메뉴 건너뛰기




Volumn 392, Issue 3, 2009, Pages 645-656

The Genesis of Ribosome Structure: How a Protein Generates RNA Structure in Real Time

Author keywords

16S rRNA; dynamics; ribosome; RNA folding; S17

Indexed keywords

RNA 16S;

EID: 69349098384     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2009.06.056     Document Type: Article
Times cited : (8)

References (42)
  • 1
    • 0014266752 scopus 로고
    • Structure and function of E. coli ribosomes. V. Reconstitution of functionally active 30S ribosomal particles from RNA and proteins
    • Traub P., and Nomura M. Structure and function of E. coli ribosomes. V. Reconstitution of functionally active 30S ribosomal particles from RNA and proteins. Proc. Natl Acad. Sci. USA 59 (1968) 777-784
    • (1968) Proc. Natl Acad. Sci. USA , vol.59 , pp. 777-784
    • Traub, P.1    Nomura, M.2
  • 2
    • 0029100747 scopus 로고
    • A model of protein synthesis based on cryo-electron microscopy of the E. coli ribosome
    • Frank J., Zhu J., Penczek P., Li Y., Srivastava S., Verschoor A., et al. A model of protein synthesis based on cryo-electron microscopy of the E. coli ribosome. Nature 376 (1995) 441-444
    • (1995) Nature , vol.376 , pp. 441-444
    • Frank, J.1    Zhu, J.2    Penczek, P.3    Li, Y.4    Srivastava, S.5    Verschoor, A.6
  • 3
    • 0021093443 scopus 로고
    • Cross-links between ribosomal proteins of 30S subunits in 70S tight couples and in 30S subunits
    • Lambert J.M., Boileau G., Cover J.A., and Traut R.R. Cross-links between ribosomal proteins of 30S subunits in 70S tight couples and in 30S subunits. Biochemistry 22 (1983) 3913-3920
    • (1983) Biochemistry , vol.22 , pp. 3913-3920
    • Lambert, J.M.1    Boileau, G.2    Cover, J.A.3    Traut, R.R.4
  • 4
    • 0029645318 scopus 로고
    • The 70S Escherichia coli ribosome at 23 Å resolution: fitting the ribosomal RNA
    • Stark H., Mueller F., Orlova E.V., Schatz M., Dube P., Erdemir T., et al. The 70S Escherichia coli ribosome at 23 Å resolution: fitting the ribosomal RNA. Structure 3 (1995) 815-821
    • (1995) Structure , vol.3 , pp. 815-821
    • Stark, H.1    Mueller, F.2    Orlova, E.V.3    Schatz, M.4    Dube, P.5    Erdemir, T.6
  • 5
    • 0023433672 scopus 로고
    • The topography of ribosomal proteins on the surface of the 30S subunit of Escherichia coli
    • Stoffler-Meilicke M., and Stoffler G. The topography of ribosomal proteins on the surface of the 30S subunit of Escherichia coli. Biochimie 69 (1987) 1049-1064
    • (1987) Biochimie , vol.69 , pp. 1049-1064
    • Stoffler-Meilicke, M.1    Stoffler, G.2
  • 6
    • 0024344098 scopus 로고
    • RNA-protein interactions in 30S ribosomal subunits: folding and function of 16S rRNA
    • Stern S., Powers T., Changchien L.M., and Noller H.F. RNA-protein interactions in 30S ribosomal subunits: folding and function of 16S rRNA. Science 244 (1989) 783-790
    • (1989) Science , vol.244 , pp. 783-790
    • Stern, S.1    Powers, T.2    Changchien, L.M.3    Noller, H.F.4
  • 7
    • 0027171312 scopus 로고
    • Dynamics of in vitro assembly of 16S rRNA into 30S ribosomal subunits
    • Powers T., Daubresse G., and Noller H.F. Dynamics of in vitro assembly of 16S rRNA into 30S ribosomal subunits. J. Mol. Biol. 232 (1993) 362-374
    • (1993) J. Mol. Biol. , vol.232 , pp. 362-374
    • Powers, T.1    Daubresse, G.2    Noller, H.F.3
  • 8
    • 0022470564 scopus 로고
    • Rapid chemical probing of conformation in 16S ribosomal RNA and 30S ribosomal subunits using primer extension
    • Moazed D., Stern S., and Noller H.F. Rapid chemical probing of conformation in 16S ribosomal RNA and 30S ribosomal subunits using primer extension. J. Mol. Biol. 187 (1986) 399-416
    • (1986) J. Mol. Biol. , vol.187 , pp. 399-416
    • Moazed, D.1    Stern, S.2    Noller, H.F.3
  • 11
    • 0016153699 scopus 로고
    • Assembly mapping of 30S ribosomal proteins from Escherichia coli. Further studies
    • Held W.A., Ballou B., Mizushima S., and Nomura M. Assembly mapping of 30S ribosomal proteins from Escherichia coli. Further studies. J. Biol. Chem. 249 (1974) 3103-3111
    • (1974) J. Biol. Chem. , vol.249 , pp. 3103-3111
    • Held, W.A.1    Ballou, B.2    Mizushima, S.3    Nomura, M.4
  • 12
    • 0037319895 scopus 로고    scopus 로고
    • Assembly of the 30S ribosomal subunit
    • Culver G.M. Assembly of the 30S ribosomal subunit. Biopolymers 68 (2003) 234-249
    • (2003) Biopolymers , vol.68 , pp. 234-249
    • Culver, G.M.1
  • 13
    • 0019849246 scopus 로고
    • *) from the 30S ribosomal subunit of Escherichia coli
    • *) from the 30S ribosomal subunit of Escherichia coli. Biochemistry 20 (1981) 6480-6484
    • (1981) Biochemistry , vol.20 , pp. 6480-6484
    • Tam, M.F.1    Hill, W.E.2
  • 14
    • 0742322957 scopus 로고    scopus 로고
    • Mapping structural differences between 30S ribosomal subunit assembly intermediates
    • Holmes K.L., and Culver G.M. Mapping structural differences between 30S ribosomal subunit assembly intermediates. Nat. Struct. Mol. Biol. 11 (2004) 179-186
    • (2004) Nat. Struct. Mol. Biol. , vol.11 , pp. 179-186
    • Holmes, K.L.1    Culver, G.M.2
  • 15
    • 0015793219 scopus 로고
    • Rate determining step in the reconstitution of Escherichia coli 30S ribosomal subunits
    • Held W.A., and Nomura M. Rate determining step in the reconstitution of Escherichia coli 30S ribosomal subunits. Biochemistry 12 (1973) 3273-3281
    • (1973) Biochemistry , vol.12 , pp. 3273-3281
    • Held, W.A.1    Nomura, M.2
  • 16
    • 0014693477 scopus 로고
    • Structure and function of Escherichia coli ribosomes. VI. Mechanism of assembly of 30S ribosomes studied in vitro
    • Traub P., and Nomura M. Structure and function of Escherichia coli ribosomes. VI. Mechanism of assembly of 30S ribosomes studied in vitro. J. Mol. Biol. 40 (1969) 391-413
    • (1969) J. Mol. Biol. , vol.40 , pp. 391-413
    • Traub, P.1    Nomura, M.2
  • 17
    • 47649126376 scopus 로고    scopus 로고
    • Cooperativity in macromolecular assembly
    • Williamson J.R. Cooperativity in macromolecular assembly. Nat. Chem. Biol. 4 (2008) 458-465
    • (2008) Nat. Chem. Biol. , vol.4 , pp. 458-465
    • Williamson, J.R.1
  • 18
    • 33748567487 scopus 로고    scopus 로고
    • Assembly of the 30S ribosomal subunit
    • Williamson J.R. Assembly of the 30S ribosomal subunit. Q. Rev. Biophys. 38 (2005) 397-403
    • (2005) Q. Rev. Biophys. , vol.38 , pp. 397-403
    • Williamson, J.R.1
  • 19
    • 28444479853 scopus 로고    scopus 로고
    • An assembly landscape for the 30S ribosomal subunit
    • Talkington M.W., Siuzdak G., and Williamson J.R. An assembly landscape for the 30S ribosomal subunit. Nature 438 (2005) 628-632
    • (2005) Nature , vol.438 , pp. 628-632
    • Talkington, M.W.1    Siuzdak, G.2    Williamson, J.R.3
  • 20
    • 55249084867 scopus 로고    scopus 로고
    • Concurrent nucleation of 16S folding and induced fit in 30S ribosome assembly
    • Adilakshmi T., Bellur D.L., and Woodson S.A. Concurrent nucleation of 16S folding and induced fit in 30S ribosome assembly. Nature 455 (2008) 1268-1272
    • (2008) Nature , vol.455 , pp. 1268-1272
    • Adilakshmi, T.1    Bellur, D.L.2    Woodson, S.A.3
  • 21
    • 0029286628 scopus 로고
    • Hydroxyl radical footprinting of ribosomal proteins on 16S rRNA
    • Powers T., and Noller H.F. Hydroxyl radical footprinting of ribosomal proteins on 16S rRNA. RNA 1 (1995) 194-209
    • (1995) RNA , vol.1 , pp. 194-209
    • Powers, T.1    Noller, H.F.2
  • 23
    • 0033057324 scopus 로고    scopus 로고
    • Efficient reconstitution of functional Escherichia coli 30S ribosomal subunits from a complete set of recombinant small subunit ribosomal proteins
    • Culver G.M., and Noller H.F. Efficient reconstitution of functional Escherichia coli 30S ribosomal subunits from a complete set of recombinant small subunit ribosomal proteins. RNA 5 (1999) 832-843
    • (1999) RNA , vol.5 , pp. 832-843
    • Culver, G.M.1    Noller, H.F.2
  • 24
    • 0015901113 scopus 로고
    • Reconstitution of Escherichia coli 30S ribosomal subunits from purified molecular components
    • Held W.A., Mizushima S., and Nomura M. Reconstitution of Escherichia coli 30S ribosomal subunits from purified molecular components. J. Biol. Chem. 248 (1973) 5720-5730
    • (1973) J. Biol. Chem. , vol.248 , pp. 5720-5730
    • Held, W.A.1    Mizushima, S.2    Nomura, M.3
  • 25
    • 34047165788 scopus 로고    scopus 로고
    • Temperature-dependent RNP conformational rearrangements: analysis of binary complexes of primary binding proteins with 16S rRNA
    • Dutca L.M., Jagannathan I., Grondek J.F., and Culver G.M. Temperature-dependent RNP conformational rearrangements: analysis of binary complexes of primary binding proteins with 16S rRNA. J. Mol. Biol. 368 (2007) 853-869
    • (2007) J. Mol. Biol. , vol.368 , pp. 853-869
    • Dutca, L.M.1    Jagannathan, I.2    Grondek, J.F.3    Culver, G.M.4
  • 26
    • 0024292371 scopus 로고
    • Interaction of proteins S16, S17 and S20 with 16S ribosomal RNA
    • Stern S., Changchien L.M., Craven G.R., and Noller H.F. Interaction of proteins S16, S17 and S20 with 16S ribosomal RNA. J. Mol. Biol. 200 (1988) 291-299
    • (1988) J. Mol. Biol. , vol.200 , pp. 291-299
    • Stern, S.1    Changchien, L.M.2    Craven, G.R.3    Noller, H.F.4
  • 27
    • 0024293439 scopus 로고
    • Model for the three-dimensional folding of 16S ribosomal RNA
    • Stern S., Weiser B., and Noller H.F. Model for the three-dimensional folding of 16S ribosomal RNA. J. Mol. Biol. 204 (1988) 447-481
    • (1988) J. Mol. Biol. , vol.204 , pp. 447-481
    • Stern, S.1    Weiser, B.2    Noller, H.F.3
  • 28
    • 27644536231 scopus 로고    scopus 로고
    • Analysis of conformational changes in 16S rRNA during the course of 30S subunit assembly
    • Holmes K.L., and Culver G.M. Analysis of conformational changes in 16S rRNA during the course of 30S subunit assembly. J. Mol. Biol. 354 (2005) 340-357
    • (2005) J. Mol. Biol. , vol.354 , pp. 340-357
    • Holmes, K.L.1    Culver, G.M.2
  • 29
    • 0024241761 scopus 로고
    • Structural analysis of RNA using chemical and enzymatic probing monitored by primer extension
    • Stern S., Moazed D., and Noller H.F. Structural analysis of RNA using chemical and enzymatic probing monitored by primer extension. Methods Enzymol. 164 (1988) 481-489
    • (1988) Methods Enzymol. , vol.164 , pp. 481-489
    • Stern, S.1    Moazed, D.2    Noller, H.F.3
  • 30
    • 0021771036 scopus 로고
    • Chemical probing of conformation in large RNA molecules. Analysis of 16S ribosomal RNA using diethylpyrocarbonate
    • Van Stolk B.J., and Noller H.F. Chemical probing of conformation in large RNA molecules. Analysis of 16S ribosomal RNA using diethylpyrocarbonate. J. Mol. Biol. 180 (1984) 151-177
    • (1984) J. Mol. Biol. , vol.180 , pp. 151-177
    • Van Stolk, B.J.1    Noller, H.F.2
  • 31
    • 2942571539 scopus 로고    scopus 로고
    • The Comparative RNA Web (CRW) Site: an online database of comparative sequence and structure information for ribosomal, intron, and other RNAs
    • Cannone J.J., S. S., Schnare M.N., Collett J.R., D'Souza L.M., Du Y., et al. The Comparative RNA Web (CRW) Site: an online database of comparative sequence and structure information for ribosomal, intron, and other RNAs. BMC Bioinformatics 3 (2002) 15
    • (2002) BMC Bioinformatics , vol.3 , pp. 15
    • Cannone, J.J.1    S., S.2    Schnare, M.N.3    Collett, J.R.4    D'Souza, L.M.5    Du, Y.6
  • 32
    • 0021012648 scopus 로고
    • Detailed analysis of the higher-order structure of 16S-like ribosomal ribonucleic acids
    • Woese C.R., Gutell R., Gupta R., and Noller H.F. Detailed analysis of the higher-order structure of 16S-like ribosomal ribonucleic acids. Microbiol. Rev. 47 (1983) 621-669
    • (1983) Microbiol. Rev. , vol.47 , pp. 621-669
    • Woese, C.R.1    Gutell, R.2    Gupta, R.3    Noller, H.F.4
  • 33
    • 0029915450 scopus 로고    scopus 로고
    • Solution structure of prokaryotic ribosomal protein S17 by high-resolution NMR spectroscopy
    • Jaishree T.N., Ramakrishnan V., and White S.W. Solution structure of prokaryotic ribosomal protein S17 by high-resolution NMR spectroscopy. Biochemistry 35 (1996) 2845-2853
    • (1996) Biochemistry , vol.35 , pp. 2845-2853
    • Jaishree, T.N.1    Ramakrishnan, V.2    White, S.W.3
  • 34
    • 0035423087 scopus 로고    scopus 로고
    • The kink-turn: a new RNA secondary structure motif
    • Klein D.J., Schmeing T.M., Moore P.B., and Steitz T.A. The kink-turn: a new RNA secondary structure motif. EMBO J. 20 (2001) 4214-4221
    • (2001) EMBO J. , vol.20 , pp. 4214-4221
    • Klein, D.J.1    Schmeing, T.M.2    Moore, P.B.3    Steitz, T.A.4
  • 35
    • 0025737972 scopus 로고
    • A functional pseudoknot in 16S ribosomal RNA
    • Powers T., and Noller H.F. A functional pseudoknot in 16S ribosomal RNA. EMBO J. 10 (1991) 2203-2214
    • (1991) EMBO J. , vol.10 , pp. 2203-2214
    • Powers, T.1    Noller, H.F.2
  • 36
    • 0027246623 scopus 로고
    • Formation of the central pseudoknot in 16S rRNA is essential for initiation of translation
    • Brink M.F., Verbeet M.P., and de Boer H.A. Formation of the central pseudoknot in 16S rRNA is essential for initiation of translation. EMBO J. 12 (1993) 3987-3996
    • (1993) EMBO J. , vol.12 , pp. 3987-3996
    • Brink, M.F.1    Verbeet, M.P.2    de Boer, H.A.3
  • 37
    • 84886628776 scopus 로고
    • Alteration of ribosomal protein S17 by mutation linked to neamine resistance in Escherichia coli. II. Localization of the amino acid replacement in protein S17 from a meaA mutant
    • Yaguchi M., Wittmann H.G., Cabezon T., DeWilde M., Villarroel R., Herzog A., and Bollen A. Alteration of ribosomal protein S17 by mutation linked to neamine resistance in Escherichia coli. II. Localization of the amino acid replacement in protein S17 from a meaA mutant. J. Mol. Biol. 104 (1976) 617-620
    • (1976) J. Mol. Biol. , vol.104 , pp. 617-620
    • Yaguchi, M.1    Wittmann, H.G.2    Cabezon, T.3    DeWilde, M.4    Villarroel, R.5    Herzog, A.6    Bollen, A.7
  • 38
    • 0018096054 scopus 로고
    • Resistance to the aminoglycoside antibiotic neamine in Escherichia coli. A new mutant whose NeaR phenotype results from the cumulative effects of two distinct mutations
    • Delcuve G., Cabezon T., Herzog A., Cannon M., and Bollen A. Resistance to the aminoglycoside antibiotic neamine in Escherichia coli. A new mutant whose NeaR phenotype results from the cumulative effects of two distinct mutations. Biochem. J. 174 (1978) 1-7
    • (1978) Biochem. J. , vol.174 , pp. 1-7
    • Delcuve, G.1    Cabezon, T.2    Herzog, A.3    Cannon, M.4    Bollen, A.5
  • 39
    • 0017275724 scopus 로고
    • Cooperative control of translational fidelity by ribosomal proteins in Escherichia coli. III. A ram mutation in the structural gene for protein S5 (rpx E)
    • Cabezon T., Herzog A., De Wilde M., Villarroel R., and Bollen A. Cooperative control of translational fidelity by ribosomal proteins in Escherichia coli. III. A ram mutation in the structural gene for protein S5 (rpx E). Mol. Gen. Genet. 144 (1976) 59-62
    • (1976) Mol. Gen. Genet. , vol.144 , pp. 59-62
    • Cabezon, T.1    Herzog, A.2    De Wilde, M.3    Villarroel, R.4    Bollen, A.5
  • 41
    • 0018289986 scopus 로고
    • A missense mutation in the gene coding for ribosomal protein S17 (rpsQ) leading to ribosomal assembly defectivity in Escherichia coli
    • Herzog A., Yaguchi M., Cabezon T., Corchuelo M.C., Petre J., and Bollen A. A missense mutation in the gene coding for ribosomal protein S17 (rpsQ) leading to ribosomal assembly defectivity in Escherichia coli. Mol. Gen. Genet. 171 (1979) 15-22
    • (1979) Mol. Gen. Genet. , vol.171 , pp. 15-22
    • Herzog, A.1    Yaguchi, M.2    Cabezon, T.3    Corchuelo, M.C.4    Petre, J.5    Bollen, A.6
  • 42
    • 16344379726 scopus 로고    scopus 로고
    • Ribosome builder: a software project to simulate the ribosome
    • Knight W., Hill W., and Lodmell J.S. Ribosome builder: a software project to simulate the ribosome. Comput. Biol. Chem. 29 (2005) 163-174
    • (2005) Comput. Biol. Chem. , vol.29 , pp. 163-174
    • Knight, W.1    Hill, W.2    Lodmell, J.S.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.