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Volumn 30, Issue 5, 2008, Pages 599-609

Distinct eRF3 Requirements Suggest Alternate eRF1 Conformations Mediate Peptide Release during Eukaryotic Translation Termination

Author keywords

PROTEINS

Indexed keywords

HYBRID PROTEIN; PEPTIDE; PROTEIN ERF3; SACCHAROMYCES CEREVISIAE PROTEIN;

EID: 44449153482     PISSN: 10972765     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.molcel.2008.03.020     Document Type: Article
Times cited : (53)

References (30)
  • 1
    • 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. In vitro reconstitution of eukaryotic translation reveals cooperativity between release factors eRF1 and eRF3. Cell 125 (2006) 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
  • 2
    • 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. Terminating eukaryote translation: domain 1 of release factor eRF1 functions in stop codon recognition. RNA 6 (2000) 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
  • 3
    • 0029153552 scopus 로고
    • The efficiency of translation termination is determined by a synergistic interplay between upstream and downstream sequences in Saccharomyces cerevisiae
    • Bonetti B., Fu L., Moon J., and Bedwell D.M. The efficiency of translation termination is determined by a synergistic interplay between upstream and downstream sequences in Saccharomyces cerevisiae. J. Mol. Biol. 251 (1995) 334-345
    • (1995) J. Mol. Biol. , vol.251 , pp. 334-345
    • Bonetti, B.1    Fu, L.2    Moon, J.3    Bedwell, D.M.4
  • 4
    • 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. The invariant uridine of stop codons contacts the conserved NIKSR loop of human eRF1 in the ribosome. EMBO J. 21 (2002) 5302-5311
    • (2002) EMBO J. , vol.21 , pp. 5302-5311
    • Chavatte, L.1    Seit-Nebi, A.2    Dubovaya, V.3    Favre, A.4
  • 5
    • 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. The C-terminus of eRF1 defines a functionally important domain for translation termination in Saccharomyces cerevisiae. Mol. Microbiol. 32 (1999) 485-496
    • (1999) Mol. Microbiol. , vol.32 , pp. 485-496
    • Eurwilaichitr, L.1    Graves, F.M.2    Stansfield, I.3    Tuite, M.F.4
  • 6
    • 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. 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
  • 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. 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
  • 9
    • 0033854425 scopus 로고    scopus 로고
    • Sequence specificity of aminoglycoside-induced stop codon readthrough: potential implications for treatment of Duchenne muscular dystrophy
    • Howard M.T., Shirts B.H., Petros L.M., Flanigan K.M., Gesteland R.F., and Atkins J.F. Sequence specificity of aminoglycoside-induced stop codon readthrough: potential implications for treatment of Duchenne muscular dystrophy. Ann. Neurol. 48 (2000) 164-169
    • (2000) Ann. Neurol. , vol.48 , pp. 164-169
    • Howard, M.T.1    Shirts, B.H.2    Petros, L.M.3    Flanigan, K.M.4    Gesteland, R.F.5    Atkins, J.F.6
  • 10
    • 0035865797 scopus 로고    scopus 로고
    • Class I release factors in ciliates with variant genetic codes
    • Inagaki Y., and Doolittle W.F. Class I release factors in ciliates with variant genetic codes. Nucleic Acids Res. 29 (2001) 921-927
    • (2001) Nucleic Acids Res. , vol.29 , pp. 921-927
    • Inagaki, Y.1    Doolittle, W.F.2
  • 11
    • 0037079664 scopus 로고    scopus 로고
    • Convergence and constraint in eukaryotic release factor 1 (eRF1) domain 1: the evolution of stop codon specificity
    • Inagaki Y., Blouin C., Doolittle W.F., and Roger A.J. Convergence and constraint in eukaryotic release factor 1 (eRF1) domain 1: the evolution of stop codon specificity. Nucleic Acids Res. 30 (2002) 532-544
    • (2002) Nucleic Acids Res. , vol.30 , pp. 532-544
    • Inagaki, Y.1    Blouin, C.2    Doolittle, W.F.3    Roger, A.J.4
  • 12
    • 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. 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 (1998) 958-972
    • (1998) RNA , vol.4 , pp. 958-972
    • Ito, K.1    Ebihara, K.2    Nakamura, Y.3
  • 13
    • 0034628438 scopus 로고    scopus 로고
    • A tripeptide 'anticodon' deciphers stop codons in messenger RNA
    • Ito K., Uno M., and Nakamura Y. 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
  • 14
    • 33747339238 scopus 로고    scopus 로고
    • Eukaryotic release factor 1 phosphorylation by CK2 protein kinase is dynamic but has little effect on the efficiency of translation termination in Saccharomyces cerevisiae
    • Kallmeyer A.K., Keeling K.M., and Bedwell D.M. Eukaryotic release factor 1 phosphorylation by CK2 protein kinase is dynamic but has little effect on the efficiency of translation termination in Saccharomyces cerevisiae. Eukaryot. Cell 5 (2006) 1378-1387
    • (2006) Eukaryot. Cell , vol.5 , pp. 1378-1387
    • Kallmeyer, A.K.1    Keeling, K.M.2    Bedwell, D.M.3
  • 15
    • 1642447080 scopus 로고    scopus 로고
    • Leaky termination at premature stop codons antagonizes nonsense-mediated mRNA decay in S. cerevisiae
    • Keeling K.M., Lanier J., Du M., Salas-Marco J., Gao L., Kaenjak-Angeletti A., and Bedwell D.M. Leaky termination at premature stop codons antagonizes nonsense-mediated mRNA decay in S. cerevisiae. RNA 10 (2004) 691-703
    • (2004) RNA , vol.10 , pp. 691-703
    • Keeling, K.M.1    Lanier, J.2    Du, M.3    Salas-Marco, J.4    Gao, L.5    Kaenjak-Angeletti, A.6    Bedwell, D.M.7
  • 16
    • 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. Newly sequenced eRF1s from ciliates: the diversity of stop codon usage and the molecular surfaces that are important for stop codon interactions. Gene 346 (2005) 277-286
    • (2005) Gene , vol.346 , pp. 277-286
    • Kim, O.T.1    Yura, K.2    Go, N.3    Harumoto, T.4
  • 17
    • 0037439231 scopus 로고    scopus 로고
    • Termination of translation: interplay of mRNA, rRNAs and release factors?
    • Kisselev L., Ehrenberg M., and Frolova L. 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
  • 18
    • 0034625234 scopus 로고    scopus 로고
    • The early evolution of the genetic code
    • Knight R.D., Freeland S.J., and Landweber L.F. The early evolution of the genetic code. Cell 101 (2000) 569-572
    • (2000) Cell , vol.101 , pp. 569-572
    • Knight, R.D.1    Freeland, S.J.2    Landweber, L.F.3
  • 19
    • 0035936577 scopus 로고    scopus 로고
    • The molecular basis of nuclear genetic code change in ciliates
    • Lozupone C.A., Knight R.D., and Landweber L.F. The molecular basis of nuclear genetic code change in ciliates. Curr. Biol. 11 (2001) 65-74
    • (2001) Curr. Biol. , vol.11 , pp. 65-74
    • Lozupone, C.A.1    Knight, R.D.2    Landweber, L.F.3
  • 20
    • 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. Molecular mechanism of stop codon recognition by eRF1: a wobble hypothesis for peptide anticodons. FEBS Lett. 488 (2001) 105-109
    • (2001) FEBS Lett. , vol.488 , pp. 105-109
    • Muramatsu, T.1    Heckmann, K.2    Kitanaka, C.3    Kuchino, Y.4
  • 21
    • 0037029037 scopus 로고    scopus 로고
    • A tripeptide discriminator for stop codon recognition
    • Nakamura Y., and Ito K. A tripeptide discriminator for stop codon recognition. FEBS Lett. 514 (2002) 30-33
    • (2002) FEBS Lett. , vol.514 , pp. 30-33
    • Nakamura, Y.1    Ito, K.2
  • 22
    • 0034640086 scopus 로고    scopus 로고
    • Mimicry grasps reality in translation termination
    • Nakamura Y., Ito K., and Ehrenberg M. Mimicry grasps reality in translation termination. Cell 101 (2000) 349-352
    • (2000) Cell , vol.101 , pp. 349-352
    • Nakamura, Y.1    Ito, K.2    Ehrenberg, M.3
  • 23
    • 4344677977 scopus 로고    scopus 로고
    • GTP hydrolysis by eRF3 facilitates stop codon decoding during eukaryotic translation termination
    • Salas-Marco J., and Bedwell D.M. GTP hydrolysis by eRF3 facilitates stop codon decoding during eukaryotic translation termination. Mol. Cell. Biol. 24 (2004) 7769-7778
    • (2004) Mol. Cell. Biol. , vol.24 , pp. 7769-7778
    • Salas-Marco, J.1    Bedwell, D.M.2
  • 24
    • 17444384877 scopus 로고    scopus 로고
    • Discrimination between defects in elongation fidelity and termination efficiency provides mechanistic insights into translational readthrough
    • Salas-Marco J., and Bedwell D.M. Discrimination between defects in elongation fidelity and termination efficiency provides mechanistic insights into translational readthrough. J. Mol. Biol. 348 (2005) 801-815
    • (2005) J. Mol. Biol. , vol.348 , pp. 801-815
    • Salas-Marco, J.1    Bedwell, D.M.2
  • 26
    • 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. 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 (2001) 3982-3987
    • (2001) Nucleic Acids Res. , vol.29 , pp. 3982-3987
    • Seit-Nebi, A.1    Frolova, L.2    Justesen, J.3    Kisselev, L.4
  • 27
    • 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. 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
  • 28
    • 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. 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
  • 29
    • 0029069222 scopus 로고
    • Genetic code deviations in the ciliates: evidence for multiple and independent events
    • Tourancheau A.B., Tsao N., Klobutcher L.A., Pearlman R.E., and Adoutte A. Genetic code deviations in the ciliates: evidence for multiple and independent events. EMBO J. 14 (1995) 3262-3267
    • (1995) EMBO J. , vol.14 , pp. 3262-3267
    • Tourancheau, A.B.1    Tsao, N.2    Klobutcher, L.A.3    Pearlman, R.E.4    Adoutte, A.5
  • 30
    • 0035812714 scopus 로고    scopus 로고
    • A posttermination ribosomal complex is the guanine nucleotide exchange factor for peptide release factor RF3
    • Zavialov A.V., Buckingham R.H., and Ehrenberg M. 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


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.