GGQ motif in the function and the stability in vivo of bacterial release factors RF1 and RF2
    • Mora L., Heurgue-Hamard V., Champ S., Ehrenberg M., Kisselev L.L., Buckingham R.H. 2003. The essential role of the invariant GGQ motif in the function and the stability in vivo of bacterial release factors RF1 and RF2. Mol. Microbiol. 1, 267-275.
    • (2003) Mol. Microbiol. , vol.1 , pp. 267-275
    • Mora, L.1    Heurgue-Hamard, V.2    Champ, S.3    Ehrenberg, M.4    Kisselev, L.L.5    Buckingham, R.H.6
  • 13
    • 0031857784 scopus 로고    scopus 로고
    • The stretch of C-terminal acidic amino acids of translational release factor eRF1 is primary binding site for eRF3 of fission yeast
    • Ito K., Ebihara K., Nakamura Y 1998. The stretch of C-terminal acidic amino acids of translational release factor eRF1 is primary binding site for eRF3 of fission yeast. RNA. 4, 958-972.
    • (1998) RNA , vol.4 , pp. 958-972
    • Ito, K.1    Ebihara, K.2    Nakamura, Y.3
  • 14
    • 0032969177 scopus 로고    scopus 로고
    • C-terminal domains of human translation termination factors eRF1 and eRF3 mediate their in vivo interaction
    • Merkulova T.I., Frolova L.Yu., Lazar M., Camonis J., Kisselev L. 1999. C-terminal domains of human translation termination factors eRF1 and eRF3 mediate their in vivo interaction. FEBS Lett. 443, 41-47.
    • (1999) FEBS Lett. , vol.443 , pp. 41-47
    • Merkulova, T.I.1    Frolova, L.Yu.2    Lazar, M.3    Camonis, J.4    Kisselev, L.5
  • 15
    • 0033016754 scopus 로고    scopus 로고
    • C-terminal interaction of translational release factors eRF1 and eRF3 of fission yeast: G-domain uncoupled binding and the role of conserved amino acids
    • Ebihara K., Nakamura Y. 1999. C-terminal interaction of translational release factors eRF1 and eRF3 of fission yeast: G-domain uncoupled binding and the role of conserved amino acids. RNA. 5, 739-750.
    • (1999) RNA , vol.5 , pp. 739-750
    • Ebihara, K.1    Nakamura, Y.2
  • 16
    • 0032937983 scopus 로고    scopus 로고
    • The C-terminus of eRF1 defines a functionally important domain for translation termination in Saccharomyces cerevisiae
    • Eurwilaichitr L., Graves F.M., Stansfield I., Tuite M.F. 1999. The C-terminus of eRF1 defines a functionally important domain for translation termination in Saccharomyces cerevisiae. Mol. Microbiol. 32, 485-496.
    • (1999) Mol. Microbiol. , vol.32 , pp. 485-496
    • Eurwilaichitr, L.1    Graves, F.M.2    Stansfield, I.3    Tuite, M.F.4
  • 17
    • 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., 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
  • 18
    • 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., 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
  • 21
    • 0034069537 scopus 로고    scopus 로고
    • Translation termination in eukaryotes: Polypeptide release factor eRF1 is composed of functionally and structurally distinct domains
    • Frolova L.Y., Merkulova T.I., Kisselev L.L. 2000. Translation termination in eukaryotes: Polypeptide release factor eRF1 is composed of functionally and structurally distinct domains. RNA. 6, 381-390.
    • (2000) RNA , vol.6 , pp. 381-390
    • Frolova, L.Y.1    Merkulova, T.I.2    Kisselev, L.L.3
  • 22
    • 0025300680 scopus 로고
    • Binding and hydrolysis of guanine nucleotides by Sec4p, a yeast protein involved in the regulation of vesicular traffic
    • Kabcenell A.K., Goud B., Northup J.K., Novick P.J. 1990 Binding and hydrolysis of guanine nucleotides by Sec4p, a yeast protein involved in the regulation of vesicular traffic. J. Biol. Chem. 265, 9366-9372.
    • (1990) J. Biol. Chem. , vol.265 , pp. 9366-9372
    • Kabcenell, A.K.1    Goud, B.2    Northup, J.K.3    Novick, P.J.4
  • 23
    • 0032529092 scopus 로고    scopus 로고
    • Functional expression of eukaryotic polypeptide chain release factors 1 and 3 by means of baculovirus/insect cells and complex formation between the factors
    • Frolova L., Simonsen J., Merkulova T., Litvinov D., Martensen P., Rechinsky V., Camonis J., Kisselev L., Justesen J. 1998. Functional expression of eukaryotic polypeptide chain release factors 1 and 3 by means of baculovirus/insect cells and complex formation between the factors. Eur. J. Biochem. 256, 36-44.
    • (1998) Eur. J. Biochem. , vol.256 , pp. 36-44
    • Frolova, L.1    Simonsen, J.2    Merkulova, T.3    Litvinov, D.4    Martensen, P.5    Rechinsky, V.6    Camonis, J.7    Kisselev, L.8    Justesen, J.9
  • 24
    • 0034178948 scopus 로고    scopus 로고
    • Class-1 polypeptide chain release factors are structurally and functionally similar to suppressor tRNAs and comprise different structural-functional families of prokaryotic/mitochondrial and eukaryotic/archaebacterial factors
    • Kisselev L.L., Oparina N.Yu., Frolova L.Yu. 2000. Class-1 polypeptide chain release factors are structurally and functionally similar to suppressor tRNAs and comprise different structural-functional families of prokaryotic/mitochondrial and eukaryotic/archaebacterial factors. Mol. Biol. 34, 427-441.
    • (2000) Mol. Biol. , vol.34 , pp. 427-441
    • Kisselev, L.L.1    Oparina, N.Yu.2    Frolova, L.Yu.3
  • 26
    • 0037154986 scopus 로고    scopus 로고
    • Ribosome structure and mechanism of translation
    • Ramakrishnan V. 2002. Ribosome structure and mechanism of translation. Cell. 108, 557-572.
    • (2002) Cell , vol.108 , pp. 557-572
    • Ramakrishnan, V.1
  • 28
    • 13544262349 scopus 로고    scopus 로고
    • The first position of a codon placed in the a site of the human 80S ribosome contacts nucleotide C1696 of the 18S rRNA as well as proteins S2, S3, S3a, S30 and S15
    • Bulygin K., Chavatte L., Frolova L., Karpova G., Favre A. 2005. The first position of a codon placed in the A site of the human 80S ribosome contacts nucleotide C1696 of the 18S rRNA as well as proteins S2, S3, S3a, S30 and S15. Biochemistry. 44, 2153-2162.
    • (2005) Biochemistry , vol.44 , pp. 2153-2162
    • Bulygin, K.1    Chavatte, L.2    Frolova, L.3    Karpova, G.4    Favre, A.5
  • 29
    • 0043168057 scopus 로고    scopus 로고
    • Stop codons and UGG promote efficient binding of the human polypeptide release factor eRF1 to the eukaryotic ribosomal A site
    • Chavatte L., Frolova L., Laugaa P., Kisselev L., Favre A. 2003. Stop codons and UGG promote efficient binding of the human polypeptide release factor eRF1 to the eukaryotic ribosomal A site. J. Mol. Biol. 331, 745-758.
    • (2003) J. Mol. Biol. , vol.331 , pp. 745-758
    • Chavatte, L.1    Frolova, L.2    Laugaa, P.3    Kisselev, L.4    Favre, A.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.