메뉴 건너뛰기




Volumn 105, Issue 50, 2008, Pages 19684-19689

Crystal structure of a translation termination complex formed with release factor RF2

Author keywords

70S ribosome structure; Polypeptide release; Stop codon recognition

Indexed keywords

AMIDE; ESTERASE; GLUTAMINE; HYDROGEN; NITROGEN; PROLINE; PROLINE TRANSFER RNA; RELEASE FACTOR 2; RELEASING FACTOR; RIBOSOME RNA; RNA 16S; SERINE; THREONINE; TRANSFER RNA; TRANSLATION TERMINATION FACTOR; UNCLASSIFIED DRUG; VALINE; GLYCINE; PEPTIDE CHAIN TERMINATION RELEASE FACTOR 2; PEPTIDYLTRANSFERASE;

EID: 58149374559     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.0810953105     Document Type: Article
Times cited : (207)

References (43)
  • 1
    • 0014631155 scopus 로고
    • Characterization of three proteins involved in polypeptide chain termination
    • Capecchi MR, Klein HA (1969) Characterization of three proteins involved in polypeptide chain termination. Cold Spring Harbor Symp Quant Biol 34:469-477.
    • (1969) Cold Spring Harbor Symp Quant Biol , vol.34 , pp. 469-477
    • Capecchi, M.R.1    Klein, H.A.2
  • 3
    • 0014650139 scopus 로고
    • Peptide chain termination. V. The role of release factors in mRNA terminator codon recognition
    • Scolnick EM, Caskey CT (1969) Peptide chain termination. V. The role of release factors in mRNA terminator codon recognition. Proc Natl Acad Sci USA 64:1235-1241.
    • (1969) Proc Natl Acad Sci USA , vol.64 , pp. 1235-1241
    • Scolnick, E.M.1    Caskey, C.T.2
  • 4
    • 0035697089 scopus 로고    scopus 로고
    • Bacterial polypeptide release factor RF2 is structurally distinct from eukaryotic eRF1
    • Vestergaard B, et al. (2001) Bacterial polypeptide release factor RF2 is structurally distinct from eukaryotic eRF1. Mol Cell 8:1375-1382.
    • (2001) Mol Cell , vol.8 , pp. 1375-1382
    • Vestergaard, B.1
  • 5
    • 29244487090 scopus 로고    scopus 로고
    • Crystal structures of the ribosome in complex with release factors RF1 and RF2 bound to a cognate stop codon
    • Petry S, et al. (2005) Crystal structures of the ribosome in complex with release factors RF1 and RF2 bound to a cognate stop codon. Cell 123:1255-1266.
    • (2005) Cell , vol.123 , pp. 1255-1266
    • Petry, S.1
  • 6
    • 4143064788 scopus 로고    scopus 로고
    • Structural analyses of peptide release factor 1 from Thermotoga maritima reveal domain flexibility required for its interaction with the ribosome
    • Shin DH, et al. (2004) Structural analyses of peptide release factor 1 from Thermotoga maritima reveal domain flexibility required for its interaction with the ribosome. J Mol Biol 341:227-239.
    • (2004) J Mol Biol , vol.341 , pp. 227-239
    • Shin, D.H.1
  • 7
    • 0034628438 scopus 로고    scopus 로고
    • A tripeptide "anticodon" deciphers stop codons in messenger RNA
    • Ito K, Uno M, 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
  • 8
    • 0037029037 scopus 로고    scopus 로고
    • A tripeptide discriminator for stop codon recognition
    • Nakamura Y, Ito K (2002) A tripeptide discriminator for stop codon recognition. FEBS Lett 514:30-33.
    • (2002) FEBS Lett , vol.514 , pp. 30-33
    • Nakamura, Y.1    Ito, K.2
  • 9
    • 49649099901 scopus 로고    scopus 로고
    • Structural basis for translation termination on the 70S ribosome
    • Laurberg M, et al. (2008) Structural basis for translation termination on the 70S ribosome. Nature 454:852-857.
    • (2008) Nature , vol.454 , pp. 852-857
    • Laurberg, M.1
  • 10
    • 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, et al. (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
  • 11
    • 34548227759 scopus 로고    scopus 로고
    • A model for how ribosomal release factors induce peptidyl-tRNA cleavage in termination of protein synthesis
    • Trobro S, Aqvist J (2007) A model for how ribosomal release factors induce peptidyl-tRNA cleavage in termination of protein synthesis. Mol Cell 27:758-766.
    • (2007) Mol Cell , vol.27 , pp. 758-766
    • Trobro, S.1    Aqvist, J.2
  • 12
    • 0034266465 scopus 로고    scopus 로고
    • Mutation of a glutamine residue in the universal tripeptide GGQ in human eRF1 termination factor does not cause complete loss of its activity
    • Seit Nebi A, Frolova L, Ivanova N, Poltaraus A, Kiselev L (2000) Mutation of a glutamine residue in the universal tripeptide GGQ in human eRF1 termination factor does not cause complete loss of its activity. Mol Biol (Moscow) 34:899-900.
    • (2000) Mol Biol (Moscow) , vol.34 , pp. 899-900
    • Seit Nebi, A.1    Frolova, L.2    Ivanova, N.3    Poltaraus, A.4    Kiselev, L.5
  • 13
    • 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
  • 14
    • 35648950403 scopus 로고    scopus 로고
    • Two distinct components of release factor function uncovered by nucleophile partitioning analysis
    • Shaw JJ, Green R (2007) Two distinct components of release factor function uncovered by nucleophile partitioning analysis. Mol Cell 28:458-467.
    • (2007) Mol Cell , vol.28 , pp. 458-467
    • Shaw, J.J.1    Green, R.2
  • 15
    • 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 LY, et al. (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
  • 16
    • 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 AV, Mora L, Buckingham RH, 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
  • 17
    • 0035805229 scopus 로고    scopus 로고
    • Recognition of cognate transfer RNA by the 30S ribosomal subunit
    • Ogle JM, et al. (2001) Recognition of cognate transfer RNA by the 30S ribosomal subunit. Science 292:897-902.
    • (2001) Science , vol.292 , pp. 897-902
    • Ogle, J.M.1
  • 18
    • 33748527208 scopus 로고    scopus 로고
    • Deletion of a conserved, central ribosomal intersubunit RNA bridge
    • Ali IK, Lancaster L, Feinberg J, Joseph S, Noller HF (2006) Deletion of a conserved, central ribosomal intersubunit RNA bridge. Mol Cell 23:865-874.
    • (2006) Mol Cell , vol.23 , pp. 865-874
    • Ali, I.K.1    Lancaster, L.2    Feinberg, J.3    Joseph, S.4    Noller, H.F.5
  • 19
    • 36248994061 scopus 로고    scopus 로고
    • Stop codon recognition by release factors induces structural rearrangement of the ribosomal decoding center that is productive for peptide release
    • Youngman EM, He SL, Nikstad LJ, Green R (2007) Stop codon recognition by release factors induces structural rearrangement of the ribosomal decoding center that is productive for peptide release. Mol Cell 28:533-543.
    • (2007) Mol Cell , vol.28 , pp. 533-543
    • Youngman, E.M.1    He, S.L.2    Nikstad, L.J.3    Green, R.4
  • 20
    • 0347721768 scopus 로고    scopus 로고
    • Rawat UB, et al. (2003) A cryo-electron microscopic study of ribosome-bound termination factor RF2. Nature 421:87-90.
    • Rawat UB, et al. (2003) A cryo-electron microscopic study of ribosome-bound termination factor RF2. Nature 421:87-90.
  • 21
    • 33644818227 scopus 로고    scopus 로고
    • Interactions of the release factor RF1 with the ribosome as revealed by cryo-EM
    • Rawat U, et al. (2006) Interactions of the release factor RF1 with the ribosome as revealed by cryo-EM. J Mol Biol 357:1144-1153.
    • (2006) J Mol Biol , vol.357 , pp. 1144-1153
    • Rawat, U.1
  • 22
    • 33749354360 scopus 로고    scopus 로고
    • Structure of the 70S ribosome complexed with mRNA and tRNA
    • Selmer M, et al. (2006) Structure of the 70S ribosome complexed with mRNA and tRNA. Science 313:1935-1942.
    • (2006) Science , vol.313 , pp. 1935-1942
    • Selmer, M.1
  • 23
    • 0035910393 scopus 로고    scopus 로고
    • Crystal structure of an initiation factor bound to the 30S ribosomal subunit
    • Carter AP, et al. (2001) Crystal structure of an initiation factor bound to the 30S ribosomal subunit. Science 291:498-501.
    • (2001) Science , vol.291 , pp. 498-501
    • Carter, A.P.1
  • 24
    • 34547696927 scopus 로고    scopus 로고
    • Structural basis for aminoglycoside inhibition of bacterial ribosome recycling
    • Borovinskaya MA, et al. (2007) Structural basis for aminoglycoside inhibition of bacterial ribosome recycling. Nat Struct Mol Biol 14:727-732.
    • (2007) Nat Struct Mol Biol , vol.14 , pp. 727-732
    • Borovinskaya, M.A.1
  • 25
    • 27244458194 scopus 로고    scopus 로고
    • Crystal structures of complexes between aminoglycosides and decoding A site oligonucleotides: Role of the number of rings and positive charges in the specific binding leading to miscoding
    • Francois B, et al. (2005) Crystal structures of complexes between aminoglycosides and decoding A site oligonucleotides: Role of the number of rings and positive charges in the specific binding leading to miscoding. Nucleic Acids Res 33:5677-5690.
    • (2005) Nucleic Acids Res , vol.33 , pp. 5677-5690
    • Francois, B.1
  • 27
    • 4444227242 scopus 로고    scopus 로고
    • Electrostatic potential of nucleotide-free protein is sufficient for discrimination between adenine and guanine-specific binding sites
    • Basu G, Sivanesan D, Kawabata T, Go N (2004) Electrostatic potential of nucleotide-free protein is sufficient for discrimination between adenine and guanine-specific binding sites. J Mol Biol 342:1053-1066.
    • (2004) J Mol Biol , vol.342 , pp. 1053-1066
    • Basu, G.1    Sivanesan, D.2    Kawabata, T.3    Go, N.4
  • 28
    • 0011824888 scopus 로고    scopus 로고
    • Structures and energies of hydrogen-bonded DNA base pairs. A nonempirical study with inclusion of electron correlation
    • Sponer J, Leszczynski J, Hobza P (1996) Structures and energies of hydrogen-bonded DNA base pairs. A nonempirical study with inclusion of electron correlation. J Phys Chem 100:1965-1974.
    • (1996) J Phys Chem , vol.100 , pp. 1965-1974
    • Sponer, J.1    Leszczynski, J.2    Hobza, P.3
  • 29
    • 0029402489 scopus 로고
    • Translational termination efficiency in both bacteria and mammals is regulated by the base following the stop codon
    • Tate WP, et al. (1995) Translational termination efficiency in both bacteria and mammals is regulated by the base following the stop codon. Biochem Cell Biol 73:1095-1103.
    • (1995) Biochem Cell Biol , vol.73 , pp. 1095-1103
    • Tate, W.P.1
  • 30
    • 0032519296 scopus 로고    scopus 로고
    • Translational termination in Escherichia coli: Three bases following the stop codon cross-link to release factor 2 and affect the decoding efficiency of UGA-containing signals
    • Poole ES, Major LL, Mannering SA, Tate WP (1998) Translational termination in Escherichia coli: Three bases following the stop codon cross-link to release factor 2 and affect the decoding efficiency of UGA-containing signals. Nucleic Acids Res 26:954-960.
    • (1998) Nucleic Acids Res , vol.26 , pp. 954-960
    • Poole, E.S.1    Major, L.L.2    Mannering, S.A.3    Tate, W.P.4
  • 31
    • 34548587149 scopus 로고    scopus 로고
    • An intact ribose moiety at A2602 of 23S rRNA is key to trigger peptidyl-tRNA hydrolysis during translation termination
    • Amort M, et al. (2007) An intact ribose moiety at A2602 of 23S rRNA is key to trigger peptidyl-tRNA hydrolysis during translation termination. Nucleic Acids Res 35:5130-5140.
    • (2007) Nucleic Acids Res , vol.35 , pp. 5130-5140
    • Amort, M.1
  • 32
    • 0037245660 scopus 로고    scopus 로고
    • The critical role of the universally conserved A2602 of 23S ribosomal RNA in the release of the nascent peptide during translation termination
    • Polacek N, et al. (2003) The critical role of the universally conserved A2602 of 23S ribosomal RNA in the release of the nascent peptide during translation termination. Mol Cell 11:103-112.
    • (2003) Mol Cell , vol.11 , pp. 103-112
    • Polacek, N.1
  • 33
    • 2542470615 scopus 로고    scopus 로고
    • The active site of the ribosome is composed of two layers of conserved nucleotides with distinct roles in peptide bond formation and peptide release
    • Youngman EM, Brunelle JL, Kochaniak AB, Green R (2004) The active site of the ribosome is composed of two layers of conserved nucleotides with distinct roles in peptide bond formation and peptide release. Cell 117:589-599.
    • (2004) Cell , vol.117 , pp. 589-599
    • Youngman, E.M.1    Brunelle, J.L.2    Kochaniak, A.B.3    Green, R.4
  • 34
    • 0034886313 scopus 로고    scopus 로고
    • X-ray snapshots of serine protease catalysis reveal a tetrahedral intermediate
    • Wilmouth RC, et al. (2001) X-ray snapshots of serine protease catalysis reveal a tetrahedral intermediate. Nat Struct Biol 8:689-694.
    • (2001) Nat Struct Biol , vol.8 , pp. 689-694
    • Wilmouth, R.C.1
  • 35
    • 0032717591 scopus 로고    scopus 로고
    • Bacterial biocatalysts: Molecular biology, three-dimensional structures, and biotechnological applications of lipases
    • Jaeger KE, Dijkstra BW, Reetz MT (1999) Bacterial biocatalysts: Molecular biology, three-dimensional structures, and biotechnological applications of lipases. Annu Rev Microbiol 53:315-351.
    • (1999) Annu Rev Microbiol , vol.53 , pp. 315-351
    • Jaeger, K.E.1    Dijkstra, B.W.2    Reetz, M.T.3
  • 36
    • 21844455282 scopus 로고    scopus 로고
    • Energetic and structural consequences of perturbing Gly-193 in the oxyanion hole of serine proteases
    • Bobofchak KM, Pineda AO, Mathews FS, Di Cera E (2005) Energetic and structural consequences of perturbing Gly-193 in the oxyanion hole of serine proteases. J Biol Chem 280:25644-25650.
    • (2005) J Biol Chem , vol.280 , pp. 25644-25650
    • Bobofchak, K.M.1    Pineda, A.O.2    Mathews, F.S.3    Di Cera, E.4
  • 37
    • 0034163510 scopus 로고    scopus 로고
    • GTPase mechanism and function: New insights from systematic mutational analysis of the phosphate-binding loop residue Ala30 of Rab5
    • Liang Z, Mather T, Li G (2000) GTPase mechanism and function: New insights from systematic mutational analysis of the phosphate-binding loop residue Ala30 of Rab5. Biochem J 346 (Pt 2):501-508.
    • (2000) Biochem J , vol.346 , Issue.PART 2 , pp. 501-508
    • Liang, Z.1    Mather, T.2    Li, G.3
  • 38
    • 0037462808 scopus 로고    scopus 로고
    • High resolution crystal structures of human Rab5a and five mutants with substitutions in the catalytically important phosphate-binding loop
    • Zhu G, et al. (2003) High resolution crystal structures of human Rab5a and five mutants with substitutions in the catalytically important phosphate-binding loop. J Biol Chem 278:2452-2460.
    • (2003) J Biol Chem , vol.278 , pp. 2452-2460
    • Zhu, G.1
  • 40
    • 2642699794 scopus 로고
    • Rapid and efficient site-specific mutagenesis without phenotypic selection
    • Kunkel TA (1985) Rapid and efficient site-specific mutagenesis without phenotypic selection. Proc Natl Acad Sci USA 82:488-492.
    • (1985) Proc Natl Acad Sci USA , vol.82 , pp. 488-492
    • Kunkel, T.A.1
  • 41
    • 0024334898 scopus 로고
    • Interaction of tRNA with 23S rRNA in the ribosomal A, P, and E sites
    • Moazed D, Noller HF (1989) Interaction of tRNA with 23S rRNA in the ribosomal A, P, and E sites. Cell 57:585-597.
    • (1989) Cell , vol.57 , pp. 585-597
    • Moazed, D.1    Noller, H.F.2
  • 42
    • 0022916242 scopus 로고
    • Transfer RNA shields specific nucleotides in 16S ribosomal RNA from attack by chemical probes
    • Moazed D, Noller HF (1986) Transfer RNA shields specific nucleotides in 16S ribosomal RNA from attack by chemical probes.Cell 47:985-994.
    • (1986) Cell , vol.47 , pp. 985-994
    • Moazed, D.1    Noller, H.F.2
  • 43
    • 27944442879 scopus 로고    scopus 로고
    • Involvement of 16S rRNA nucleotides G1338 and A1339 in discrimination of initiator tRNA
    • Lancaster L, Noller HF (2005) Involvement of 16S rRNA nucleotides G1338 and A1339 in discrimination of initiator tRNA.Mol Cell 20:623-632.
    • (2005) Mol Cell , vol.20 , pp. 623-632
    • Lancaster, L.1    Noller, H.F.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.