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Volumn 579, Issue 15, 2005, Pages 3207-3213

A crevice adjoining the ribosome tunnel: Hints for cotranslational folding

Author keywords

Cotranslational folding; Macrolide binding pocket; Nascent chain; Rapamycin; Ribosome; Tunnel crevice

Indexed keywords

KETOLIDE; MACROLIDE; MEMBRANE PROTEIN; POLYKETIDE; RAPAMYCIN;

EID: 20444368456     PISSN: 00145793     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.febslet.2005.03.023     Document Type: Article
Times cited : (28)

References (45)
  • 1
    • 0034637111 scopus 로고    scopus 로고
    • The complete atomic structure of the large ribosomal subunit at 2.4 Å resolution
    • N. Ban, P. Nissen, J. Hansen, P.B. Moore, and T.A. Steitz The complete atomic structure of the large ribosomal subunit at 2.4 Å resolution Science 289 2000 905 920
    • (2000) Science , vol.289 , pp. 905-920
    • Ban, N.1    Nissen, P.2    Hansen, J.3    Moore, P.B.4    Steitz, T.A.5
  • 3
    • 0028170807 scopus 로고
    • Signal sequence recognition and protein targeting to the endoplasmic reticulum membrane
    • P. Walter, and A.E. Johnson Signal sequence recognition and protein targeting to the endoplasmic reticulum membrane Annu. Rev. Cell Biol. 10 1994 87 119
    • (1994) Annu. Rev. Cell Biol. , vol.10 , pp. 87-119
    • Walter, P.1    Johnson, A.E.2
  • 4
    • 0032784010 scopus 로고    scopus 로고
    • Signal sequence recognition and protein targeting
    • R.M. Stroud, and P. Walter Signal sequence recognition and protein targeting Curr. Opin. Struct. Biol. 9 1999 754 759
    • (1999) Curr. Opin. Struct. Biol. , vol.9 , pp. 754-759
    • Stroud, R.M.1    Walter, P.2
  • 5
    • 0037040406 scopus 로고    scopus 로고
    • Regulatory nascent peptides in the ribosomal tunnel
    • T. Tenson, and M. Ehrenberg Regulatory nascent peptides in the ribosomal tunnel Cell 108 2002 591 594
    • (2002) Cell , vol.108 , pp. 591-594
    • Tenson, T.1    Ehrenberg, M.2
  • 8
    • 14544282996 scopus 로고    scopus 로고
    • The co-translational folding and interactions of nascent protein chains: A new approach using fluorescence resonance energy transfer
    • A.E. Johnson The co-translational folding and interactions of nascent protein chains: a new approach using fluorescence resonance energy transfer FEBS Lett. 579 2005 916 920
    • (2005) FEBS Lett. , vol.579 , pp. 916-920
    • Johnson, A.E.1
  • 10
    • 14544275165 scopus 로고    scopus 로고
    • From peptide-bond formation to cotranslational folding: Dynamic, regulatory and evolutionary aspects
    • D. Baram, and A. Yonath From peptide-bond formation to cotranslational folding: dynamic, regulatory and evolutionary aspects FEBS Lett. 579 2005 948 954
    • (2005) FEBS Lett. , vol.579 , pp. 948-954
    • Baram, D.1    Yonath, A.2
  • 11
    • 0037040411 scopus 로고    scopus 로고
    • The ribosomal exit tunnel functions as a discriminating gate
    • H. Nakatogawa, and K. Ito The ribosomal exit tunnel functions as a discriminating gate Cell 108 2002 629 636
    • (2002) Cell , vol.108 , pp. 629-636
    • Nakatogawa, H.1    Ito, K.2
  • 12
    • 0037072627 scopus 로고    scopus 로고
    • Instruction of translating ribosome by nascent peptide
    • F. Gong, and C. Yanofsky Instruction of translating ribosome by nascent peptide Science 297 2002 1864 1867
    • (2002) Science , vol.297 , pp. 1864-1867
    • Gong, F.1    Yanofsky, C.2
  • 19
    • 3242712966 scopus 로고    scopus 로고
    • Alterations at the peptidyl transferase centre of the ribosome induced by the synergistic action of the streptogramins dalfopristin and quinupristin
    • J. Harms, F. Schluenzen, P. Fucini, H. Bartels, and A. Yonath Alterations at the peptidyl transferase centre of the ribosome induced by the synergistic action of the streptogramins dalfopristin and quinupristin BMC Biol. 2 4 2004 1 10
    • (2004) BMC Biol. , vol.2 , Issue.4 , pp. 1-10
    • Harms, J.1    Schluenzen, F.2    Fucini, P.3    Bartels, H.4    Yonath, A.5
  • 20
    • 5644257352 scopus 로고    scopus 로고
    • Ribosomal antibiotics: Structural basis for resistance, synergism and selectivity
    • T. Auerbach, A. Bashan, and A. Yonath Ribosomal antibiotics: structural basis for resistance, synergism and selectivity Trends Biotechnol. 22 2004 570 576
    • (2004) Trends Biotechnol. , vol.22 , pp. 570-576
    • Auerbach, T.1    Bashan, A.2    Yonath, A.3
  • 21
    • 0015745765 scopus 로고
    • Biochemical and genetic studies on two different types of erythromycin resistant mutants of Escherichia coli with altered ribosomal proteins
    • H.G. Wittmann, G. Stoffler, D. Apirion, L. Rosen, K. Tanaka, M. Tamaki, R. Takata, S. Dekio, and E. Otaka Biochemical and genetic studies on two different types of erythromycin resistant mutants of Escherichia coli with altered ribosomal proteins Mol. Gen. Genet. 127 1973 175 189
    • (1973) Mol. Gen. Genet. , vol.127 , pp. 175-189
    • Wittmann, H.G.1    Stoffler, G.2    Apirion, D.3    Rosen, L.4    Tanaka, K.5    Tamaki, M.6    Takata, R.7    Dekio, S.8    Otaka, E.9
  • 22
    • 0036384268 scopus 로고    scopus 로고
    • L22 ribosomal protein and effect of its mutation on ribosome resistance to erythromycin
    • N. Davydova, V. Streltsov, M. Wilce, A. Liljas, and M. Garber L22 ribosomal protein and effect of its mutation on ribosome resistance to erythromycin J. Mol. Biol. 322 2002 635 644
    • (2002) J. Mol. Biol. , vol.322 , pp. 635-644
    • Davydova, N.1    Streltsov, V.2    Wilce, M.3    Liljas, A.4    Garber, M.5
  • 27
    • 0032915417 scopus 로고    scopus 로고
    • Regulation of ribosome biogenesis by the rapamycin-sensitive TOR-signaling pathway in Saccharomyces cerevisiae
    • T. Powers, and P. Walter Regulation of ribosome biogenesis by the rapamycin-sensitive TOR-signaling pathway in Saccharomyces cerevisiae Mol. Biol. Cell 10 1999 987 1000
    • (1999) Mol. Biol. Cell , vol.10 , pp. 987-1000
    • Powers, T.1    Walter, P.2
  • 28
    • 0031596416 scopus 로고    scopus 로고
    • Rapamycin induces the G0 program of transcriptional repression in yeast by interfering with the TOR signaling pathway
    • D. Zaragoza, A. Ghavidel, J. Heitman, and M.C. Schultz Rapamycin induces the G0 program of transcriptional repression in yeast by interfering with the TOR signaling pathway Mol. Cell. Biol. 18 1998 4463 4470
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 4463-4470
    • Zaragoza, D.1    Ghavidel, A.2    Heitman, J.3    Schultz, M.C.4
  • 29
    • 11144273952 scopus 로고    scopus 로고
    • TOR regulates ribosomal protein gene expression via PKA and the Forkhead transcription factor FHL1
    • D.E. Martin, A. Soulard, and M.N. Hall TOR regulates ribosomal protein gene expression via PKA and the Forkhead transcription factor FHL1 Cell 119 2004 969 979
    • (2004) Cell , vol.119 , pp. 969-979
    • Martin, D.E.1    Soulard, A.2    Hall, M.N.3
  • 30
    • 0345602742 scopus 로고    scopus 로고
    • Homodirectional changes in transcriptome composition and mRNA translation induced by rapamycin and heat shock
    • T. Preiss, J. Baron-Benhamou, W. Ansorge, and M.W. Hentze Homodirectional changes in transcriptome composition and mRNA translation induced by rapamycin and heat shock Nat. Struct. Biol. 10 2003 1039 1047
    • (2003) Nat. Struct. Biol. , vol.10 , pp. 1039-1047
    • Preiss, T.1    Baron-Benhamou, J.2    Ansorge, W.3    Hentze, M.W.4
  • 32
    • 0036049283 scopus 로고    scopus 로고
    • An unexpected inhibitory effect of rapamycin against germination of spores of Bacillus brevis strain Nagano
    • W.S. Kim, L. Xu, D. Souw, A. Fang, and A.L. Demain An unexpected inhibitory effect of rapamycin against germination of spores of Bacillus brevis strain Nagano J. Antibiot. 55 2002 650 654
    • (2002) J. Antibiot. , vol.55 , pp. 650-654
    • Kim, W.S.1    Xu, L.2    Souw, D.3    Fang, A.4    Demain, A.L.5
  • 33
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • C.W. Carter Jr. R.M. Sweet Academic Press London
    • Z. Otwinowski, and W. Minor Processing of X-ray diffraction data collected in oscillation mode C.W. Carter Jr. R.M. Sweet Methods in Enzymology Macromolecular Crystallography, Part A Vol. 276 1997 Academic Press London 307 326
    • (1997) Methods in Enzymology Macromolecular Crystallography, Part A , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 35
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron density maps and the location of errors in these models
    • T.A. Jones, J.Y. Zou, S.W. Cowan, and Kjeldgaard Improved methods for building protein models in electron density maps and the location of errors in these models Acta Crystallogr. A 47 1991 110 119
    • (1991) Acta Crystallogr. a , vol.47 , pp. 110-119
    • Jones, T.A.1    Zou, J.Y.2    Cowan, S.W.3    Kjeldgaard4
  • 36
    • 0028103275 scopus 로고
    • The CCP4 suite - Programs for protein crystallography
    • S. Bailey The CCP4 suite - programs for protein crystallography Acta Crystallogr. D 50 1994 760 763
    • (1994) Acta Crystallogr. D , vol.50 , pp. 760-763
    • Bailey, S.1
  • 37
  • 38
    • 0003098935 scopus 로고    scopus 로고
    • Footprinting and modification-interference analysis of binding sites on RNA
    • C.W.J. Smith Oxford University Press UK, Oxford
    • C. Merryman, and H.F. Noller Footprinting and modification-interference analysis of binding sites on RNA C.W.J. Smith RNA:Protein Interactions 1998 Oxford University Press UK, Oxford 237 253
    • (1998) RNA:Protein Interactions , pp. 237-253
    • Merryman, C.1    Noller, H.F.2
  • 40
    • 0028963496 scopus 로고
    • Erythromycin resistance by ribosome modification
    • B. Weisblum Erythromycin resistance by ribosome modification Antimicrob. Agents Chemother. 39 1995 577 585
    • (1995) Antimicrob. Agents Chemother. , vol.39 , pp. 577-585
    • Weisblum, B.1
  • 41
    • 0034763651 scopus 로고    scopus 로고
    • Structures of ketolides and macrolides determine their mode of interaction with the ribosomal target site
    • S. Douthwaite, and W.S. Champney Structures of ketolides and macrolides determine their mode of interaction with the ribosomal target site J. Antimicrob. Chemother. 48 2001 1 8
    • (2001) J. Antimicrob. Chemother. , vol.48 , pp. 1-8
    • Douthwaite, S.1    Champney, W.S.2
  • 42
    • 1542358892 scopus 로고    scopus 로고
    • Nascent membrane and secretory proteins differ in FRET-detected folding far inside the ribosome and in their exposure to ribosomal proteins
    • C.A. Woolhead, P.J. McCormick, and A.E. Johnson Nascent membrane and secretory proteins differ in FRET-detected folding far inside the ribosome and in their exposure to ribosomal proteins Cell 116 2004 725 736
    • (2004) Cell , vol.116 , pp. 725-736
    • Woolhead, C.A.1    McCormick, P.J.2    Johnson, A.E.3
  • 43
    • 17044425907 scopus 로고    scopus 로고
    • 23S rRNA base-pair 2057-2611 determines ketolide susceptibility and fitness cost of the macrolide resistance mutation 2058A → G
    • in press
    • Pfister, P., Corti, N., Hobbie, S., Bruell, C., Zarivach, R., Yonath, A. and Bottger, E.C. (2005). 23S rRNA base-pair 2057-2611 determines ketolide susceptibility and fitness cost of the macrolide resistance mutation 2058A → G. Proc. Natl. Acad. Sci. USA (in press)
    • (2005) Proc. Natl. Acad. Sci. USA
    • Pfister, P.1    Corti, N.2    Hobbie, S.3    Bruell, C.4    Zarivach, R.5    Yonath, A.6    Bottger, E.C.7
  • 45
    • 0036342198 scopus 로고    scopus 로고
    • The structures of four macrolide antibiotics bound to the large ribosomal subunit
    • J.L. Hansen, J.A. Ippolito, N. Ban, P. Nissen, P.B. Moore, and T.A. Steitz The structures of four macrolide antibiotics bound to the large ribosomal subunit Mol. Cell 10 2002 117 128
    • (2002) Mol. Cell , vol.10 , pp. 117-128
    • Hansen, J.L.1    Ippolito, J.A.2    Ban, N.3    Nissen, P.4    Moore, P.B.5    Steitz, T.A.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.