메뉴 건너뛰기




Volumn 39, Issue 2, 2011, Pages 599-608

A single amino acid change of translation termination factor eRF1 switches between bipotent and omnipotent stop-codon specificity

Author keywords

[No Author keywords available]

Indexed keywords

ADENINE; ALANINE; GUANINE; TRANSLATION TERMINATION FACTOR; URACIL;

EID: 79551484186     PISSN: 03051048     EISSN: 13624962     Source Type: Journal    
DOI: 10.1093/nar/gkq759     Document Type: Article
Times cited : (26)

References (38)
  • 1
    • 0037439231 scopus 로고    scopus 로고
    • Termination of translation: Interplay of mRNA, rRNAs and release factors
    • Kisselev, L.L., Ehrenberg, M. and Frolova, L.Yu. (2003) Termination of translation: interplay of mRNA, rRNAs and release factors. EMBO J., 22, 175-182.
    • (2003) EMBO J. , vol.22 , 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. and 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. and 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
    • 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. and 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
  • 6
    • 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. and 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
  • 7
    • 0036216442 scopus 로고    scopus 로고
    • Highly conserved NIKS tetrapeptide is functionally essential in eukaryotic translation termination factor eRF1
    • Frolova, L., Seit-Nebi, A. and 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
  • 8
    • 0036747332 scopus 로고    scopus 로고
    • Conversion of omnipotent translation termination factor eRF1 into ciliate-like UGA-only unipotent eRF1
    • Seit-Nebi, A., Frolova, L. and 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
  • 9
    • 0036792666 scopus 로고    scopus 로고
    • The invariant uridine of stop codons contacts the conserved NIKSR loop of human eRF1 in the ribosome
    • Chavatte, L., Seit-Nebi, A., Dubovaya, V. and Favre, A. (2002) The invariant uridine of stop codons contacts the conserved NIKSR loop of human eRF1 in the ribosome. EMBO J., 21, 5302-5311.
    • (2002) EMBO J. , vol.21 , pp. 5302-5311
    • Chavatte, L.1    Seit-Nebi, A.2    Dubovaya, V.3    Favre, A.4
  • 10
    • 0037079664 scopus 로고    scopus 로고
    • Convergence and constraint in eukaryotic release factor (eRF1) domain 1: The evolution of stop codon specificity
    • Inagaki, Y., Bloin, C., Doolitle, W.F. and Roger, A.J. (2002) Convergence and constraint in eukaryotic release factor (eRF1) domain 1: the evolution of stop codon specificity. Nucleic Acids Res., 30, 532-544.
    • (2002) Nucleic Acids Res. , vol.30 , pp. 532-544
    • Inagaki, Y.1    Bloin, C.2    Doolitle, W.F.3    Roger, A.J.4
  • 11
    • 0345146926 scopus 로고    scopus 로고
    • Stop codon selection in eukaryotic translation termination: Comparison of the discriminating potential between human and ciliate eRF1s
    • Chavatte, L., Kervestin, S., Favre, A. and Jean-Jean, O. (2003) Stop codon selection in eukaryotic translation termination: comparison of the discriminating potential between human and ciliate eRF1s. EMBO J., 22, 1644-1653.
    • (2003) EMBO J. , vol.22 , pp. 1644-1653
    • Chavatte, L.1    Kervestin, S.2    Favre, A.3    Jean-Jean, O.4
  • 13
    • 14744303845 scopus 로고    scopus 로고
    • Newly sequenced eRF1s from ciliates: The diversity of stop codon usage and the molecular surfaces that are important for stop codon interactions
    • Kim, O.T., Yura, K., Go, N. and Harumoto, T. (2005) Newly sequenced eRF1s from ciliates: the diversity of stop codon usage and the molecular surfaces that are important for stop codon interactions. Gene, 346, 277-286.
    • (2005) Gene , vol.346 , pp. 277-286
    • Kim, O.T.1    Yura, K.2    Go, N.3    Harumoto, T.4
  • 14
    • 18844421633 scopus 로고    scopus 로고
    • Decoding the decoding region: Analysis of eukaryotic release factor (eRF1) stop codon-binding residues
    • Liang, H., Wong, J.Y., Bao, Q., Cavalcanti, A.R. and Landweber, L.F. (2005) Decoding the decoding region: analysis of eukaryotic release factor (eRF1) stop codon-binding residues. J. Mol. Evol., 60, 337-344.
    • (2005) J. Mol. Evol. , vol.60 , pp. 337-344
    • Liang, H.1    Wong, J.Y.2    Bao, Q.3    Cavalcanti, A.R.4    Landweber, L.F.5
  • 15
    • 0035910449 scopus 로고    scopus 로고
    • Molecular mechanism of stop codon recognition by eRF1: A wobble hypothesis for peptide anticodons
    • Muramatsu, T., Heckmann, K., Kitanaka, C. and Kuchino, Y. (2001) Molecular mechanism of stop codon recognition by eRF1: a wobble hypothesis for peptide anticodons. FEBS Lett., 488, 105-109.
    • (2001) FEBS Lett. , vol.488 , pp. 105-109
    • Muramatsu, T.1    Heckmann, K.2    Kitanaka, C.3    Kuchino, Y.4
  • 16
    • 34547414394 scopus 로고    scopus 로고
    • Different modes of stop codon restriction by the Stylonychia and Paramecium eRF1 translation termination factors
    • Lekomtsev, S., Kolosov, P., Bidou, L., Frolova, L., Rousset, J.P. and Kisselev, L. (2007) Different modes of stop codon restriction by the Stylonychia and Paramecium eRF1 translation termination factors. Proc. Natl Acad. Sci. USA, 104, 10824-10829.
    • (2007) Proc. Natl Acad. Sci. USA , vol.104 , pp. 10824-10829
    • Lekomtsev, S.1    Kolosov, P.2    Bidou, L.3    Frolova, L.4    Rousset, J.P.5    Kisselev, L.6
  • 17
    • 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. and 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
  • 18
    • 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. and 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
  • 19
    • 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
  • 21
    • 0031857784 scopus 로고    scopus 로고
    • The stretch of C-terminal acidic amino acids of translational release factor eRF1 is a primary binding site for eRF3 of fission yeast
    • Ito, K., Ebihara, K. and Nakamura, Y. (1998) The stretch of C-terminal acidic amino acids of translational release factor eRF1 is a 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
  • 22
    • 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.Y., Lazar, M., Camonis, J. and Kisselev, L.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.Y.2    Lazar, M.3    Camonis, J.4    Kisselev, L.L.5
  • 23
    • 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. and 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
  • 25
    • 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
  • 26
    • 4344677977 scopus 로고    scopus 로고
    • GTP hydrolysis by eRF3 facilitates stop codon decoding during eukaryotic translation termination
    • Salas-Marco, J. and Bedwell, D.M. (2004) GTP hydrolysis by eRF3 facilitates stop codon decoding during eukaryotic translation termination. Mol. Cell Biol., 24, 7769-7778.
    • (2004) Mol. Cell Biol. , vol.24 , pp. 7769-7778
    • Salas-Marco, J.1    Bedwell, D.M.2
  • 27
    • 0021833489 scopus 로고
    • An unusual genetic code in nuclear genes of Tetrahymena
    • Horowitz, S. and Gorovsky, M.A. (1985) An unusual genetic code in nuclear genes of Tetrahymena. Proc. Natl Acad. Sci. USA, 82, 2452-2455.
    • (1985) Proc. Natl Acad. Sci. USA , vol.82 , pp. 2452-2455
    • Horowitz, S.1    Gorovsky, M.A.2
  • 29
    • 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. and 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
  • 34
    • 0016017204 scopus 로고
    • Mammalian release factor: In vitro assay and purification
    • Caskey, C., Beaudet, A.L. and Tate, W.P. (1974) Mammalian release factor: in vitro assay and purification. Methods Enzymol., 30, 293-303.
    • (1974) Methods Enzymol. , vol.30 , pp. 293-303
    • Caskey, C.1    Beaudet, A.L.2    Tate, W.P.3
  • 36
    • 0017836245 scopus 로고
    • Leaky UAG termination codon in tobacco mosaic virus RNA
    • Pelham, H.R. (1978) Leaky UAG termination codon in tobacco mosaic virus RNA. Nature, 272, 469-471.
    • (1978) Nature , vol.272 , pp. 469-471
    • Pelham, H.R.1
  • 37
    • 78650923220 scopus 로고    scopus 로고
    • Functional characterization of polypeptide release factor 1b in the ciliate Euplotes
    • [Epub ahead of print] PMID: 20136636 February 8 2010
    • Wang, Y., Chai, B., Wang, W. and Liang, A. (2010) Functional characterization of polypeptide release factor 1b in the ciliate Euplotes. Biosci. Rep., [Epub ahead of print] PMID: 20136636 February 8, 2010.
    • (2010) Biosci. Rep.
    • Wang, Y.1    Chai, B.2    Wang, W.3    Liang, A.4
  • 38
    • 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
    • Freistroffer, D.V., Pavlov, M.Y., MacDougall, J., Buckingham, R.H. and Ehrenberg, M. (1997) 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, 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


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.