메뉴 건너뛰기




Volumn 3, Issue 9, 2002, Pages 881-886

Conversion of omnipotent translation termination factor eRF1 into ciliate-like UGA-only unipotent eRF1

Author keywords

[No Author keywords available]

Indexed keywords

ADENINE; CYSTEINE; GUANINE; TRANSLATION TERMINATION FACTOR; URACIL;

EID: 0036747332     PISSN: 1469221X     EISSN: None     Source Type: Journal    
DOI: 10.1093/embo-reports/kvf178     Document Type: Article
Times cited : (86)

References (27)
  • 1
    • 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
  • 2
    • 0016017204 scopus 로고
    • Mammalian release factor: In vitro assay and purification
    • Caskey, C.T., 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.T.1    Beaudet, A.L.2    Tate, W.P.3
  • 3
    • 0028581973 scopus 로고
    • A highly conserved eukaryotic protein family possessing properties of polypeptide chain release factor
    • Frolova, L. et al. (1994) A highly conserved eukaryotic protein family possessing properties of polypeptide chain release factor. Nature, 372, 701-703.
    • (1994) Nature , vol.372 , pp. 701-703
    • Frolova, L.1
  • 5
    • 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.Yu., Tsivkovskii, R., Sivolobova, G., Oparina, N., Serpinsky, O., Blinov, V., Tatkov, S. and Kisselev, 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.Yu.1    Tsivkovskii, R.2    Sivolobova, G.3    Oparina, N.4    Serpinsky, O.5    Blinov, V.6    Tatkov, S.7    Kisselev, L.8
  • 6
    • 0034069537 scopus 로고    scopus 로고
    • Translation termination in eukaryotes: Polypeptide release factor eRF1 is composed of two functionally and structurally distinct domains
    • Frolova, L.Yu., Merkulova, T.I. and Kisselev, L.L. (2000) Translation termination in eukaryotes: polypeptide release factor eRF1 is composed of two functionally and structurally distinct domains. RNA, 6, 381-390.
    • (2000) RNA , vol.6 , pp. 381-390
    • Frolova, L.Yu.1    Merkulova, T.I.2    Kisselev, L.L.3
  • 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
  • 9
    • 0035865797 scopus 로고    scopus 로고
    • Class I release factors in ciliates with variant genetic codes
    • Inagaki, Y. and Doolittle, W.F. (2001) Class I release factors in ciliates with variant genetic codes. Nucleic Acids Res., 29, 921-927.
    • (2001) Nucleic Acids Res , vol.29 , pp. 921-927
    • Inagaki, Y.1    Doolittle, W.F.2
  • 10
    • 0037079664 scopus 로고    scopus 로고
    • Convergence and constraint in eukaryotic release factor 1 (eRF1) domain 1: Evolution of stop codon specificity
    • Inagaki, Y., Blouin, C., Doolittle, W.F. and Roger, A.J. (2002) Convergence and constraint in eukaryotic release factor 1 (eRF1) domain 1: evolution of stop codon specificity. Nucleic Acids Res., 30, 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
  • 11
    • 0034628438 scopus 로고    scopus 로고
    • A tripeptide anticodon deciphers stop codons in messenger RNA
    • Ito, K., Uno, M. and Nakamura, Y. (2000) A tripeptide anticodon deciphers stop codons in messenger RNA. Nature, 403, 680-684.
    • (2000) Nature , vol.403 , pp. 680-684
    • Ito, K.1    Uno, M.2    Nakamura, Y.3
  • 12
    • 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
  • 13
    • 0034860257 scopus 로고    scopus 로고
    • Stop codon recognition in ciliates: Euplotes release factor does not respond to reassigned UGA codon
    • Kervestin, S., Frolova, L., Kisselev, L. and Jean-Jean, O. (2001) Stop codon recognition in ciliates: Euplotes release factor does not respond to reassigned UGA codon. EMBO rep., 2,680-684.
    • (2001) EMBO Rep , vol.2 , pp. 680-684
    • Kervestin, S.1    Frolova, L.2    Kisselev, L.3    Jean-Jean, O.4
  • 14
    • 0036156042 scopus 로고    scopus 로고
    • Polypeptide release factors in prokaryotes and eukaryotes: Same function, different structure
    • Kisselev, L. (2002) Polypeptide release factors in prokaryotes and eukaryotes: same function, different structure. Structure, 10, 8-9.
    • (2002) Structure , vol.10 , pp. 8-9
    • Kisselev, L.1
  • 15
  • 16
    • 0034185463 scopus 로고    scopus 로고
    • Class-1 translation termination factors are structurally and functionally similar to suppressor tRNAs and belong to distinct structurally and functional families (prokaryotes/mitochondria and eukaryotes/archaea)
    • Kisselev, L.L., Oparina, N.Yu. and Frolova, L.Yu. (2000) Class-1 translation termination factors are structurally and functionally similar to suppressor tRNAs and belong to distinct structurally and functional families (prokaryotes/mitochondria and eukaryotes/archaea). Mol. Biol. (Moscow), 34, 427-442.
    • (2000) Mol. Biol. (Moscow) , vol.34 , pp. 427-442
    • Kisselev, L.L.1    Oparina, N.Yu.2    Frolova, L.Yu.3
  • 17
    • 0034625234 scopus 로고    scopus 로고
    • The early evolution of the genetic code
    • Knight, R.D. and Landweber, L.F. (2000) The early evolution of the genetic code. Cell, 101, 569-572.
    • (2000) Cell , vol.101 , pp. 569-572
    • Knight, R.D.1    Landweber, L.F.2
  • 18
    • 0035234558 scopus 로고    scopus 로고
    • Rewiring the keyboard evolvability of genetic code
    • Knight, R.D., Freeland, S.J. and Landweber, L.F. (2001) Rewiring the keyboard. evolvability of genetic code. Nat. Rev. Genet., 2, 49-58.
    • (2001) Nat. Rev. Genet , vol.2 , pp. 49-58
    • 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. (2001) The molecular basis of nuclear genetic code change in ciliates. Curr. Biol., 11, 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. (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
  • 21
    • 0034640086 scopus 로고    scopus 로고
    • Mimicry grasps reality in translation termination
    • Nakamura, Y., Ito, K. and Ehrenberg, M. (2000) Mimicry grasps reality in translation termination. Cell, 101, 349-352.
    • (2000) Cell , vol.101 , pp. 349-352
    • Nakamura, Y.1    Ito, K.2    Ehrenberg, M.3
  • 22
    • 0034618493 scopus 로고    scopus 로고
    • Release factors and their role as decoding proteins: Specificity and fidelity for termination of protein synthesis
    • Poole, E: and Tate, W. (2000) Release factors and their role as decoding proteins: specificity and fidelity for termination of protein synthesis. Biochim. Biophys. Acta, 1493, 1-11.
    • (2000) Biochim. Biophys. Acta , vol.1493 , pp. 1-11
    • Poole, E.1    Tate, W.2
  • 23
    • 0025325983 scopus 로고
    • The 'megaprimer' method of site-directed mutagenesis
    • Sarkar, G. and Sommer, S.S. (1990) The 'megaprimer' method of site-directed mutagenesis. Biotechniques, 8, 404-407.
    • (1990) Biotechniques , vol.8 , pp. 404-407
    • Sarkar, G.1    Sommer, S.S.2
  • 24
    • 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
  • 25
    • 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
  • 26
    • 0035951295 scopus 로고    scopus 로고
    • Genetic interaction between yeast Saccharomyces cerevisiae release factors and the decoding region of 18S rRNA
    • Velichutina, I.V., Hong, J.Y., Mesecar, A.D., Chernoff, Y.O. and Liebman, S.W. (2001) Genetic interaction between yeast Saccharomyces cerevisiae release factors and the decoding region of 18S rRNA. J. Mol. Biol., 305, 715-727.
    • (2001) J. Mol. Biol , vol.305 , pp. 715-727
    • Velichutina, I.V.1    Hong, J.Y.2    Mesecar, A.D.3    Chernoff, Y.O.4    Liebman, S.W.5
  • 27


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.